-- dump date 20140620_032625 -- class Genbank::CDS -- table cds_note -- id note NP_945357.1 binds to the dnaA-box as an ATP-bound complex at the origin of replication during the initiation of chromosomal replication; can also affect transcription of multiple genes including itself. NP_945358.1 binds the polymerase to DNA and acts as a sliding clamp NP_945359.1 Required for DNA replication; binds preferentially to single-stranded, linear DNA NP_945360.1 negatively supercoils closed circular double-stranded DNA NP_945361.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945364.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945365.1 acts as a promotor non-specific transcription repressor NP_945366.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945372.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945374.1 CcoO; FixO NP_945375.1 CcoN; FixN NP_945376.1 catalyzes the formation of 2-dehydropantoate from (R)-pantoate NP_945379.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945383.1 catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphate, phenylalanine sensitive NP_945384.1 involved in de novo purine biosynthesis NP_945386.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945390.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945391.1 catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily NP_945393.1 catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 1 subfamily NP_945394.1 binds directly to 23S ribosomal RNA prior to in vitro assembly of the 50S ribosomal subunit NP_945395.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945396.1 IF-3 has several functions that are required and promote translation initiation including; preventing association of 70S by binding to 30S; monitoring codon-anticodon interactions by promoting disassociation of fMet-tRNA(fMet) from initiation complexes formed on leaderless mRNAs or incorrectly bound noninitiatior tRNAs and complexes with noncanonical start sites; stimulates codon-anticodon interactions at P-site; involved in moving mRNA to the P-site; and in recycling subunits NP_945397.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945400.1 BacA; phosphatase activity in Escherichia coli not kinase; involved in bacitracin resistance as bacitracin supposedly sequesters undecaprenyl disphosphate which reduces the pool of lipid carrier available to the cell NP_945401.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945402.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945405.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945406.1 sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; sigma 54 factor is responsible for the expression of enzymes involved in nitrogen assimilation and metabolism; the rhizobia often have 2 copies of this sigma factor; in Rhizobium etli RpoN1 shown to be involved in the assimilation of several nitrogen and carbon sources during free-living aerobic growth and RpoN2 is involved in symbiotic nitrogen fixation; in Bradyrhizobium both RpoN1 and N2 are functional in free-living and symbiotic conditions, rpoN1 gene was regulated in response to oxygen NP_945407.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945411.1 part of the UgpABCE glycerol-3-phosphate uptake system NP_945414.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945415.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945416.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945417.1 catalyzes the formation of 5-O-(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate and 3-phosphoshikimate in tryptophan biosynthesis NP_945418.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945419.1 Catalyzes the formation of (d)CDP from ATP and (d)CMP NP_945420.1 in Escherichia coli this protein is involved in binding to the leader sequence of mRNAs and is itself bound to the 30S subunit; autoregulates expression via a C-terminal domain; in most gram negative organisms this protein is composed of 6 repeats of the S1 domain while in gram positive there are 4 repeats; the S1 nucleic acid-binding domain is found associated with other proteins NP_945421.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945422.1 This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control NP_945423.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945424.1 catalyzes the formation of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate from N-(5-phospho-beta-D-ribosyl)-anthranilate in tryptophan biosynthesis NP_945425.1 catalyzes the formation of L-tryptophan from L-serine and 1-(indol-3-yl)glycerol 3-phosphate NP_945426.1 catalyzes the formation of indole and glyceraldehyde 3-phosphate from indoleglycerol phosphate in tryptophan biosynthesis NP_945427.1 catalyzes the carboxylation of acetyl-CoA to malonyl-CoA; forms a tetramer of AccA2D2 subunits NP_945429.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945432.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945434.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945436.1 catalyzes the formation of dUMP from dUTP NP_945437.2 catalyzes the conjugation of cysteine to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, which is then decarboxylated to form 4'-phosphopantotheine; in the alphaproteobacteria, this protein contains an N-terminal SbtC-like domain NP_945438.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945439.1 Catalyzes the carbon methylation reaction in the biosynthesis of ubiquinone NP_945440.1 Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases NP_945441.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945444.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945445.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945458.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945462.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945464.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945475.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945489.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945490.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945492.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945496.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945498.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945510.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945511.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945512.1 involved in the peptidyltransferase reaction during translation NP_945515.1 essential GTPase; exhibits high exchange rate for GTP/GDP; associates with 50S ribosomal subunit; involved in regulation of chromosomal replication NP_945516.1 catalyzes the formation of glutamate 5-phosphate from glutamate in proline biosynthesis NP_945517.1 Catalyzes the phosphorylation of L-glutamate during the proline biosynthesis pathway NP_945518.1 transfers an adenyl group from ATP to NaMN to form nicotinic acid adenine dinucleotide (NaAD) which is then converted to the ubiquitous compound NAD by NAD synthetase; essential enzyme in bacteria NP_945520.1 SPOUT methyltransferase family protein; crystal structure shows homodimer; in Escherichia coli this protein methylates pseudouridine at position 1915 of the 23S ribosomal RNA NP_945522.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945524.1 hydrolyzes diadenosine polyphosphate NP_945527.1 hydrolyzes diadenosine polyphosphate NP_945528.1 produces ATP from ADP in the presence of a proton gradient across the membrane; the epsilon subunit is part of the catalytic core of the ATP synthase complex NP_945529.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. The beta chain is a regulatory subunit NP_945530.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is a regulatory subunit NP_945531.1 produces ATP from ADP in the presence of a proton gradient across the membrane; the alpha chain is a catalytic subunit NP_945532.1 Produces ATP from ADP in the presence of a proton gradient across the membrane; the delta subunit is part of the catalytic core of the ATP synthase complex NP_945534.1 binding of PriA to forked DNA starts the assembly of the primosome, also possesses 3'-5' helicase activity NP_945535.1 site-specific tyrosine recombinase which cuts and rejoins DNA molecules; binds cooperatively to specific DNA consensus sites; forms a heterotetrameric complex with XerC; XerCD exhibit similar sequences; essential to convert chromosome dimers to monomers during cell division and functions during plasmid segregation; cell division protein FtsK may regulate the XerCD complex; enzyme from Streptococcus group has unusual active site motifs NP_945536.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945538.1 Catalyzes the oxidation of dihydrolipoamide to lipoamide NP_945539.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945541.1 component of 2-oxoglutarate dehydrogenase complex; catalyzes the transfer of succinyl coenzyme A to form succinyl CoA as part of the conversion of 2-oxoglutarate to succinyl-CoA NP_945542.1 SucA; E1 component of the oxoglutarate dehydrogenase complex which catalyzes the formation of succinyl-CoA from 2-oxoglutarate; SucA catalyzes the reaction of 2-oxoglutarate with dihydrolipoamide succinyltransferase-lipoate to form dihydrolipoamide succinyltransferase-succinyldihydrolipoate and carbon dioxide NP_945543.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945544.1 catalyzes the interconversion of succinyl-CoA and succinate NP_945545.1 Catalyzes the reversible oxidation of malate to oxaloacetate NP_945546.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945549.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945555.1 Catalyzes the conversion of citrate to isocitrate NP_945556.1 ATP-binding protein; required for proper cytochrome c maturation NP_945559.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945560.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945561.1 Involved in cell division; probably involved in intracellular septation NP_945562.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945564.1 Acs; catalyzes the conversion of acetate and CoA to acetyl-CoA NP_945566.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945568.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945569.1 part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase NP_945570.1 part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol NP_945574.1 catalyzes the formation of malonyl-CoA from malonate and CoA NP_945575.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945578.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945580.1 catalyzes the oxidation of 3-isopropylmalate to 3-carboxy-4-methyl-2-oxopentanoate in leucine biosynthesis NP_945581.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945583.1 catalyzes the formation of 4-aspartyl phosphate from aspartate 4-semialdehyde NP_945585.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945586.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945588.1 catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate in leucine biosynthesis; forms a heterodimer of LeuC/D NP_945589.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945593.1 dehydratase component, catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate NP_945594.1 this protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site NP_945595.1 methylates guanosine-37 in various tRNAs; uses S-adenosyl-L-methionine to transfer methyl group to tRNA NP_945596.1 Essential for efficient processing of 16S rRNA NP_945597.1 binds to lower part of 30S body where it stabilizes two domains; required for efficient assembly of 30S; in Escherichia coli this protein has nuclease activity NP_945598.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945601.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945603.1 involved in lysine biosynthesis; DAP epimerase; produces DL-diaminopimelate from LL-diaminopimelate NP_945606.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945607.1 catalyzes the NAD(P)H-dependent reduction of glycerol 3-phosphate to glycerone phosphate NP_945608.1 in most organisms, only the N-terminal domain is present in a single polypeptide; in some archaea this domain is fused to a kinase domain; this gene is essential for growth in Escherichia coli and Bacillus subtilis; the secreted glycoprotease from Pasteurella haemolytica showed specificity for O-sialoglycosylated proteins; the Pyrococcus structure shows DNA-binding properties, iron-binding, ATP-binding, and AP endonuclease activity NP_945609.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945610.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945611.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945612.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945614.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945615.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945620.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945621.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945622.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945623.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945624.1 Citation: Kuveret et al. (1995) J. Arch. Microbiol. 164:337-345 NP_945625.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945627.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945628.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945633.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945636.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945640.1 leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase NP_945641.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945642.1 required for the assembly and function of the DNAX complex which are required for the assembly of the beta subunit onto primed DNA NP_945644.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945645.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945646.1 glucose-inhibited division protein B; SAM-dependent methyltransferase; methylates the N7 position of guanosine in position 527 of 16S rRNA NP_945647.1 GidA; glucose-inhibited cell division protein A; involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U) of the wobble uridine base in some tRNAs NP_945648.1 in Escherichia coli this protein is involved in the biosynthesis of the hypermodified nucleoside 5-methylaminomethyl-2-thiouridine, which is found in the wobble position of some tRNAs and affects ribosomal frameshifting; shows potassium-dependent dimerization and GTP hydrolysis; also involved in regulation of glutamate-dependent acid resistance and activation of gadE NP_945649.1 An RNA-DNA helicase that actively releases nascent mRNAs from paused transcription complexes NP_945653.1 catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; involved in coenzyme A biosynthesis NP_945655.1 molecular chaperone that is required for the normal export of envelope proteins out of the cell cytoplasm; in Escherichia coli this proteins forms a homotetramer in the cytoplasm and delivers proteins to be exported to SecA NP_945656.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945659.1 heat shock protein involved in degradation of misfolded proteins NP_945661.1 heat shock protein involved in degradation of misfolded proteins NP_945662.1 catalyzes the dehydration of D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate to 3-(imidazol-4-yl)-2-oxopropyl phosphate in histidine biosynthesis NP_945664.1 with HisF IGPS catalyzes the conversion of phosphoribulosyl-formimino-5-aminoimidazole-4-carboxamide ribonucleotide phosphate and glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamide ribonucleotide, and glutamate in histidine biosynthesis; the HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of imidazole-glycerol phosphate and 5-aminoimidazol-4-carboxamide ribonucleotide NP_945665.1 catalyzes the formation of 5-(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino-l- (5-phosphoribosyl)imidazole-4-carboxamide from 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide NP_945666.1 catalyzes the conversion of 5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]- 1-(5-phosphoribosyl)imidazole-4-carboxamideand glutamine to imidazole-glycerol phosphate, 5-aminoimidazol-4-carboxamideribonucleotide and glutamate; the HisF subunit acts as a cyclase NP_945667.1 catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribolsyl)-ATP in histidine biosynthesis NP_945668.1 catalyzes the formation of (R)-4'-phosphopantothenate in coenzyme A biosynthesis NP_945675.1 catalyzes the second step in the glutathione biosynthesis pathway, where it synthesizes ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione NP_945678.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945680.1 catalyzes the oxygen-independent formation of protoporphyrinogen-IX from coproporphyrinogen-III NP_945681.1 HAM1-like protein; Rec-dependent growth; RgdB; yggV; it is suspected that this protein functions to remove misincorporated bases such as xanthine or hypoxanthine NP_945682.1 RNase PH; tRNA nucleotidyltransferase; forms hexamers in Bacillus subtilis; phosphoroltic 3'-5' exoribonuclease; involved in maturation of tRNA precursors and removes terminal nucleotides near CCA acceptor arms of mature tRNAs NP_945683.1 Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons NP_945684.1 with DnaK and DnaJ acts in response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins; may act as a thermosensor NP_945685.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945686.1 heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria NP_945687.1 chaperone Hsp40; co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, dnaK-independent fashion NP_945690.1 OMP decarboxylase; OMPDCase; OMPdecase; type 1 subfamily; involved in last step of pyrimidine biosynthesis; converts orotidine 5'-phosphate to UMP and carbon dioxide; OMP decarboxylase; OMPDCase; OMPdecase NP_945691.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945692.1 catalyzes the reduction of 2,3-dihydrodipicolinate to 2,3,4,5-tetrahydrodipicolinate in lysine and diaminopimelate biosynthesis NP_945693.1 catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate NP_945697.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945699.1 role in sulfur assimilation NP_945700.1 catalyzes the phosphorylation/dephosphorylation of the enzyme isocitrate dehydrogenase on a specific serine which regulates activity; unphosphorylated IDH is fully active when cells are grown on glucose while the enzyme becomes phosphorylated and inactive in the presence of acetate or ethanol NP_945701.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945705.1 binds to the ribosome on the universally-conserved alpha-sarcin loop NP_945708.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945711.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945712.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945713.1 PEP carboxykinase; PEP carboxylase; PEPCK; catalyzes the phosphorylation and decarboxylation of oxaloacetate to form phosphoenolpyruvate using ATP NP_945714.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945719.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945720.1 binds with the catalytic core of RNA polymerase to produce the holoenzyme; this sigma factor is responsible for the expression of heat shock promoters NP_945725.1 CTG start codon NP_945730.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945732.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945733.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945734.1 catalyzes the formation of ADP-glucose and diphosphate from ATP and alpha-D-glucose 1-phosphate NP_945735.1 catalyzes the formation of alpha-1,4-glucan chains from ADP-glucose NP_945736.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_945738.1 Involved in DNA double-strand break repair and recombination. Promotes the annealing of complementary single-stranded DNA and by simulation of RAD51 recombinase NP_945741.1 the Vibrio parahaemolyticus gene VP2867 was found to be a potassium/proton antiporter; can rapidly extrude potassium against a potassium gradient at alkaline pH when cloned and expressed in Escherichia coli NP_945742.1 D-alanyl-D-alanine endopeptidase; functions in hydrolyzing cell wall peptidoglycan; similar to LAS metallopeptidases; forms a dimer in periplasm NP_945745.1 catalyzes the formation of arginosuccinate from citrulline and aspartate in arginine biosynthesis NP_945750.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945753.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945757.1 4-alpha-hydroxytetrahydrobiopterin dehydratase activity; catalyzes the formation of (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7, 8-dihydro-6H-pterin from (6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7, 8-tetrahydro-4a-hydroxypterin; functions in recycling tetrahydrobiopterin (BH4) in phenylalanine hydroxylase reaction NP_945761.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945764.1 catalyzes the hydrolysis of pyrophosphate to phosphate NP_945766.1 catalyzes the formation of 5,10-methenyltetrahydrofolate from 5,10-methylenetetrahydrofolate and subsequent formation of 10-formyltetrahydrofolate from 5,10-methenyltetrahydrofolate NP_945769.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_945771.1 Catalyzes the transfer of the ammonia group from glutamine to a new carbon-nitrogen group NP_945772.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945775.1 Involved in the metabolism of aromatic amino acids NP_945777.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945778.1 catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to 2,3-decenoyl-ACP or 3,4-decenoyl-ACP NP_945779.1 FabB, beta-Ketoacyl-ACP synthase I, KASI; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP NP_945780.1 Catalyzes a key regulatory step in fatty acid biosynthesis NP_945782.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945784.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945785.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945786.1 primary rRNA binding protein; helps nucleate assembly of 30S; binds directly to the 16S rRNA and an intersubunit bridge to the 23S rRNA; autoregulates translation through interactions with the mRNA leader sequence NP_945787.1 catalyzes isomerization of specific uridines in RNA to pseudouridine; responsible for residues in T loops of many tRNAs NP_945788.1 associates with free 30S ribosomal subunits; essential for efficient processing of 16S rRNA; in Escherichia coli rbfA is induced by cold shock NP_945789.1 Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits during initiation of protein synthesis. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex NP_945791.1 modifies transcription through interactions with RNA polymerase affecting elongation, readthrough, termination, and antitermination NP_945792.1 in Streptococcus pneumoniae this gene was found to be essential; structure determination of the Streptococcus protein shows that it is similar to a number of other proteins NP_945795.1 tRNA (guanine-N(7)-)-methyltransferase; catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA by transferring the methyl residue from S-adenosyl-L-methionine NP_945796.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945797.1 Transfers the fatty acyl group on membrane lipoproteins NP_945800.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945801.1 catalyzes the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine from N6-(dimethylallyl)adenosine (i(6)A) NP_945803.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945806.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945808.1 catalyzes a two-step reaction, first charging a tryptophan molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA NP_945810.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945811.1 activates fatty acids by binding to coenzyme A NP_945813.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945814.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945815.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_945818.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945820.1 Catalyzes the reduction of hydroxypyruvate to form D-glycerate, using NADH as an electron donor NP_945827.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945828.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945832.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945833.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945835.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945836.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945837.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_945838.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945841.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945842.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945844.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945846.1 required for 70S ribosome assembly NP_945849.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945851.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945854.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945856.1 catalyzes the formation of 3-dehydroquinate from 3-deoxy-arabino-heptulonate 7-phosphate; functions in aromatic amino acid biosynthesis NP_945857.1 catalyzes the formation of shikimate 3-phosphate from shikimate in aromatic amino acid biosynthesis NP_945861.1 catalyzes the carboxylation of acetyl-CoA to malonyl-CoA; forms a tetramer composed of two alpha (AccA) and two beta (AccD) subunits; one of the two catalytic subunits that can form the acetyl CoA carboxylase enzyme together with a carrier protein NP_945863.1 functions in protein export; can interact with acidic membrane phospholipids and the SecYEG protein complex; binds to preproteins; binds to ATP and undergoes a conformational change to promote membrane insertion of SecA/bound preprotein; ATP hydrolysis appears to drive release of the preprotein from SecA and deinsertion of SecA from the membrane; additional proteins SecD/F/YajC aid SecA recycling; exists in an equilibrium between monomers and dimers; may possibly form higher order oligomers; proteins in this cluster correspond SecA1; SecA2 is not essential and seems to play a role in secretion of a subset of proteins NP_945864.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945865.1 This protein performs the mismatch recognition step during the DNA repair process NP_945866.1 catalyzes the thiolytic cleavage of beta-ketoadipyl-CoA to succinate and acetyl-CoA NP_945872.1 catalyzes the conversion of 2C-methyl-D-erythritol 2,4-cyclodiphosphate into 4-hydroxy-3-methyl-2-en-1-yl diphosphate; involved in isoprenoid synthesis NP_945877.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945878.1 glycosyltransferase; polymerizes glycan strands in the peptidoglycan NP_945879.1 some L32 proteins have zinc finger motifs consisting of CXXC while others do not NP_945882.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945883.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945884.1 Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; in Rhizobia and Ralstonia is involved in PHB biosynthesis NP_945885.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945891.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945893.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945896.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945903.1 Member of the extracytoplasmic function sigma factors which are active under specific conditions; binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription; this sigma factor is involved in heat shock and oxidative stress response NP_945905.1 involved in the transport of C4-dicarboxylates across the membrane NP_945907.1 catalyzes the formation of glyoxylate from (S)-ureidoglycolate NP_945910.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945911.1 catalyzes the formation of (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate and L-aspartate in purine biosynthesis; SAICAR synthase NP_945912.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945913.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945915.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945919.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945921.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945924.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945926.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945928.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945931.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945933.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945935.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945936.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945937.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945943.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945944.1 catalyzes the uridylylation or deuridylylation of the PII nitrogen regulatory protein NP_945945.1 bifunctional arginine biosynthesis protein ArgJ; functions at the 1st and 5th steps in arginine biosynthesis; involved in synthesis of acetylglutamate from glutamate and acetyl-CoA and ornithine by transacetylation between acetylornithine and glutmate NP_945951.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945952.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945956.1 Involved in ubiquinone biosynthesis NP_945957.1 catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP, in Bacillus, lysine sensitive; regulated by response to starvation. NP_945958.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945959.1 recognizes the termination signals UAG and UAA during protein translation a specificity which is dependent on amino acid residues residing in loops of the L-shaped tRNA-like molecule of RF1; this protein is similar to release factor 2 NP_945961.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945963.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945965.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945967.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945968.1 catalyzes the DNA-template-directed extension of the 3'-end of a DNA strand; the tau chain serves as a scaffold to help in the dimerizaton of the alpha,epsilon and theta core complex; the gamma chain seems to interact with the delta and delta' subunits to transfer the beta subunit on the DNA NP_945969.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945970.1 involved in a recombinational process of DNA repair, independent of the recBC complex NP_945971.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_945972.1 E. coli beta lactamase (AmpC) regulator NP_945974.1 cleaves off formyl group from N-terminal methionine residues of newly synthesized proteins; binds iron(2+) NP_945975.1 modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet) which is important in translation initiation; inactivation of this gene in Escherichia coli severely impairs growth NP_945976.1 mediates pseudouridylation (positions 38, 39, 40) at the tRNA anticodon region which contributes to the structural stability NP_945977.1 dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE), catalyzes the hydrolysis of N-succinyl-L,Ldiaminopimelate L,L-SDAP to L,L-diaminopimelate and succinate. It is a metalloprotease containing dinuclear active sites. Its structure is similar to the carboxypeptidase G2 from Pseudomonas sp. strain RS-16 and the aminopeptidase from Aeromonas proteolytica. NP_945979.1 catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway NP_945982.1 catalyzes the phosphorylation of N-acetyl-L-glutamate to form N-acetyl-L-glutamate 5-phosphate NP_945984.1 binds guanine nucleotides; in Escherichia coli depletion results in defective cell division and filamentation; in Bacillus subtilis this gene is essential NP_945985.1 functions to insert inner membrane proteins into the IM in Escherichia coli; interacts with transmembrane segments; functions in both Sec-dependent and -independent membrane insertion; similar to Oxa1p in mitochondria NP_945987.1 in Escherichia coli transcription of this gene is enhanced by polyamines NP_945992.1 Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription NP_945998.1 the hook connects flagellar basal body to the flagellar filament NP_946002.1 with FlgK acts as a hook filament junction protein to join the flagellar filament to the hook NP_946003.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946004.1 AliA; in Rhodopseudomonas palustris, this enzyme was found to act on 3-chlorobenzoate and allows the organism to grow on this substrate NP_946006.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946007.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946014.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946021.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946025.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946029.1 cleaves the ring of 2,3-dihydro-2,3-dihydroxybenzoyl-CoA forming 6-hydroxy-3-hexenoyl-CoA NP_946031.2 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946034.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946042.1 E. coli PhnM, HisM-like integral membrane protein NP_946055.1 E. coli PhnM, HisM-like integral membrane protein NP_946062.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946066.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946068.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946069.1 with CobST catalyzes the formation of cobyrinic acid a,c-diamide from hydrogenobyrinic acid a,c-diamide in an ATP-dependent manner; involved in porphyrin and chlorophyll metabolism; vitamin B12 metabolism NP_946070.1 catalyzes the formation of adenosylcob(III)yrinic acid a,c-diamide from cob(I)yrinic acid a,c-diamide NP_946071.1 catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation NP_946073.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946075.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946078.1 E. coli sugE is a multicopy suppressor of groEL mutations. This gene cannot encode the long form of the protein (sugEL). NP_946081.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946085.1 catalyzes the oxidation of formate to carbon dioxide and hydrogen using NAD or NADP as the acceptor NP_946088.1 involved in the production or activity of formate dehydrogenase-H which is active when nitrate is not present during anaerobic growth NP_946091.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946094.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946096.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946099.1 Shewanella putrefaciens homolog is involved in metal reduction. Homology is only in C-terminal 60% of predicted protein. NP_946100.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946103.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946104.1 catalyzes the reduction of 3'-phosphoadenylyl sulfate into sulfite NP_946105.1 with CysN catalyzes the formation of adenylylsulfate from sulfate and ATP NP_946106.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946114.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946129.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946135.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946137.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946138.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946140.1 metalloprotease NP_946144.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946147.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946148.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946149.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946150.1 catalyzes the conversion of dihydroorotate to orotate in the pyrimidine biosynthesis pathway; uses a flavin nucleotide as an essential cofactor; class 2 enzymes are monomeric and compared to the class 1 class 2 possess an extended N terminus, which plays a role in the membrane association of the enzyme and provides the binding site for the respiratory quinones that serve as physiological electron acceptors NP_946155.1 catalyzes the ATP-dependent formation of a phosphodiester at the site of a single strand break in duplex DNA NP_946158.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946159.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946167.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946169.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946170.1 Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation NP_946171.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946173.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946178.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946183.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946184.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946186.1 converts protoheme IX and farnesyl diphosphate to heme O NP_946188.1 involved in the insertion of copper into subunit I of cytochrome C oxidase NP_946192.2 catalyzes the formation of L-threonine from O-phospho-L-homoserine NP_946193.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946195.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946196.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946197.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946198.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit C is part of the membrane proton channel F0 NP_946199.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit A is part of the membrane proton channel F0 NP_946201.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946205.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946206.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946207.1 catalyzes the formation of 5-aminolevulinate from succinyl-CoA and glycine NP_946209.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946210.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946213.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946214.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946215.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946218.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946219.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946220.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946225.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946226.1 68% identity to Bradyrhizobium japonicum bll7755 NP_946228.1 protoheme ferro-lyase; catalyzes the insertion of a ferrous ion into protoporphyrin IX to form protoheme; involved in protoheme biosynthesis; in some organisms this protein is membrane-associated while in others it is cytosolic NP_946229.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946232.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946237.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946240.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946241.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946242.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946244.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946245.1 glutamate synthase is composed of subunits alpha and beta; beta subunit is a flavin adenine dinucleotide-NADPH dependent oxidoreductase; provides electrons to the alpha subunit, which binds L-glutamine and 2-oxoglutarate and forms L-glutamate NP_946248.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946251.1 catalyzes the formation of dihydrodipicolinate from L-aspartate 4-semialdehyde and pyruvate in lysine and diaminopimelate biosynthesis NP_946257.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946260.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946262.1 stationary phase protein that binds TrpR repressor NP_946265.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946267.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946268.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946269.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946271.1 RpmE; there appears to be two types of ribosomal proteins L31 in bacterial genomes; some contain a CxxC motif while others do not; Bacillus subtilis has both types; the proteins in this cluster do not have the CXXC motif; RpmE is found in exponentially growing Bacilli while YtiA was found after exponential growth; expression of ytiA is controlled by a zinc-specific transcriptional repressor; RpmE contains one zinc ion and a CxxC motif is responsible for this binding; forms an RNP particle along with proteins L5, L18, and L25 and 5S rRNA; found crosslinked to L2 and L25 and EF-G; may be near the peptidyltransferase site of the 50S ribosome NP_946272.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946284.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946285.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946286.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946287.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946290.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946291.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946292.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946293.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946296.1 Converts 3-phospho-D-glycerate to 3-phospho-D-glyceroyl phosphate during the glycolysis pathway NP_946297.1 catalyzes the formation of 3-phospho-D-glyceroyl phosphate from D-glyceraldehyde 3-phosphate NP_946298.1 catalyzes the formation of ribose 5-phosphate and xylulose 5-phosphate from sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate; can transfer ketol groups between several groups; in Escherichia coli there are two tkt genes, tktA expressed during exponential growth and the tktB during stationary phase NP_946300.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946305.1 catalyzes the formation of 1-deoxy-D-xylulose 5-phosphate from pyruvate and D-glyceraldehyde 3-phosphate NP_946306.1 catalyzes the bidirectional exonucleolytic cleavage of DNA NP_946311.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946314.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946320.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946334.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946336.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946343.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946345.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946346.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946353.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946357.1 extradiol catechol dioxygenase that catalyzes the oxidative cleavage of substituted catechols; part of the bacterial aromatic compound degradation pathway NP_946358.1 extradiol catechol dioxygenase that catalyzes the oxidative cleavage of substituted catechols; part of the bacterial aromatic compound degradation pathway NP_946360.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946364.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946373.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946381.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946385.1 RNH2; RNase HII; binds manganese; endonuclease which specifically degrades the RNA of RNA-DNA hybrids NP_946388.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946389.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946390.1 An essential enzyme in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis NP_946391.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946393.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946394.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946396.1 glycine--tRNA ligase alpha chain; GlyRS; class II aminoacyl tRNA synthetase; tetramer of alpha(2)beta(2); catalyzes a two-step reaction; first charging a glycine molecule by linking its carboxyl group to the alpha-phosphate of ATP; second by transfer of the aminoacyl-adenylate to its tRNA NP_946398.1 glycine--tRNA ligase beta chain; glyS; class II aminoacyl tRNA synthetase; tetramer of alpha(2)beta(2); catalyzes a two-step reaction; first charging a glycine molecule by linking the carboxyl group to the alpha-phosphate of ATP; second by transfer of the aminoacyl-adenylate to its tRNA NP_946402.1 catalyzes the formation of phosphoenolpyruvate from pyruvate NP_946404.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946405.1 catalyzes the formation of oxaloacetate from L-aspartate NP_946406.1 3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphate NP_946407.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946411.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946419.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946420.1 Catalyzes the reversible hydrolysis of the amide bond within dihydroorotate. This metabolic intermediate is required for the biosynthesis of pyrimidine nucleotides NP_946427.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946443.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946444.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946445.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946446.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946448.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946450.1 endonuclease; resolves Holliday structures; forms a complex of RuvABC; the junction binding protein RuvA forms a hexameric ring along with the RuvB helicase and catalyzes branch migration; RuvC then interacts with RuvAB to resolve the Holliday junction by nicking DNA strands of like polarity NP_946451.1 plays an essential role in ATP-dependent branch migration of the Holliday junction NP_946452.1 Reclaims exogenous and endogenous cytidine and 2'-deoxycytidine molecules for UMP synthesis NP_946453.1 promotes strand exchange during homologous recombination; RuvAB complex promotes branch migration; RuvABC complex scans the DNA during branch migration and resolves Holliday junctions at consensus sequences; forms hexameric rings around opposite DNA arms; requires ATP for branch migration and orientation of RuvAB complex determines direction of migration NP_946455.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946465.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946467.1 Member of the extracytoplasmic function sigma factors which are active under specific conditions; binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription NP_946468.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946471.1 forms dimers; may be involved in cell envelope integrity; interacts with outer membrane proteins and with the C-terminal domain of inner membrane protein TolA NP_946474.1 Brucella abortus, contains similarity to peptidoglycan-associated lipoprotein precursor; observed by proteomics NP_946477.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946482.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946484.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946488.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946490.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946491.1 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; the rhizobia have multiple copies of the groEL gene which are active under different environmental conditions; the S. meliloti protein in this cluster is not associated with a groES gene NP_946492.1 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring NP_946493.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946495.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946497.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946499.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946500.1 long form of enzyme; catalyzes the formation of N'-5'-phosphoribosyl-ATP from phosphoribosyl pyrophosphate; crucial role in histidine biosynthesis; forms active dimers and inactive hexamers which is dependent on concentration of substrates and inhibitors NP_946501.1 May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine NP_946502.1 in Escherichia coli RsmE methylates the N3 position of the U1498 base in 16S rRNA; cells lacking this function can grow, but are outcompeted by wild-type; SAM-dependent m(3)U1498 methyltransferase NP_946504.1 UbiA prenyltransferase family catalyzes the transfer of a prenyl group to various acceptors with hydrophobic ring structures in the biosynthesis of respiratory quinones, hemes, chlorophylls, vitamin E, and shikonin NP_946506.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946508.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946509.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946510.1 transfers the gamma-phosphate of ATP to the 4' position of a tetraacyldisaccharide 1-phosphate intermediate to form tetraacyldisaccharide 1,4'-bis-phosphate NP_946511.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946512.1 bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides NP_946513.1 catalyzes the formation of N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-D-ribosylamine and glycine in purine biosynthesis NP_946516.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946518.1 involved in methylation of ribosomal protein L3 NP_946520.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946522.1 The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision NP_946524.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946526.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946528.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946529.1 catalyzes a two-step reaction, first charging a histidine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class II aminoacyl-tRNA synthetase; forms homodimers; some organisms have a paralogous gene, hisZ, that is similar to hisS and produces a protein that performs the first step in histidine biosynthesis along with HisG NP_946530.1 catalyzes the formation of pyruvate and beta-alanine from L-alanine and 3-oxopropanoate NP_946532.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946536.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946539.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946543.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946544.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946545.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946546.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946547.1 catalyzes the formation of pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate NP_946549.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946550.1 Catalyzes a key regulatory step in fatty acid biosynthesis NP_946552.1 catalyzes the formation of chorismate from 5-O-(1-carboxyvinyl)-3-phosphoshikimate in aromatic amino acid biosynthesis NP_946554.2 involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation; binds to the N-terminal domain of the chaperone ClpA NP_946556.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946557.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946563.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946564.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946568.1 catalyzes the release of C-terminal glutamate residues from N-acylating moieties NP_946569.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946570.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946571.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946575.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946577.1 Couples the complete acetyl-CoA oxidation to aromatic ring reduction by the use of the low-potential electron shuttle ferredoxin NP_946578.1 catalyzes the coenzyme A dependent formation of succinyl-CoA from 2-oxoglutarate and ferredoxin NP_946579.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946580.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946584.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946586.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946587.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946588.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946589.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_946593.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946597.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946610.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946611.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946612.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946614.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946615.2 the MS-ring anchors the flagellum to the cytoplasmic membrane; part of the flagellar basal body which consists of four rings L, P, S, and M mounted on a central rod NP_946616.1 One of three proteins involved in switching the direction of the flagellar rotation NP_946617.1 binds to and inhibits the function of flagella specific ATPase FliI NP_946618.1 One of three proteins involved in switching the direction of the flagellar rotation NP_946619.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946627.1 catalyzes production of carbamoyl phosphate from bicarbonate and glutamine in pyrimidine and arginine biosynthesis pathways; forms an octamer composed of four CarAB dimers NP_946628.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946629.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946638.1 synthesizes RNA primers at the replication forks NP_946639.1 sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; this is the primary sigma factor of bacteria NP_946649.1 catalyzes the condensation of acetyl-CoA with malonyl-ACP to initiate cycles of fatty acid elongation; differs from 3-oxoacyl-(acyl carrier protein) synthase I and II in that it utilizes CoA thioesters as primers rather than acyl-ACPs NP_946654.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946656.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946657.1 catalyzes a sulfuration reaction to synthesize 2-thiouridine at the U34 position of tRNAs NP_946658.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946675.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946679.1 class II family (does not require metal); tetrameric enzyme; fumarase C; reversibly converts (S)-malate to fumarate and water; functions in the TCA cycle NP_946681.1 malate dehydrogenase; catalyzes the oxidation of malate to oxaloacetate NP_946712.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946717.1 with SoxZ catalyzes the oxidation of sulfur compounds NP_946726.1 nitrogenase iron protein; nitrogenase component 2; with component 1, an molybdenum-iron protein, catalyzes the fixation of nitrogen to ammonia; nitrogen reductase provides electrons to the nitrogenase complex; in R. etli there are three essentially identical copies of nifH which are actively expressed during symbiosis NP_946737.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946752.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946754.1 catalyzes the hydrolysis of allophanate NP_946761.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946764.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946765.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946766.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946767.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946770.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946771.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946772.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946773.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946776.1 part of the metNIQ transport system for methionine NP_946778.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946780.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946788.1 nitrogenase iron protein; nitrogenase component 2; with component 1, an molybdenum-iron protein, catalyzes the fixation of nitrogen to ammonia; nitrogen reductase provides electrons to the nitrogenase complex; alternative NifH, may be molybdenum-independent NP_946791.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946792.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946796.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946799.1 activates fatty acids by binding to coenzyme A NP_946801.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946806.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946811.1 catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis NP_946814.1 catalyzes the hydrolysis of allophanate NP_946817.1 catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia NP_946830.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946832.1 catalyzes the interconversion of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate NP_946836.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946842.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946843.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946844.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946845.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946848.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946852.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946853.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946854.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946855.1 involved in chelation of magnesium into protoporphyrin IX; involved in bacteriochlorophyll biosynthesis; part of a complex with BchI, BchD, and BchH NP_946857.1 catalyzes the formation of coproporphyrinogen from uroporphyrinogen III NP_946858.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946860.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946862.1 catalyzes the conversion of the propionic acid groups of rings I and III to vinyl groups during heme synthesis NP_946863.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946867.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946869.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946870.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946871.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946872.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946876.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946880.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946883.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946884.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946885.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946888.1 light-independent reduction of protochlorophyllide to form chlorophyllide a NP_946889.1 light-independent reduction of protochlorophyllide to form chlorophyllide a NP_946890.1 involved in chelation of magnesium into protoporphyrin IX; involved in bacteriochlorophyll biosynthesis; the enzyme from Rhodobacter capsulatus contains an Fe-S cluster; part of a complex with BchI, BchD, and BchH NP_946891.1 light-independent; with chlN(bchN) and chlB(bchB) reduces ring D of protochlorophyllide to form chlorophyllide a in chlorophyll/bacteriochlorophyll production NP_946892.1 catalyzes the formation of Mg-protoporphyrin IX methyl ester and S-adenosyl-L-homocysteine from Mg-protoporphyrin IX and S-adenosyl-L-methionine NP_946894.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946896.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946898.1 oxidative; catalyzes the formation of divinylprotochlorophyllide from magnesium-protoporphyrin IX 13-monomethyl ester in isocyclic ring formation in chlorophyll biosynthesis NP_946900.1 catalyzes the formation of 5-aminolevulinate from succinyl-CoA and glycine NP_946905.1 type III RuBisCO; involved in carbon fixation NP_946915.1 catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol NP_946916.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946918.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946919.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946922.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946925.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946926.1 proline utilization protein A; multifunctional protein that functions in proline catabolism in the first two enzymatic steps resulting in the conversion of proline to glutamate; in Escherichia coli this protein self regulates transcription via a DNA-binding domain at the N-terminus but the proteins from this group do not and in addition appear to have a truncated C-terminal domain NP_946932.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946935.1 primary rRNA binding protein; nucleates 30S assembly; involved in translational accuracy with proteins S5 and S12; interacts with protein S5; involved in autogeneously regulating ribosomal proteins by binding to pseudoknot structures in the polycistronic mRNA; interacts with transcription complex and functions similar to protein NusA in antitermination NP_946937.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946938.1 converts L-glutamate to D-glutamate, a component of peptidoglycan NP_946940.1 catalyzes the formation of L-tryptophan from indole and L-serine NP_946942.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946943.1 catalyzes the formation of 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine from N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide and L-glutamine in purine biosynthesis NP_946946.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946952.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946953.1 CTG start codon; 64% identity to Bradyrhizobium japonicum Bll5710 protein NP_946954.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946955.1 catalyzes the formation of benzaldehyde from benzoylformate NP_946956.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946957.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946958.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946960.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946963.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946964.1 thiamine-pyrophosphate requiring enzyme NP_946966.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946968.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946969.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946972.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946973.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946974.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946975.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946976.1 regulates chemotaxis by demethylation of methyl-accepting chemotaxis proteins NP_946978.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946979.1 involved in type III protein export during flagellum assembly NP_946980.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946982.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946984.1 membrane protein involved in the flagellar export apparatus NP_946986.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946990.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946991.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946994.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946997.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_946999.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947000.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947001.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947005.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947006.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947009.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947010.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947012.1 catalyzes the oxygen-independent formation of protoporphyrinogen-IX from coproporphyrinogen-III NP_947013.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947014.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947015.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947019.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947022.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947023.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947024.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947028.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947029.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947030.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947032.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947033.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947036.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947039.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947040.1 may be involved in chromosome condensation; overexpression in Escherichia coli protects against decondensation by camphor; overexpressing the protein results in an increase in supercoiling NP_947046.1 catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia NP_947048.1 activates fatty acids by binding to coenzyme A NP_947049.1 Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation NP_947051.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947053.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947054.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947055.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947056.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947058.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947069.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947071.1 catalyzes the ring cleavage reaction in phenylacetate degradation and the formation of 3-hydroxyacyl-CoA from crotonyl-CoA NP_947072.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947074.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947078.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947079.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947080.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947081.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947082.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947083.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947086.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947087.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947090.1 allantoate amidohydrolase and N-carbamoyl-L-amino acid amidohydrolase are very similar; the allantoate amidohydrolase from Escherichia coli forms a dimer and binds zinc ions for catalytic activity and catalyzes the conversion of allantoate to (S)-ureidoglycolate and ammonia; carbamoyl amidohydrolase from Bacillus sp. converts N-carbamoyl amino acids to amino acids, ammonia, and carbon dioxide NP_947092.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947093.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947096.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947097.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947101.1 Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation NP_947102.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947103.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_947105.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947106.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_947108.1 activates fatty acids by binding to coenzyme A NP_947109.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947110.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_947111.1 activates fatty acids by binding to coenzyme A NP_947117.1 catalyzes the formation of oxaloacetate from phosphoenolpyruvate NP_947119.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947120.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947122.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947123.1 catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia NP_947126.1 catalyzes the formation of protocatechuate from 4-hydroxybenzoate NP_947127.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947131.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_947132.1 catalyzes the conversion of ferulic acid to feruloyl-CoA NP_947134.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947136.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947137.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947141.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947143.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947148.1 DNA polymerase involved in damage-induced mutagenesis and translesion synthesis. It is not the major replicative DNA polymerase. NP_947155.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947156.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947158.1 Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription NP_947164.1 Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription NP_947167.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947169.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947173.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947174.1 functions in transport of arginine/ornithine; inner membrane ATPase that cleaves ATP and phosphorylates two periplasmic proteins that function as two distinct transport systems, the AO (arginine and ornithine) and LAO (lysine, arginine, and ornithine) periplasmic binding proteins NP_947177.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947180.1 MDM; functions in conversion of succinate to propionate NP_947182.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947183.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947184.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947185.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947187.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947188.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947189.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947190.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947191.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947196.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947197.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947198.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947201.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947205.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947207.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947217.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947218.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947221.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947224.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947229.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947233.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947260.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947264.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947265.1 CycJ; periplasmic heme chaperone that binds heme transiently via a histidine residue and delivers it to newly synthesized and exported c-type cytochromes; requires the ATP hydrolysis activity of the CcmA protein in order to transfer the heme to the apocytochrome; part of the cytochrome c maturation system; periplasmic protein anchored to the inner membrane NP_947268.1 formamide amidohydrolase; catalyzes the hydrolysis of formamide to formate NP_947272.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947273.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947274.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947276.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947278.1 catalyzes the ATP-dependent addition of AMP to a subunit of glutamine synthetase; also catalyzes the reverse reaction - deadenylation; adenylation/deadenylation of glutamine synthetase subunits is important for the regulation of this enzyme NP_947284.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947285.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947286.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947288.1 ketopantoate reductase; catalyzes the NADPH reduction of ketopantoate to pantoate; functions in pantothenate (vitamin B5) biosynthesis NP_947290.1 catalyzes the formation of oxalyl-CoA from oxalate and Formyl-CoA NP_947292.1 possibly involved in transport of pyrroloquinoline quinone transport NP_947293.1 Required in the synthesis of PPQ, but its exact function is unknown NP_947300.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947302.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947316.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947318.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947319.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947320.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947322.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947323.1 together with moaC, is involved in the conversion of a guanosine derivative (GXP) into molybdopterin precursor Z NP_947324.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947325.1 catalyzes the formation of glycolate and phosphate from 2-phosphoglycolate NP_947326.1 Catalyzes D-ribose 5-phosphate --> D-ribulose 5-phosphate in the nonoxidative branch of the pentose phosphate pathway NP_947327.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947328.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947329.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947331.1 NH(3)-dependent; catalyzes the formation of nicotinamide adenine dinucleotide (NAD) from nicotinic acid adenine dinucleotide (NAAD) using either ammonia or glutamine as the amide donor and ATP; ammonia-utilizing enzymes include the ones from Bacillus and Escherichia coli while glutamine-utilizing enzymes include the Mycobacterial one; forms homodimers NP_947339.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947342.1 catalyzes a two-step reaction; charges a cysteine by linking its carboxyl group to the alpha-phosphate of ATP then transfers the aminoacyl-adenylate to its tRNA NP_947344.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947345.1 catalyzes the formation of 2-isopropylmalate from 1-methyl-2-oxobutanoate and acetyl-CoA NP_947346.1 thiamine-pyrophosphate requiring enzyme NP_947347.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947351.2 catalyzes the decarboxylaton of phospatidyl-L-sering to phosphatidylethanolamine NP_947353.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947357.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947359.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947362.1 Acylates the intermediate (KDO)2-lipid IVA to form (KDO)2-(lauroyl)-lipid IVA NP_947364.1 FabF, beta-Ketoacyl-ACP synthase II, KASII; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP. NP_947365.1 FabF; beta-ketoacyl-ACP synthase II, KASII; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP NP_947367.1 Involved in the biosynthetic pathways of fatty acids, phospholipids, lipopolysaccharides, and oligosaccharides NP_947369.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947374.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947375.1 IPP transferase; isopentenyltransferase; involved in tRNA modification; in Escherichia coli this enzyme catalyzes the addition of a delta2-isopentenyl group from dimethylallyl diphosphate to the N6-nitrogen of adenosine adjacent to the anticodon of tRNA species that read codons starting with uracil; further tRNA modifications may occur; mutations in miaA result in defects in translation efficiency and fidelity NP_947376.1 catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive NP_947377.1 with IlvI catalyzes the formation of 2-acetolactate from pyruvate, the small subunit is required for full activity and valine sensitivity; E.coli produces 3 isoenzymes of acetolactate synthase which differ in specificity to substrates, valine sensitivity and affinity for cofactors; also known as acetolactate synthase 3 small subunit NP_947380.1 catalyzes the formation of (R)-2,3-dihydroxy-3-methylbutanoate from (S)-2-hydroxy-2-methyl-3-oxobutanoate in valine and isoleucine biosynthesis NP_947388.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947390.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947391.1 catalyzes the formation of 2-isopropylmalate from acetyl-CoA and 2-oxoisovalerate in leucine biosynthesis NP_947392.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947406.1 reduces nitrous oxide to nitrogen NP_947427.1 catalyzes 2 sequential methylations, the formation of precorrin-1 and S-adenosyl-L-homocysteine from S-adenosyl-L-methionine and uroporphyrin III, and the formation of precorrin-2 and S-adenosyl-L-homocysteine from S-adenosyl-L-methionine and precorrin-1 NP_947428.1 responsible for the amidation of carboxylic groups at position A and C of cobyrinic acid or hydrogenobrynic acid NP_947429.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947432.1 CobK/CbiJ; there are 2 pathways for cobalamin (vitamin B12) production, one aerobic (ex. P. denitrificans), the other anaerobic (ex. S. typhimurium); the CobK/CbiJ perform similar reactions in both; the anaerobic pathway includes the use of a chelated cobalt ion in order for ring contraction to occur; CobK thus converts precorrin 6 into dihydro-precorrin 6 while CbiJ converts cobalt-precorrin 6 into cobalt-deihydro-precorrin 6 NP_947434.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947435.1 catalyzes the interconversion of precorrin-8X and hydrogenobyrinate NP_947438.1 catalyzes the oxidation of tricarballylate to cis-aconitate; FAD-dependent; required for the utilization of tricarballylate as a carbon and energy source by S. enterica NP_947439.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947441.1 catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation NP_947442.1 catalyzes the formation of precorrin 6x from precorrin 5 NP_947450.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947457.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947460.1 catalyzes the reaction of cyanate and bicarbonate to produce ammonia and carbon dioxide NP_947462.1 An electron-transfer protein; flavodoxin binds one FMN molecule, which serves as a redox-active prosthetic group NP_947463.1 with HmuTU is involved in the transport of hemin NP_947465.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947466.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947467.1 catalyzes the oxygen-independent formation of protoporphyrinogen-IX from coproporphyrinogen-III NP_947468.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947469.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947470.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947471.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947481.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947482.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947488.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947489.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947490.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_947492.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947493.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947494.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947498.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947500.1 catalyzes the formation of 3-methyl-2-oxobutanoate from 2,3,-dihydroxy-3-methylbutanoate NP_947501.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947509.1 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is co-regulated with symbiotic nitrogen fixation genes NP_947510.1 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring NP_947513.1 Citation: Saier et al. BBA 1422:1-56, 1999 NP_947516.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947517.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947518.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947522.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947523.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947524.1 catalyzes the conversion of guanine, xanthine and, to a lesser extent, hypoxanthine to GMP, XMP and IMP, respectively NP_947526.1 catalyzes the formation of tetrahydropteroyl-L-glutamate and methionine from L-homocysteine and 5-methyltetrahydropteroyltri-L-glutamate NP_947531.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947538.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947539.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947542.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947545.1 catalyzes the synthesis of xanthosine monophosphate by the NAD+ dependent oxidation of inosine monophosphate NP_947546.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947547.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947548.1 contains glutamine-hydrolyzing domain and glutamine amidotransferase; GMP-binding domain; functions to produce GMP from XMP in the IMP pathway NP_947562.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947563.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947566.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947572.1 type IV secretion VirB6 family NP_947575.1 type IV secretion system VirB4 family NP_947580.1 type IV secretion VirD4 coupling protein family NP_947597.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947602.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947605.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947611.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947614.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947616.1 catalyzes the formation of phosphoenolpyruvate from pyruvate NP_947617.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947620.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947621.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947624.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947625.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947630.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947636.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947640.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947642.1 structural flagella protein; Bradyrhizobium has one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagellum NP_947647.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947649.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947659.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947661.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_947664.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947670.1 catalyzes the formation of L-ornithine from N(2)-acetyl-L-ornithine NP_947671.1 thiamine-pyrophosphate requiring enzyme NP_947678.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947679.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947680.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947681.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947683.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947687.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947689.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947690.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947723.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947733.1 activates fatty acids by binding to coenzyme A NP_947734.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947740.1 catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine to form methionine NP_947742.1 with CobST catalyzes the formation of cobyrinic acid a,c-diamide from hydrogenobyrinic acid a,c-diamide in an ATP-dependent manner; involved in porphyrin and chlorophyll metabolism; vitamin B12 metabolism NP_947751.1 Citation: EMBO J 1999 Oct 1;18(19):5175-86 NP_947752.1 Citation: EMBO J 1999 Oct 1;18(19):5175-86 NP_947753.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947761.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947763.1 Provides the input to the respiratory chain from the NAD-linked dehydrogenases of the citric acid cycle. The complex couples the oxidation of NADH and the reduction of ubiquinone, to the generation of a proton gradient which is then used for ATP synthesis NP_947767.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947771.1 leucyltransferase; phenylalanyltransferse; functions in the N-end rule pathway; transfers Leu, Phe, Met, from aminoacyl-tRNAs to N-terminal of proteins with Arg or Lys NP_947774.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947775.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947776.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947777.1 an AccC homodimer forms the biotin carboxylase subunit of the acetyl CoA carboxylase, an enzyme that catalyzes the formation of malonyl-CoA, which in turn controls the rate of fatty acid metabolism NP_947778.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947779.1 catalyzes the formation of 3-dehydroshikimate from 3-dehydroquinate in chorismate biosynthesis NP_947782.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947784.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947785.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947786.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947788.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947792.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947794.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947795.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947798.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947799.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947802.1 catalyzes the formation of tyrosyl-tRNA(Tyr) from tyrosine and tRNA(Tyr) NP_947803.1 catalyzes hydrolysis of 1,6-anhydro bond of anyhydro-N-acetylmuramic acid (anhMurNAc) and phosphorylates anhMurNAc to produce N-acetyl-muramate-6-phosphate; involved in murein recycling NP_947804.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947806.1 with SufCD activates cysteine desulfurase SufS NP_947807.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947808.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947813.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947815.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947819.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947821.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947822.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947827.1 porin involved in osmoregulation allowing water to move into and out of the cell in response to osmotic pressure NP_947828.1 decatenates newly replicated chromosomal DNA and relaxes positive and negative DNA supercoiling NP_947830.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947832.1 Citation: Honjo et al. (1990) J. Bact. 172:1783-1790. NP_947833.1 catalyzes the reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde in arginine biosynthesis NP_947841.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947843.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947844.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947845.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947846.1 catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine NP_947847.1 type II fructose 1,6-bisphosphatae; in Escherichia coli this protein forms a dimer and binds manganese NP_947854.1 similar to YegS from E. coli NP_947855.1 Involved in peptide bond synthesis; alters the affinity of the ribosome for aminoacyl-tRNA NP_947857.1 Citation: Ruzicka et al. (2000) J. Bact. 182:469-476 NP_947858.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947865.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947867.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947868.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947875.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947880.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947881.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947882.1 Citation: Baltscheffsky et al. (1997) Biochim. Biophys. Acta 1337:113-122 NP_947885.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947888.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947889.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947894.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947895.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947896.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947899.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947901.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947902.1 observed by proteomics; Citation: Walshaw and Poole (1996) Mol. Microbiol. 21:1239-52 NP_947903.1 Citation: Walshaw and Poole (1996) Mol. Microbiol. 21:1239-52 NP_947904.1 Citation: Walshaw and Poole (1996) Mol. Microbiol. 21:1239-52 NP_947905.1 Citation: Walshaw and Poole (1996) Mol. Microbiol. 21:1239-52; observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947910.1 CysK; forms a complex with serine acetyltransferase CysE; functions in cysteine biosynthesis NP_947913.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947922.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947923.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947924.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947925.1 valine--tRNA ligase; ValRS; converts valine ATP and tRNA(Val) to AMP PPi and valyl-tRNA(Val); class-I aminoacyl-tRNA synthetase type 1 subfamily; has a posttransfer editing process to hydrolyze mischarged Thr-tRNA(Val) which is done by the editing domain NP_947928.1 responsible for recognizing base lesions in the genome and initiating base excision DNA repair NP_947929.1 catalyzes the radical-mediated insertion of two sulfur atoms into an acyl carrier protein (ACP) bound to an octanoyl group to produce a lipoyl group NP_947932.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947933.1 Citation: Foster-Hartnett et al. (1993) Mol. Microbiol. 8:903-914 NP_947934.1 observed by proteomics; Citation: Foster-Hartnett et al. (1993) Mol. Microbiol. 8:903-914 NP_947935.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947936.1 Citation: Pawlowski et al. (1991) Mol. Gen. Genet. 231:124-38; observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947937.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947938.1 catalyzes the transamination of D-amino acids and their alpha-keto acids NP_947939.1 Stimulates the elongation of poly(A) tails NP_947940.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947941.2 negatively supercoils closed circular double-stranded DNA NP_947943.1 Catalyzes the conversion of ATP and pantetheine 4'-phosphate to diphosphate and 3'-dephospho-coA NP_947944.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947946.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947947.1 Synthesizes oQ from preQ1 in a single S-adenosylmethionine-requiring step NP_947948.1 Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr) NP_947952.1 Citation: Vermeij et al. (1999) Mol. Microbiol. 32:913-926 NP_947953.1 Citation: Van Der Ploeg et al. (1999) J. Biol. Chem. 274:29358-29365 NP_947954.1 catalyzes the release of sulfite from alkanesulfonates NP_947962.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947963.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947964.1 Citation: Beil et al. (1995) Eur. J. Biochem. 229:385-394 NP_947966.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947969.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947970.1 Citation: Walshaw and Poole (1996) Mol. Microbiol. 21:1239-52 NP_947971.1 Citation: Walshaw and Poole (1996) Mol. Microbiol. 21:1239-52 NP_947972.1 Citation: Walshaw and Poole (1996) Mol. Microbiol. 21:1239-52 NP_947985.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947988.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947989.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947990.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947991.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947993.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947994.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947995.1 Citation: Tadros and Waterkamp (1989) EMBO J. 8:1303-1308 NP_947997.1 Citation: Bhagwat and Keister (1995) Mol. Plant Microbe Interact. 8:366-370 NP_947998.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_947999.1 observed by proteomics; Citation: Bhagwat et al. (1996) J. Bact. 178:4635-4642 NP_948001.1 forms a homotrimer; catalyzes the acetylation of glucosamine-1-phosphate and uridylation of N-acetylglucosamine-1-phosphate to produce UDP-GlcNAc; function in cell wall synthesis NP_948002.1 Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source NP_948003.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948009.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948013.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948014.1 Citation: Sohlenkamp et al. (2000) J. Biol. Chem. 275:18919-18925 NP_948016.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948017.1 catalyzes the methylthiolation of an aspartic acid residue of the S12 protein of the 30S ribosomal subunit NP_948023.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948025.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948026.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948028.1 catalyzes the formation of dihydrodipicolinate from L-aspartate 4-semialdehyde and pyruvate in lysine and diaminopimelate biosynthesis NP_948029.1 homopentamer; channel that opens in response to pressure or hypoosmotic shock NP_948030.1 binds to ssrA RNA (tmRNA) and is required for its successful binding to ribosomes; also appears to function in the trans-translation step by promoting accommodation of tmRNA into the ribosomal A site; SmpB protects the tmRNA from RNase R degradation in Caulobacter crescentus; both the tmRNA and SmpB are regulated in cell cycle-dependent manner; functions in release of stalled ribosomes from damaged mRNAs and targeting proteins for degradation NP_948031.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948033.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948034.1 Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits NP_948035.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948036.1 involved in the de novo synthesis of pyridoxine (Vitamin B6) NP_948037.1 Catalyzes the formation of holo-ACP, which mediates the essential transfer of acyl fatty acid intermediates during the biosynthesis of fatty acids and lipids NP_948038.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948039.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948040.1 Era; Escherichia coli Ras-like protein; Bex; Bacillus Era-complementing segment; essential protein in Escherichia coli that is involved in many cellular processes; GTPase; binds the cell membrane through apparent C-terminal domain; mutants are arrested during the cell cycle; Streptococcus pneumoniae Era binds to RNA and Escherichia coli Era binds 16S rRNA and 30S ribosome NP_948042.1 involved in DNA repair and RecFOR pathway recombination; RecFOR proteins displace ssDNA-binding protein and facilitate the production of RecA-coated ssDNA NP_948045.1 decatenates newly replicated chromosomal DNA and relaxes positive and negative DNA supercoiling NP_948048.1 Citation: Kehres et al. (2000) Mol. Microbiol. 36:1085-1100 NP_948053.1 Conjugates Arg from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate NP_948055.1 catalyzes the formation of porphobilinogen from 5-aminolevulinate NP_948057.1 activates fatty acids by binding to coenzyme A NP_948058.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948063.1 YghU; B2989; one of eight glutathione transferase proteins from E. coli NP_948067.1 catalyzes the reaction of glycine with 5,10-methylenetetrahydrofolate to form L-serine and tetrahydrofolate NP_948068.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948069.1 EC_number 1.1.193.-; observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948070.1 catalyzes the formation of riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine NP_948071.1 RibE; 6,7-diimethyl-8-ribityllumazine synthase; DMRL synthase; lumazine synthase; beta subunit of riboflavin synthase; condenses 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate to generate 6,6-dimethyl-8-lumazine (DMRL); riboflavin synthase then uses 2 molecules of DMRL to produce riboflavin (vitamin B12); involved in the last steps of riboflavin biosynthesis; forms a 60mer (icosahedral shell) in both Bacillus subtilis and Escherichia coli; in Bacillus subtilis this 60mer is associated with the riboflavin synthase subunit (alpha) while in Escherichia coli it is not NP_948072.1 Regulates rRNA biosynthesis by transcriptional antitermination NP_948073.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948074.1 pyrophosphate-energized proton pump; pyrophosphate-energized inorganic pyrophosphatase; H+-PPase; can cleave pyrophosphate to two phosphates; can generate a proton motive force and drive pyrophosphate synthesis when PMF is sufficient NP_948080.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948082.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948083.1 involved in acylation of glycerol-3-phosphate to form 1-acyl-glycerol-3 phosphate for use in phospholipid biosynthesis; functions with PlsY NP_948084.1 FabH; beta-ketoacyl-acyl carrier protein synthase III; catalyzes the condensation of acetyl-CoA with malonyl-ACP to initiate cycles of fatty acid elongation; differs from 3-oxoacyl-(acyl carrier protein) synthase I and II in that it utilizes CoA thioesters as primers rather than acyl-ACPs NP_948085.1 This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control NP_948091.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948092.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948098.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948106.1 catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol NP_948107.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948108.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_948109.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948110.1 in Escherichia coli this protein is one of the earliest assembly proteins in the large subunit NP_948111.1 forms a direct contact with the tRNA during translation NP_948113.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948114.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948118.1 catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to thymidine monophosphate (dTMP) to form thymidine diphosphate (dTDP) NP_948119.1 catalyzes the DNA-template-directed extension of the 3'-end of a DNA strand; the delta' subunit seems to interact with the gamma subunit to transfer the beta subunit on the DNA NP_948120.1 methionine--tRNA ligase; MetRS; adds methionine to tRNA(Met) with cleavage of ATP to AMP and diphosphate; some MetRS enzymes form dimers depending on a C-terminal domain that is also found in other proteins such as Trbp111 in Aquifex aeolicus and the cold-shock protein CsaA from Bacillus subtilis while others do not; four subfamilies exist based on sequence motifs and zinc content NP_948123.1 activates fatty acids by binding to coenzyme A NP_948125.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948132.1 subunit A of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; in S. meliloti it is known to be involved with K+ NP_948133.1 subunit C of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali NP_948134.1 subunit D of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; contains an oxidoreductase domain; catalyzes the transfer of electrons from NADH to ubiquinone NP_948135.1 subunit E of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; in S. meliloti it is known to be involved specifically with K+ transport NP_948136.1 subunit F of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; in S. meliloti it is known to be involved specifically with K+ transport NP_948137.1 Citation: Putkorny et al. (1998) Mol. Microbiol. 28:1091-1101 NP_948139.1 catalyzes the reaction of glycine with 5,10-methylenetetrahydrofolate to form L-serine and tetrahydrofolate NP_948140.1 Citation: Rossbach et al. (1994) Mol. Gen. Genet. 245:11-24 NP_948142.1 Citation: Yang et al. (1996) FEMS Microbiol. Lett. 141:89-95 NP_948144.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948148.1 Citation: Payne et al. (1997) Biochemistry 36:5447-5454 NP_948149.1 Citation: Payne et al. (1997) Biochemistry 36:5447-5454 NP_948154.1 functions in degradation of stringent response intracellular messenger ppGpp; in Escherichia coli this gene is co-transcribed with the toxin/antitoxin genes mazEF; activity of MazG is inhibited by MazEF in vitro; ppGpp inhibits mazEF expression; MazG thus works in limiting the toxic activity of the MazF toxin induced during starvation; MazG also interacts with the GTPase protein Era NP_948157.1 binds to single stranded DNA and may facilitate the binding and interaction of other proteins to DNA NP_948159.1 The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 uvrA and 2 uvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by uvrB, the uvrA molecules dissociate NP_948160.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948168.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948170.1 TrmFO; Gid; glucose-inhibited division protein; similar to GidA; the gene from Bacillus subtilis encodes a tRNA-methyltransferase that utilizes folate as the carbon donor and bound flavin as reductant; modifies tRNA at position 54 (uridine) of the T-psi loop to form a C5-methyluridine NP_948173.1 forms a complex with SecD and YajC; SecDFyajC stimulates the proton motive force-driven protein translocation; seems to modulate the cycling of SecA by stabilizing its membrane-inserted state and appears to be required for the release of mature proteins from the extracytoplasmic side of the membrane; in some organisms, such as Bacillus subtilis, SecD is fused to SecF NP_948174.1 part of the preprotein secretory system; when complexed with proteins SecF and YajC, SecDFyajC stimulates the proton motive force-driven protein translocation, and appears to be required for the release of mature proteins from the extracytoplasmic side of the membrane NP_948175.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948176.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948180.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948184.1 catalyzes the conversion of a phosphate monoester to an alcohol and a phosphate NP_948186.1 catalyzes a two-step reaction, first charging a serine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA NP_948189.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948190.1 TatA; similar to TatE that is found in some proteobacteria; part of system that translocates proteins with a conserved twin arginine motif across the inner membrane; capable of translocating folded substrates typically those with bound cofactors; similar to a protein import system in thylakoid membranes NP_948191.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948193.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948194.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948195.1 catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class-I aminoacyl-tRNA synthetase NP_948197.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948198.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948204.1 E3 component of pyruvate complex; catalyzes the oxidation of dihydrolipoamide to lipoamide NP_948205.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948206.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948207.1 catalyzes the oxidative decarboxylation of pyruvate with concomitant acetylation of a lipoic acid-containing dihydrolipoamide acetyltransferase within the complex. The E1 component of the pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase(E2) and lipoamide dehydrogenase NP_948208.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948210.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948211.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948213.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948214.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948215.1 enolase; catalyzes the formation of phosphoenolpyruvate from 2-phospho-D-glycerate in glycolysis NP_948216.1 NADPH-dependent; catalyzes the reduction of 7-cyano-7-deazaguanine to 7-aminomethyl-7-deazaguanine in queuosine biosynthesis NP_948217.1 involved in the biosynthesis of osmoregulated periplasmic glucans; required for the assembly of the polyglucose structure of glucan NP_948218.1 necessary for biosynthesis of osmoregulated periplasmic glucans possibly involved in the transfer to the periplasmic space NP_948220.1 catalyzes the formation of 2-dehydro-3-deoxy-D-octonate 8-phosphate from phosphoenolpyruvate and D-arabinose 5-phosphate in LPS biosynthesis NP_948227.1 CTP synthase; CTP synthase; cytidine triphosphate synthetase; catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen; in Escherichia coli this enzyme forms a homotetramer NP_948229.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948230.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948231.1 Catalyzes the conversion of N-(5-phospho-D-ribosyl)-anthranilate and diphosphate to anthranilate and 5-phospho-alpha-D-ribose 1-diphosphate NP_948232.1 involved in tryptophan biosynthesis; amino acid biosynthesis; converts 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate and carbon dioxide and water NP_948233.1 MoaC; along with MoaA is involved in conversion of a guanosine derivative into molybdopterin precursor Z; involved in molybdenum cofactor biosynthesis NP_948244.1 Represses a number of genes involved in the response to DNA damage NP_948246.1 catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA NP_948247.1 Charges one glutamine molecule and pairs it to its corresponding RNA trinucleotide during protein translation NP_948248.1 type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH NP_948250.1 catalyzes the formation of lipid A disaccharide from UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate, lipid A disaccharide is a precursor of lipid A that anchors LPS to the OM NP_948252.1 catalyzes the addition of (R)-3-hydroxytetradecanoyl to the glucosamine disaccharide in lipid A biosynthesis NP_948253.1 in Pseudomonas aeruginosa this enzyme is a trimer of dimers; essential for membrane formation; performs third step of type II fatty acid biosynthesis; catalyzes dehydration of (3R)-hydroxyacyl-ACP to trans-2-acyl-ACP NP_948254.1 adds the O-linked and N-linked 3(R)-hydroxy fatty acids to the glucosamine disaccharide during lipid A biosynthesis NP_948255.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948256.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948257.1 catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate NP_948258.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948259.1 catalyzes the formation of undecaprenyl pyrophosphate from isopentenyl pyrophosphate NP_948260.1 Rrf; Frr; ribosome-recycling factor; release factor 4; RF4; recycles ribosomes upon translation termination along with release factor RF-3 and elongation factor EF-G; A GTPase-dependent process results in release of 50S from 70S; inhibited by release factor RF-1; essential for viability; structurally similar to tRNAs NP_948261.1 Catalyzes the phosphorylation of UMP to UDP NP_948262.1 EF-Ts; functions during elongation stage of protein translation; forms a dimer; associates with EF-Tu-GDP complex and promotes exchange of GDP to GTP resulting in regeneration of the active form of EF-Tu NP_948263.1 one of the last subunits in the assembly of the 30S subunit; absence of S2 does not inhibit assembly but results in an inactive subunit NP_948265.1 catalyzes DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time; main replicative polymerase NP_948267.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948268.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948269.1 catalyzes the formation of prolyl-tRNA(Pro) from proline and tRNA(Pro) NP_948272.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948275.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948277.1 catalyzes the formation of biotinyl-5'-AMP, also acts as a transcriptional repressor of the biotin operon NP_948278.1 Catalyzes the transfer of electrons from NADH to quinone NP_948279.1 Catalyzes the transfer of electrons from NADH to quinone NP_948280.1 Catalyzes the transfer of electrons from NADH to ubiquinone NP_948281.1 Catalyzes the transfer of electrons from NADH to quinone NP_948282.1 Catalyzes the transfer of electrons from NADH to quinone NP_948283.1 Catalyzes the transfer of electrons from NADH to quinone NP_948284.1 Catalyzes the transfer of electrons from NADH to quinone NP_948285.1 Catalyzes the transfer of electrons from NADH to quinone NP_948286.1 part of NADH-ubiquinone oxidoreductase complex I; shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain; NuoF is part of the soluble NADH dehydrogenase fragment, which represents the electron input part of NADH dehydrogenase NP_948288.1 Catalyzes the transfer of electrons from NADH to quinone NP_948290.1 Catalyzes the transfer of electrons from NADH to quinone NP_948291.1 Catalyzes the transfer of electrons from NADH to quinone NP_948292.1 The point of entry for the majority of electrons that traverse the respiratory chain eventually resulting in the reduction of oxygen NP_948293.1 Catalyzes the transfer of electrons from NADH to quinone NP_948294.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948295.1 catalyzes the release of the N-terminal amino acid from a tripeptide NP_948296.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948297.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948300.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948301.1 binds and unfolds substrates as part of the ClpXP protease NP_948302.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948303.1 Tig; RopA; peptidyl-prolyl cis/trans isomerase; promotes folding of newly synthesized proteins; binds ribosomal 50S subunit; forms a homodimer NP_948306.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948307.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948308.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948310.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948311.1 catalyzes the formation of S-adenosyl-4-methylthionine-2-oxobutanoate and 7,8-diaminononanoate from S-adenosyl-L-methionine and 8-amino-7-oxononanoate NP_948312.1 DTB synthetase; dethiobiotin synthase; involved in production of dethiobiotin from ATP and 7,8-diaminononanoate and carbon dioxide; contains magnesium NP_948313.1 catalyzes the formation of 8-amino-7-oxononanoate from 6-carboxyhexanoyl-CoA and L-alanine NP_948315.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948316.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948318.1 Catalyzes the rate-limiting step in dNTP synthesis NP_948319.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948326.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948335.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948343.1 one of the components of the high-affinity ATP-driven potassium transport (or KDP)system, which catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions; the C subunit may be involved in assembly of the KDP complex NP_948344.1 One of the components of the high-affinity ATP-driven potassium transport (or KDP) system, which catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions NP_948345.1 catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions NP_948351.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948354.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948359.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948360.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948362.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948363.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948367.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948372.1 catalyzes the formation of L-ornithine from N(2)-acetyl-L-ornithine NP_948376.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948378.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948381.1 NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate NP_948382.1 catalyzes a two-step reaction, first charging an aspartate molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; contains discriminating and non-discriminating subtypes NP_948384.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948386.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948387.1 catalyzes the reversible transfer of the terminal phosphate of ATP to form a long chain polyphosphate NP_948390.1 catalyzes the formation of 1-(5-phosphoribosyl)-5-aminoimidazole from 2-(formamido)-N1-(5-phosphoribosyl)acetamidine and ATP in purine biosynthesis NP_948392.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948393.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948395.1 catalyzes the formation of nucleoside triphosphate from ATP and nucleoside diphosphate NP_948397.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948398.1 binds to single-strand binding (SSB) protein and acts as a bridge between the DnaX clamp loader complex and the SSB NP_948399.1 catalyzes the removal of N-terminal amino acids preferably leucine from various peptides NP_948402.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948403.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948404.1 catalyzes oxidation of 4-(phosphohydroxy)-L-threonine into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which decarboxylates to form 1-amino-3-(phosphohydroxy)propan-2-one (3-amino-2-oxopropyl phosphate) NP_948405.1 catalyzes the transfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adenosine bases A1518 and A1519 in 16S rRNA; mutations in ksgA causes resistance to the translation initiation inhibitor kasugamycin NP_948406.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948407.1 28% identity with Bradyrhizobium japonicum Bll4089 protein NP_948408.1 Essential for recycling GMP and indirectly, cGMP NP_948409.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948410.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948411.1 FabF; beta-ketoacyl-ACP synthase II, KASII; catalyzes a condensation reaction in fatty acid biosynthesis: addition of an acyl acceptor of two carbons from malonyl-ACP; required for the elongation of short-chain unsaturated acyl-ACP NP_948412.1 carries the fatty acid chain in fatty acid biosynthesis NP_948413.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948414.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948416.1 binds cooperatively with S18 to the S15-16S complex, allowing platform assembly to continue with S11 and S21 NP_948417.1 binds as a heterodimer with protein S6 to the central domain of the 16S rRNA; helps stabilize the platform of the 30S subunit NP_948419.1 in Escherichia coli this protein is wrapped around the base of the L1 stalk NP_948420.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948423.1 unwinds double stranded DNA NP_948428.1 Sms; stabilizes the strand-invasion intermediate during the DNA repair; involved in recombination of donor DNA and plays an important role in DNA damage repair after exposure to mutagenic agents NP_948429.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948430.1 Catalyzes first step of the de novo purine nucleotide biosynthetic pathway NP_948431.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948432.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948434.1 EngA; essential Neisserial GTPase; synchronizes cellular events by interacting with multiple targets with tandem G-domains; overexpression in Escherichia coli suppresses rrmJ mutation; structural analysis of the Thermotoga maritima ortholog shows different nucleotide binding affinities in the two binding domains NP_948435.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948436.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948437.1 catalyzes the formation of tetrahydrofolate and 2-dehydropantoate from 5,10-methylenetetrahydrofolate and 3-methyl-2-oxobutanoate NP_948439.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948440.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948443.1 allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases; reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA NP_948444.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948446.1 allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases; reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA NP_948450.1 allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases; reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA; some Mycoplasma proteins contain an N-terminal fusion to an unknown domain NP_948452.1 similar to RuvC resolvase with substantial differences; NMR structural information suggests this protein is monomeric; unknown cellular function NP_948454.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948456.1 catalyzes the transfer of the carbamoyl moiety from carbamoyl phosphate to L- aspartate in pyrimidine biosynthesis NP_948457.1 Catalyzes the reversible hydrolysis of the amide bond within dihydroorotate. This metabolic intermediate is required for the biosynthesis of pyrimidine nucleotides NP_948458.1 involved in acylation of glycerol-3-phosphate to form 1-acyl-glycerol-3 phosphate for use in phospholipid biosynthesis; functions with PlsX NP_948463.1 catalyzes the ATP-dependent breakage of single-stranded DNA followed by passage and rejoining, maintains net negative superhelicity NP_948466.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948468.1 in Escherichia coli BM108, a mutation that results in lack of L33 synthesis had no effect on ribosome synthesis or function; there are paralogous genes in several bacterial genomes, and a CXXC motif for zinc binding and an upstream regulation region of the paralog lacking this motif that are regulated by zinc similar to other ribosomal proteins like L31; the proteins in this group lack the CXXC motif NP_948471.1 involved in swarmer-to-stalked cell differentiation in Caulobacter crescentus; catalyzes the condensation of two GTP molecules to form the secondary messenger cyclic di-GMP (c-di-GMP); upon phosphorylation of domain D1 the protein dimerizes; presumably this allows the two GTP-bound GGDEF (diguanylate cyclase) domains to catalyze the condensation reaction; allosterically inhibited by c-di-GMP NP_948473.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948474.1 involved in translesion DNA polymerization with beta clamp of polymerase III; belongs to Y family of polymerases; does not contain proofreading function NP_948475.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948476.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948479.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948486.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948487.1 involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation; binds to the N-terminal domain of the chaperone ClpA NP_948494.1 catalyzes the formation of (R)-pantothenate from pantoate and beta-alanine NP_948496.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948498.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948508.1 lipoyl/octanoyltransferase; catalyzes the transfer of the lipoyl/octanoyl moiety of lipoyl/octanoyl-ACP onto lipoate-dependent enzymes like pyruvate dehydrogenase and the glycine cleavage system H protein NP_948512.1 catalyzes the hydrolysis of acylphosphate NP_948513.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948514.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948516.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948524.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948527.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948529.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948530.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948531.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948532.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948533.1 Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation NP_948534.1 Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates NP_948538.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948542.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948547.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948554.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948556.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948560.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948562.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948563.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948564.1 is a component of the macrolide binding site in the peptidyl transferase center NP_948565.1 catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Dimerization of the alpha subunit is the first step in the sequential assembly of subunits to form the holoenzyme NP_948566.1 located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA; forms part of the Shine-Dalgarno cleft in the 70S ribosome; interacts with S7 and S18 and IF-3 NP_948567.2 located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA; makes contact with the large subunit via RNA-protein interactions and via protein-protein interactions with L5; contacts P-site tRNA NP_948568.1 essential enzyme that recycles AMP in active cells; converts ATP and AMP to two molecules of ADP NP_948569.1 forms heterotrimeric complex in the membrane; in bacteria the complex consists of SecY which forms the channel pore and SecE and SecG; the SecG subunit is not essential; in bacteria translocation is driven via the SecA ATPase NP_948570.1 late assembly protein NP_948571.1 L30 binds domain II of the 23S rRNA and the 5S rRNA; similar to eukaryotic protein L7 NP_948572.1 located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body; contacts S4 and S8; with S4 and S12 plays a role in translational accuracy; mutations in this gene result in spectinomycin resistance NP_948573.1 binds 5S rRNA along with protein L5 and L25 NP_948574.1 ribosomal protein L6 appears to have arisen as a result of an ancient gene duplication as based on structural comparison of the Bacillus stearothermophilus protein; RNA-binding appears to be in the C-terminal domain; mutations in the L6 gene confer resistance to aminoglycoside antibiotics such as gentamicin and these occur in truncations of the C-terminal domain; it has been localized to a region between the base of the L7/L12 stalk and the central protuberance NP_948575.1 binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit NP_948576.1 located in the peptidyl transferase center and involved in assembly of 30S ribosome subunit; similar to what is observed with proteins L31 and L33, some proteins in this family contain CXXC motifs that are involved in zinc binding; if two copies are present in a genome, then the duplicated copy appears to have lost the zinc-binding motif and is instead regulated by zinc; the proteins in this group do not appear to have the zinc-binding motif NP_948577.1 part of 50S and 5S/L5/L18/L25 subcomplex; contacts 5S rRNA and P site tRNA; forms a bridge to the 30S subunit in the ribosome by binding to S13 NP_948578.1 assembly initiator protein; binds to 5' end of 23S rRNA and nucleates assembly of the 50S; surrounds polypeptide exit tunnel NP_948579.1 binds to the 23S rRNA between the centers for peptidyl transferase and GTPase NP_948580.1 primary binding protein; helps mediate assembly; involved in translation fidelity NP_948581.1 one of the stabilizing components for the large ribosomal subunit NP_948582.1 located in the peptidyl transferase center and may be involved in peptidyl transferase activity; similar to archaeal L10e NP_948583.1 forms a complex with S10 and S14; binds the lower part of the 30S subunit head and the mRNA in the complete ribosome to position it for translation NP_948584.1 binds specifically to 23S rRNA during the early stages of 50S assembly; makes contact with all 6 domains of the 23S rRNA in the assembled 50S subunit and ribosome; mutations in this gene result in erythromycin resistance; located near peptidyl-transferase center NP_948585.1 protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA NP_948586.1 one of the primary rRNA-binding proteins; required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation NP_948587.1 binds third domain of 23S rRNA and protein L29; part of exit tunnel NP_948588.1 L4 is important during the early stages of 50S assembly; it initially binds near the 5' end of the 23S rRNA NP_948589.1 binds directly near the 3' end of the 23S rRNA, where it nucleates assembly of the 50S subunit; essential for peptidyltransferase activity; mutations in this gene confer resistance to tiamulin NP_948590.1 NusE; involved in assembly of the 30S subunit; in the ribosome, this protein is involved in the binding of tRNA; in Escherichia coli this protein was also found to be involved in transcription antitermination; NusB/S10 heterodimers bind boxA sequences in the leader RNA of rrn operons which is required for antitermination; binding of NusB/S10 to boxA nucleates assembly of the antitermination complex NP_948591.1 EF-Tu; promotes GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; when the tRNA anticodon matches the mRNA codon, GTP hydrolysis results; the inactive EF-Tu-GDP leaves the ribosome and release of GDP is promoted by elongation factor Ts; many prokaryotes have two copies of the gene encoding EF-Tu NP_948592.1 EF-G; promotes GTP-dependent translocation of the ribosome during translation; many organisms have multiple copies of this gene NP_948593.1 binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit NP_948594.1 interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone; located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side; mutations in the S12 gene confer streptomycin resistance NP_948604.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948606.1 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Subunit beta' binds to sigma factor allowing it to bind to the -10 region of the promoter NP_948607.1 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates; beta subunit is part of the catalytic core which binds with a sigma factor to produce the holoenzyme NP_948608.1 present in two forms; L12 is normal, while L7 is aminoacylated at the N-terminal serine; the only multicopy ribosomal protein; 4:1 ratio of L7/L12 per ribosome; two L12 dimers bind L10; critically important for translation efficiency and fidelity; stimulates GTPase activity of translation factors NP_948609.2 binds the two ribosomal protein L7/L12 dimers and anchors them to the large ribosomal subunit NP_948611.1 in Escherichia coli and Methanococcus, this protein autoregulates expression; the binding site in the mRNA mimics the binding site in the 23S rRNA NP_948612.1 binds directly to 23S ribosomal RNA NP_948613.1 Modulates Rho-dependent transcription termination NP_948614.1 forms a complex with SecY and SecG; SecYEG forms a protein-conducting channel to which secA binds and translocates targeted polypeptides across the cytoplasmic membrane, a process driven by ATP and a proton-motive force NP_948622.1 EF-Tu; promotes GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; when the tRNA anticodon matches the mRNA codon, GTP hydrolysis results; the inactive EF-Tu-GDP leaves the ribosome and release of GDP is promoted by elongation factor Ts; many prokaryotes have two copies of the gene encoding EF-Tu NP_948623.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948624.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948625.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948626.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948627.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948628.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948632.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948633.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948636.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948640.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948643.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948644.1 CTG start codon NP_948647.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948648.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948661.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948681.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948685.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948686.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948699.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948701.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948703.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948704.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948713.1 catalyzes the phosphorylation of NAD to NADP NP_948715.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948726.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948729.1 PR-AMP cyclohydrolase; functions in histidine biosynthesis from PRPP; converts 1-(5-phosphoribosyl)-AMP to 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4- carboxyamide during the histidine biosynthesis pathway; binds zinc and magnesium; forms homodimers NP_948730.1 involved in the first step of tetrahydrofolate biosynthesis; catalyzes the formation of formate and 2-amino-4-hydroxy-6-(erythro-1,2, 3-trihydroxypropyl)dihydropteridine triphosphate from GTP and water; forms a homopolymer NP_948745.1 catalyzes a two-step reaction, first charging a threonine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; catalyzes the formation of threonyl-tRNA(Thr) from threonine and tRNA(Thr) NP_948747.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948751.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948762.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948764.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948767.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948769.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948778.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948779.1 catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia NP_948780.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_948784.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948785.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948786.1 catalyzes the formation of 3-hydroxy-2-methylpropanoate from 3-hydroxy-2-methylpropanoyl-CoA NP_948789.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948792.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_948795.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948796.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948804.1 Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation NP_948805.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948808.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948809.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948810.1 catalyzes the formation of 3-methyl-2-oxobutanoate from 2,3,-dihydroxy-3-methylbutanoate NP_948811.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948812.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948814.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948815.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948816.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948817.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948818.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948820.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948824.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948826.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948828.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948829.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948831.1 ThyA; catalyzes formation of dTMP and 7,8-dihydrofolate from 5,10-methylenetetrahydrofolate and dUMP; involved in deoxyribonucleotide biosynthesis; there are 2 copies in some Bacilli, one of which appears to be phage-derived NP_948838.1 class II family (does not require metal); tetrameric enzyme; fumarase C; reversibly converts (S)-malate to fumarate and water; functions in the TCA cycle NP_948839.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948840.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948841.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948848.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948857.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948858.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948859.1 zinc-dependent; catalyzes the deacetylation of UDP-(3-O-acyl)-N-acetylglucosamine to UDP-3-O-(3-hydroxytetradecanoyl)-glucosamine in the second step of lipid A biosynthesis NP_948860.1 GTPase; similar structure to tubulin; forms ring-shaped polymers at the site of cell division; other proteins such as FtsA, ZipA, and ZapA, interact with and regulate FtsZ function NP_948863.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948866.1 catalyzes the reduction of UDP-N-acetylglucosamine enolpyruvate to form UDP-N-acetylmuramate in peptidoglycan biosynthesis NP_948867.1 Catalyzes the formation of UDP-N-acetylmuramoyl-L-alanine from UDP-N-acetylmuramate and L-alanine in peptidoglycan synthesis NP_948868.1 UDP-N-acetylglucosamine--N-acetylmuramyl- (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase; involved in cell wall formation; inner membrane-associated; last step of peptidoglycan synthesis NP_948870.1 UDP-N-acetylmuramoylalanine--D-glutamate ligase; involved in peptidoglycan biosynthesis; cytoplasmic; catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine during cell wall formation NP_948871.1 First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan NP_948872.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948873.1 involved in cell wall formation; peptidoglycan synthesis; cytoplasmic enzyme; catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-aceylmuramoyl-l-alanyl-d-glutamate NP_948884.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948887.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948889.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948900.1 in Rhodopseudomonas palustris this protein confers resistance to arsenite; catalyzes the formation of a number of methylated intermediates from arsenite and SAM producing trimethylarsine NP_948902.1 tryptophan indole-lyase; catalyzes the formation of indole and pyruvate from tryptophan NP_948906.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948911.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948913.1 functions in thiamine (vitamin B1) biosynthesis; in Bacillus subtilis this enzyme catalyzes the formation of thiazole from dehydroxyglycine and 1-deoxy-D-xylulose-5-phosphate and ThiS-thiocarboxylate NP_948914.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948915.1 required for the synthesis of the hydromethylpyrimidine moiety of thiamine NP_948926.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948928.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948931.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948936.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948938.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948940.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948943.1 catalyzes the formation of (E)-3-(methoxycarbonyl)pent-2-enedioate and S-adenosyl-L-homocysteine from S-adenosyl-L-methionine and trans-aconitate NP_948947.1 ChvD; in Agrobacterium tumefaciens, mutations in both Walker boxes were found to affect virulence NP_948949.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948951.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948952.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948956.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948962.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948964.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948965.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948966.1 catalyzes the hydrolysis of a monocarboxylic acid amid to form a monocarboxylate and ammonia NP_948972.1 catalyzes the reversible formation of D-erythrose 4-phosphate and D-fructose 6-phosphate from sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate; catalyzes isomerization of glucose 6-phosphate and fructose 6-phosphate NP_948973.1 similar to full-length Gnd, these proteins seems to have a truncated C-terminal 6PGD domainin; in Methylobacillus flagellatus this gene is essential for NAD+-dependent oxidation of 6-phosphogluconate NP_948974.1 catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphate NP_948980.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948982.1 catalyzes the transfer of a segment of a 1,4-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain NP_948988.1 catalyzes the ATP dependent formation of a phosphodiester at the site of a single-strand break in duplex DNA NP_948992.1 in Escherichia coli MobA links a guanosine 5'-phosphate to molydopterin to form molybdopterin guanine dinucleotide during molybdenum cofactor biosynthesis NP_948993.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948995.1 activates fatty acids by binding to coenzyme A NP_948997.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_948998.1 ureases catalyze the hydrolysis of urea into ammonia and carbon dioxide; in Helicobacter pylori the ammonia released plays a key role in bacterial survival by neutralizing acids when colonizing the gastric mucosa; the holoenzyme is composed of 3 ureC (alpha) and 3 ureAB (gamma/beta) subunits NP_949000.1 ureases catalyze the hydrolysis of urea into ammonia and carbon dioxide; in Helicobacter pylori and Yersinia enterocolitica the ammonia released plays a key role in bacterial survival by neutralizing acids when colonizing the gastric mucosa; the holoenzyme is composed of 3 UreC (alpha) and 3 UreAB (gamma/beta); in Brucella suis the urease encoded by this operon (one of two urease-encoding operons found in its genome) is involved with urease activity, optimum growth, resistance to low-pH killing in-vitro and persistence in-vivo, while the other operon does not seem to be active NP_949001.1 UreA, with UreB and UreC catalyzes the hydrolysis of urea into ammonia and carbon dioxide; nickel metalloenzyme; accessory proteins UreD, UreE, UreF, and UreG are necessary for assembly of the metallocenter NP_949007.1 Citation: O'Hara et al. (1999) EMBO J. 18:5175-86 and Wilson et al. EMBO J. (1993) 12:3637-42; observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949009.1 stimulates the activities of the other two initiation factors, IF-2 and IF-3 NP_949010.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949011.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949017.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949023.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949030.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949031.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949032.1 CMP-2-keto-3-deoxyoctulosonic acid synthetase; catalyzes the formation of CMP-3-deoxy-D-manno-octulosonate from CTP and 3-deoxy-D-manno-octulosonate which is incorporated into LPS NP_949033.1 catalyzes the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis NP_949039.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949040.1 one of two methionine synthases in Escherichia coli; MetH catalyzes a methyl transfer reaction from methyltetrahydrofolate to homocysteine to create methionine; requires zinc for activity NP_949048.1 ferredoxin-dependent assimilatory nitrite reductase NP_949049.1 Catalyzes the reduction of sulfite to sulfide, an essential step in the anaerobic sulfate-respiration pathway NP_949050.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949051.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949052.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949054.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949055.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949056.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949057.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949060.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949061.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949062.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949063.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949067.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949069.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949070.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949071.1 catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP); functions in the nonmevalonate isoprenoid biosynthesis pathway NP_949072.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949077.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949078.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949081.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949082.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949084.1 catalyzes the formation of acetaldehyde from ethanolamine NP_949088.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949092.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949093.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949097.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949100.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949101.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949103.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949104.1 with PaaBCDE catalyzes the hydroxylation of phenylacetyl-CoA; involved in phenylacetate degradation NP_949105.1 with PaaBCDE catalyzes the hydroxylation of phenylacetyl-CoA NP_949107.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949108.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949110.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949112.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949113.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949118.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949119.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949121.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949122.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949123.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949135.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949138.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949139.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949140.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949141.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949146.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949147.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949150.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949151.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949152.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949154.1 Catalyzes two discrete reactions in the de novo synthesis of purines: the cleavage of adenylosuccinate and succinylaminoimidazole carboxamide ribotide NP_949155.1 catalyzes the formation of 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine from N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide and L-glutamine in purine biosynthesis NP_949157.1 With PurL and PurQ catalyzes the conversion of formylglycinamide ribonucleotide, ATP, and glutamine to formylglycinamidine ribonucleotide, ADP, and glutamate in the fourth step of the purine biosynthetic pathway NP_949158.1 catalyzes the formation of (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate and L-aspartate in purine biosynthesis; SAICAR synthase NP_949159.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949166.1 activates RNA polymerase to cleave back-tracked RNA during elongational pausing NP_949168.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949170.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949171.1 Converts isocitrate to alpha ketoglutarate NP_949184.1 Catalyzes a two-step reaction, first charging an alanyl molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA NP_949185.1 catalyzes the transfer of a methylene carbon from the methylamine-loaded GcvH protein to tetrahydrofolate, causing the release of ammonia and the generation of reduced GcvH protein NP_949186.1 part of multienzyme complex composed of H, L, P, and T proteins which catalyzes oxidation of glycine to yield carbon dioxide, ammonia, 5,10-CH2-H4folate and a reduced pyridine nucleotide; protein H is involved in transfer of methylamine group from the P to T protein; covalently bound to a lipoyl cofactor NP_949187.1 acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine NP_949188.1 catalyzes the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs NP_949198.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949201.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949205.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949208.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949212.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949213.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949215.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949218.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949219.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949220.1 membrane protein responsible for substrate specificity switching from rod/hook-type export to filament-type export NP_949221.1 FliR, with proteins FliP and FliQ, forms the core of the central channel in the flagella export apparatus NP_949222.1 FliQ, with proteins FliP and FliR, forms the core of the central channel in the flagella export apparatus; Bradyrhizobium have one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagellum NP_949223.1 forms a junction between the M-ring and FlgB during flagella biosynthesis; Bradyrhizobium has one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagella NP_949224.1 with FlgF and B makes up the proximal portion of the flagellar basal body rod NP_949225.1 with FlgF and C makes up the proximal portion of the flagellar basal body rod; Bradyrhizobium has one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagellum NP_949226.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949227.1 FliP, with proteins FliQ and FliR, forms the core of the central channel in the flagella export apparatus NP_949228.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949232.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949234.1 with FliG and FliN makes up the switch complex which is involved in switching the direction of the flagella rotation; Bradyrhizobium has one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagellum NP_949235.1 interacts with the cytoplasmic MS ring of the basal body and may act to stabilize the MotAB complexes which surround the MS ring NP_949236.1 FlgF, with FlgB and C, makes up the proximal portion of the flagellar basal body rod; Bradyrhizobium has one thick flagellum and several thin flagella; the Bradyrhizobium protein in this cluster is associated with the thick flagellum NP_949237.1 makes up the distal portion of the flagellar basal body rod; Bradyrhizobium has one thick flagellum and several thin flagella; the Bradyrhizobium protein in this cluster is associated with the thick flagella NP_949238.1 required for the assembly of the flagellar basal body P-ring; Bradyrhizobium has one thick flagellum and several thin flagella; the Bradyrhizobium protein in this cluster is associated with the thick flagellum NP_949239.1 part of the flagellar basal body which consists of four rings L,P, S and M mounted on a central rod NP_949240.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949241.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949242.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949244.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949245.1 regulator of the sigma 54 transcriptional activator FlbD; represses FlbD when the class II flagellar structure is absent and activates FlbD when the structure is present NP_949246.1 part of the basal body which consists of four rings L, P, S, and M mounted on a central rod; Vibrio parahaemolyticus, Yersinia, Bradyrhizobium and other bacteria have two copies of this and other flagellar genes; the V. parahaemolyticus protein is associated with the polar flagella and the Bradyrhizobium protein is associated with the thick flagellum NP_949250.1 acts as an activator of flagellin translation and may be required for filament secretion or assembly; Bradyrhizobium has one thick flagellum and several thin flagella; the Bradyrhizobium protein in this cluster is associated with the thick flagellum NP_949251.1 post-transcriptional repressor of flagellum biosynthesis; promotes degradation of fljK mRNA; Bradyrhizobium has one thick and several thin flagella, the Bradyrhizobium protein in this cluster is associated with the thin flagella NP_949252.1 structural flagella protein; Bradyrhizobium has one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagellum NP_949266.1 structural flagella protein; Bradyrhizobium has one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagellum NP_949267.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949268.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949269.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949270.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949274.1 this stereospecific enzymes reduces the R isomer of methionine sulfoxide while MsrA reduces the S form; provides protection against oxidative stress NP_949284.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949286.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949287.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949291.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949293.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949295.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949297.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949298.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949308.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949310.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949311.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949312.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949313.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949315.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949316.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949320.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949321.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949324.1 catalyzes the isomerization of sedoheptulose 7-phosphate to D-glycero-D-manno-heptose 7-phosphate NP_949328.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949329.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949330.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949338.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949339.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949351.1 catalyzes the formation of L-homocysteine from S-adenosyl-L-homocysteine NP_949352.1 methionine adenosyltransferase; catalyzes the formation of S-adenosylmethionine from methionine and ATP; methionine adenosyltransferase NP_949354.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949355.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949360.1 catalyzes the formation of tetrahydropteroyl-L-glutamate and methionine from L-homocysteine and 5-methyltetrahydropteroyltri-L-glutamate NP_949365.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949368.1 produces formate from formyl-tetrahydrofolate which is the major source of formate for PurT in de novo purine nucleotide biosynthesis; has a role in one-carbon metabolism; forms a homohexamer; activated by methionine and inhibited by glycine NP_949370.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949374.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949378.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949381.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949384.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949385.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949386.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949388.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949389.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949390.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949392.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949393.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949405.1 this stereospecific enzymes reduces the R isomer of methionine sulfoxide while MsrA reduces the S form; provides protection against oxidative stress NP_949406.2 this stereospecific enzymes reduces the S isomer of methionine sulfoxide while MsrB reduces the R form; provides protection against oxidative stress NP_949407.1 four CarB-CarA dimers form the carbamoyl phosphate synthetase holoenzyme that catalyzes the production of carbamoyl phosphate; CarB is responsible for the amidotransferase activity NP_949408.1 necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites; arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus NP_949412.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949413.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949418.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949428.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949437.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949441.1 Citation: Gonzalez-Pasayo and Martinez-Romero (2000) Mol. Plant Microbe Interact. 13:572-577 NP_949442.1 Citation: Gonzalez-Pasayo and Martinez-Romero (2000) Mol. Plant Microbe Interact. 13:572-577 NP_949446.1 in group A Streptococci this protein was found to cross react with anti myosin antibodies and may play a role in rheumatic fever NP_949454.1 type IV secretion VirB6 family NP_949457.1 type IV secretion system VirB4 family NP_949465.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949466.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949468.1 type IV secretion VirD4 coupling protein family NP_949472.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949473.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949474.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949483.1 catalyzes the formation of thymine and 2-deoxy-alpha-D-ribose 1-phosphate from thymidine NP_949484.1 Catalyzes the formation of PRPP from ATP and ribose 5-phosphate NP_949485.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949488.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949491.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949492.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949496.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949506.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949507.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949509.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949510.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949511.1 With PurE catalyzes the conversion of aminoimidazole ribonucleotide to carboxyaminoimidazole ribonucleotide in the de novo purine nucleotide biosynthetic pathway NP_949512.1 a small basic protein that is one of the last in the subunit assembly; omission does not prevent assembly but the subunit is inactive; binds central domain of 16S rRNA NP_949514.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949515.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949516.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949518.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949521.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949524.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949526.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949527.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949529.1 catalyzes the formation of phosphoenolpyruvate from pyruvate NP_949530.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949533.1 smallest protein in the large subunit; similar to what is found with protein L31 and L33 several bacterial genomes contain paralogs which may be regulated by zinc; the protein from Thermus thermophilus has a zinc-binding motif and contains a bound zinc ion; the proteins in this group do not have the motif NP_949534.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949536.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949542.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949544.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949545.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949547.1 catalyzes the formation of glutamate from glutamine NP_949549.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949550.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949552.1 catalyzes the formation of malate from glyoxylate and acetyl-CoA NP_949553.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949556.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949559.1 in Caulobacter crescentus, CC3477 is differentially expressed in minimal salts media with glucose as compared to complex media NP_949560.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949561.1 Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription NP_949566.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949572.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949575.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949577.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949580.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949581.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949583.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949584.1 response regulator for histidine kinase FixL; part of global network that controls expression of aerobic respiratory terminal oxidases and carbon and nitrogen metabolic enzymes NP_949585.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949586.1 transcriptional regulator that positively regulated fixLJ operon; upregulated transcription by FixJ; part of global network that controls expression of aerobic respiratory terminal oxidases and carbon and nitrogen metabolic enzymes NP_949587.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949593.1 Catalyzes the transfer of electrons from NADH to quinone NP_949595.1 Catalyzes the transfer of electrons from NADH to quinone NP_949597.1 Catalyzes the transfer of electrons from NADH to quinone NP_949598.1 NuoCD; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain; subunits NuoCD, E, F, and G constitute the peripheral sector of the complex; in Escherichia coli this gene encodes a fusion protein of NuoC and NuoD that are found separate in other organisms NP_949599.1 The point of entry for the majority of electrons that traverse the respiratory chain eventually resulting in the reduction of oxygen NP_949601.1 responsible for transport of beta-1,2-glucans from the cytoplasm to periplasm; inner membrane ABC transporter permease component; Cgt; ChvA; NdvA NP_949602.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949603.1 activates fatty acids by binding to coenzyme A NP_949604.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949605.1 An endonuclease that specifically degrades the RNA strand of RNA-DNA hybrids NP_949606.1 catalyzes the formation of O-phospho-L-homoserine from L-homoserine NP_949607.1 catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP); functions in the nonmevalonate isoprenoid biosynthesis pathway NP_949608.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949620.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949622.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949630.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949631.1 catalyzes the formation of N6-(1,2,-dicarboxyethyl)-AMP from L-aspartate, inosine monophosphate and GTP in AMP biosynthesis NP_949632.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949638.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949642.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949644.1 catalyzes the formation of 3-phosphonooxypyruvate from 3-phospho-D-glycerate in serine biosynthesis; can also reduce alpha ketoglutarate to form 2-hydroxyglutarate NP_949645.1 catalyzes the formation of 3-phosphonooxypyruvate and glutamate from O-phospho-L-serine and 2-oxoglutarate NP_949647.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949654.1 catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate NP_949656.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949657.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949661.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949664.1 EF-G; promotes GTP-dependent translocation of the ribosome during translation; many organisms have multiple copies of this gene NP_949665.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949666.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949667.1 catalyzes the formation of oxalozcetate and L-glutamate from L-aspartate and 2-oxoglutarate NP_949671.1 unwinds double stranded DNA NP_949672.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949675.1 Catalyzes the reversible hydration of unsaturated fatty acyl-CoA to beta-hydroxyacyl-CoA NP_949679.1 The UvrABC repair system catalyzes the recognition and processing of DNA lesions. The beta-hairpin of the Uvr-B subunit is inserted between the strands, where it probes for the presence of a lesion NP_949682.1 Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation NP_949683.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949685.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949687.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949688.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949690.1 translation-associated GTPase; the crystal structure of the Haemophilus influenzae YchF protein showed similarity to the yeast structure (PDB: 1NI3); fluorescence spectroscopy revealed nucleic acid binding; the yeast protein YBR025c interacts with the translation elongation factor eEF1 NP_949691.1 Enables the recycling of peptidyl-tRNAs produced at termination of translation NP_949692.1 the Ctc family of proteins consists of two types, one that contains the N-terminal ribosomal protein L25 domain only which in Escherichia coli binds the 5S rRNA while a subset of proteins contain a C-terminal extension that is involved in the stress response NP_949693.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949694.1 transfers the N-acyl diglyceride moiety to the prospective N-terminal cysteine in prolipoprotein NP_949696.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949698.1 catalyzes the formation of 5-phospho-alpha-D-ribose 1-phosphate from D-ribose 5-phosphate and ATP NP_949699.1 RibE; 6,7-diimethyl-8-ribityllumazine synthase; DMRL synthase; lumazine synthase; beta subunit of riboflavin synthase; condenses 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate to generate 6,6-dimethyl-8-lumazine (DMRL); riboflavin synthase then uses 2 molecules of DMRL to produce riboflavin (vitamin B12); involved in the last steps of riboflavin biosynthesis; forms a 60mer (icosahedral shell) in both Bacillus subtilis and Escherichia coli; in Bacillus subtilis this 60mer is associated with the riboflavin synthase subunit (alpha) while in Escherichia coli it is not NP_949702.1 catalyzes the formation of L-proline from pyrroline-5-carboxylate NP_949704.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949706.1 catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids NP_949707.1 This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. Promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex NP_949709.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949710.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949711.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949712.1 lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis NP_949713.1 IleRS; catalyzes the formation of isoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile); since isoleucine and other amino acids such as valine are similar, there are additional editing function in this enzyme; one is involved in hydrolysis of activated valine-AMP and the other is involved in deacylation of mischarged Val-tRNA(Ile); there are two active sites, one for aminoacylation and one for editing; class-I aminoacyl-tRNA synthetase family; some organisms carry two different copies of this enzyme NP_949715.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949717.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949724.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949725.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949729.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949730.1 Catalyzes the first step in the glyoxalate cycle, which converts lipids to carbohydrates NP_949731.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949732.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949733.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949734.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949739.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949740.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949746.1 in Escherichia coli this homodimeric enzyme is expressed under aerobic conditions; anaerobic expression is repressed by the arcAB system; converts sn-glycerol-3-phosphate and ubiquinone-8 to dihydroxy acetone phosphate and ubiquinol-8; associates with the cytoplasmic membrane NP_949754.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949755.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949757.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949760.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949761.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949763.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949768.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949769.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949773.1 Catalyzes the conversion of acetyl-CoA and L-homoserine to CoA and O-acetyl-L-homoserine NP_949775.1 catalyzes the formation of L-histidinol phosphate from imidazole-acetol phosphate and glutamate in histidine biosynthesis NP_949776.1 dual function enzyme catalyzes the formation of 4-hydroxyphenylpyruvate from prephenate and the formation of tyrosine from arogenate NP_949777.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949778.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949779.1 activates fatty acids by binding to coenzyme A NP_949784.1 Member of the extracytoplasmic function sigma factors which are active under specific conditions; binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription NP_949785.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949792.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949793.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949796.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949799.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949800.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949802.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949803.1 with SoxZ catalyzes the oxidation of sulfur compounds NP_949804.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949805.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949806.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949812.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949815.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949817.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949823.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949825.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949828.1 catalyzes a salvage reaction resulting in the formation of AMP which is metabolically less costly than a de novo synthesis NP_949830.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949832.1 trpE(G); catalyzes the formation of anthranilate from chorismate and glutamine; contains both component I and II NP_949835.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949836.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949838.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949844.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949847.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949849.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949861.1 Maf; overexpression in Bacillus subtilis inhibits septation in the dividing cell NP_949865.1 catalyzes the oxidation of L-histidinol to L-histidinaldehyde and then to L-histidine in histidine biosynthesis; functions as a dimer NP_949867.1 adds enolpyruvyl to UDP-N-acetylglucosamine as a component of cell wall formation; gram-positive bacteria have 2 copies of MurA which are active NP_949885.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949890.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949895.1 catalyzes the NADPH-dependent deamination of GMP to inosine monophosphate NP_949901.1 Catalyses the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate NP_949902.1 Catalyzes a key regulatory step in fatty acid biosynthesis NP_949903.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949912.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949914.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949921.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949924.1 catalyzes the formation of O-succinyl-L-homoserine from succinyl-CoA and L-homoserine in methionine biosynthesis NP_949926.1 activates fatty acids by binding to coenzyme A; may be involved in acyclic terpene utilization NP_949927.1 catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids NP_949929.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949930.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949932.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949934.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949936.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949937.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949938.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949939.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949940.1 associates with NifD and may protect the nitrogenase Fe-Mo protein from oxidative damage NP_949941.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949942.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949944.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949946.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949947.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949948.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949949.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949950.1 functions with NifE to assemble FeMo cofactor; functions in assembly of nitrogenase MoFe NP_949951.1 functions with NifN to assemble FeMo cofactor; functions in assembly of nitrogenase MoFe NP_949952.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949953.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949954.1 nitrogenase iron protein; nitrogenase component 2; with component 1, an molybdenum-iron protein, catalyzes the fixation of nitrogen to ammonia; nitrogen reductase provides electrons to the nitrogenase complex; in R. etli there are three essentially identical copies of nifH which are actively expressed during symbiosis NP_949957.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949958.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949960.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949964.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949965.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949966.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949967.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949972.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949973.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949975.1 catalyzes the carboxylation of D-ribulose 1,5-bisphosphate in carbon dioxide fixation NP_949976.1 class II aldolase; catalyzes the reversible aldol condensation of dihydroxyacetonephosphate and glyceraldehyde 3-phosphate in the Calvin cycle, glycolysis and gluconeogenesis NP_949977.1 catalyzes the formation of ribose 5-phosphate and xylulose 5-phosphate from sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate; can transfer ketol groups between several groups; in Escherichia coli there are two tkt genes, tktA expressed during exponential growth and the tktB during stationary phase NP_949978.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949979.1 catalyzes the formation of D-fructose 6-phosphate from fructose-1,6-bisphosphate NP_949980.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949982.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949985.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949988.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949990.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949992.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_949997.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950000.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950001.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950002.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950003.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950006.1 An oxygenase that acts to open the ring of homogentisate formingmaleylacetoacetate as part of the catabolism of L-tyrosine and L-phenylalanine NP_950018.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950019.1 class I; LysRS1; catalyzes a two-step reaction, first charging a lysine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Methanosarcina barkeri this enzyme charges both tRNA molecules for lysine that exist in this organism (but the tRNALysUUU very poorly) and in the presence of LysRS2 can charge tRNAPyl with lysine NP_950025.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950026.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950032.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950035.1 extradiol catechol dioxygenase that catalyzes the oxidative cleavage of substituted catechols; part of the bacterial aromatic compound degradation pathway NP_950036.1 extradiol catechol dioxygenase that catalyzes the oxidative cleavage of substituted catechols; part of the bacterial aromatic compound degradation pathway NP_950037.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950042.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950048.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950051.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950053.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950055.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950056.1 undetermined function NP_950057.1 has 3'-5' exonuclease, 5'-3' exonuclease and 5'-3'polymerase activities, primarily functions to fill gaps during DNA replication and repair NP_950058.1 involved in fifth step of pyrimidine biosynthesis; converts orotidine 5'-phosphate and diphosphate to orotate and 5-phospho-alpha-D-ribose 1-diphosphate NP_950064.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950065.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950072.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950077.1 catalyzes the formation of arginine from (N-L-arginino)succinate NP_950082.1 converts (S)-3-hydroxybutanoyl-CoA to 3-acetoacetyl-CoA NP_950083.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950084.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950085.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950088.2 this tRNA synthetase lacks the tRNA anticodon interaction domain; instead this enzyme modifies tRNA(Asp) with glutamate by esterifying glutamate to the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of queosine generating a modified nucleoside at the first anticodon position of tRNAAsp; the modified tRNA does not bind elongation factor Tu NP_950090.1 Inhibits transcription at high concentrations of nickel NP_950094.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950099.1 Catalyzes the deamination of dCTP to form dUTP NP_950100.1 catalyzes the conversion of O-succinylhomoserine and sulfide to homocysteine; second step in methionine biosynthesis NP_950101.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950104.1 protein associated with Co2+ and Mg2+ efflux NP_950105.1 becomes active under oxidative stress; four conserved cysteines bind a zinc atom when they are in the reduced state and the enzyme is inactive; oxidative stress results in oxidized cysteines, release of zinc, and binding of Hsp33 to aggregation-prone proteins; forms dimers and higher order oligomers NP_950106.1 catalyzes the formation of L-citrulline from carbamoyl phosphate and L-ornithine in arginine biosynthesis and degradation NP_950107.2 DapATase; functions in arginine biosynthetic pathway; catalyzes the formation of N-acetyl-L-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine NP_950108.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950110.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950111.1 ATP-binding protein; PstABCS is an ATP dependent phosphate uptake system which is responsible for inorganic phosphate uptake during phosphate starvation NP_950114.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950118.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950120.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950121.1 consists of N-terminal helix-turn-helix domain and C-terminal shikimate kinase-like domain which may bind benzoyl-CoA; controls inducible expression of the bzd catabolic operon that is involved in the anaerobic catabolism of benzoate NP_950124.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950125.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950126.1 Bacteria have multiple sigma factors which are active under specific conditions; the sigma factor binds with the catalytic core of RNA polymerase to produce the holoenzyme and directs bacterial core RNA polymerase to specific promoter elements to initiate transcription NP_950130.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950131.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950132.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950133.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950141.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950147.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950149.1 molecular chaperone NP_950154.1 isomerizes methylthioribose-1-phosphate into methylthioribulose-1-phosphate; involved in methionine salvage pathway NP_950155.1 Catalyzes the reversible phosphorolysis of 5'-deoxy-5'- methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1- phosphate NP_950156.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950157.1 activates fatty acids by binding to coenzyme A NP_950163.1 observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished NP_950168.1 this stereospecific enzymes reduces the S isomer of methionine sulfoxide while MsrB reduces the R form; provides protection against oxidative stress NP_950170.1 binds directly to the 16S rRNA and is involved in post-translational inhibition of arginine and ornithine decarboxylase NP_950204.1 similar to plasmid encoded restriction endonuclease from Rhizobium leguminosarun VF39SM (Rochepeau et al., Mol. Gen. Genet. 256:387-396 (1997)) NP_950205.1 64% identity to plasmid encoded restriction methylase from Rhizobium leguminosarun VF39SM (Rochepeau et al., Mol. Gen. Genet. 256:387-396 (1997)) NP_950206.1 IPR006119 Resolvase, N-terminal, residues 2-137; IPR006120 Resolvase helix-turn-helix domain, residues 139-183, 43% identity to Q83SV1 DNA-invertase from Salmonella typhi NP_950207.1 35% identity to Q9AGT5 homocitrate synthase from Rhizobium meliloti