-- dump date 20140620_000513 -- class Genbank::CDS -- table cds_note -- id note NP_892122.1 binds the polymerase to DNA and acts as a sliding clamp NP_892124.1 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_892125.1 Catalyzes first step of the de novo purine nucleotide biosynthetic pathway NP_892130.1 Regulates rRNA biosynthesis by transcriptional antitermination NP_892133.1 catalyzes the formation of arginine from (N-L-arginino)succinate NP_892138.1 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_892142.1 catalyzes the reduction of UDP-N-acetylglucosamine enolpyruvate to form UDP-N-acetylmuramate in peptidoglycan biosynthesis NP_892144.1 Citation: AJ245541; Mol Biol Evol 2001 Dec;18(12):2240-2249. NP_892145.1 Citation: Webb and Downs (1997) J. Biol. Chem. 272:15702-15707 NP_892147.1 Involved in peptide bond synthesis; alters the affinity of the ribosome for aminoacyl-tRNA NP_892149.1 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_892156.1 BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT AMINOTRANSFERASES NP_892157.1 Catalyzes the methylation of C-1 in cobalt-precorrin-5 and the subsequent extrusion of acetic acid from the resulting intermediate to form cobalt-precorrin-6A NP_892158.1 contains glutamine-hydrolyzing domain and glutamine amidotransferase; GMP-binding domain; functions to produce GMP from XMP in the IMP pathway NP_892165.1 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_892166.1 catalyzes the formation of agmatine from arginine in putrescine and spermidine biosynthesis NP_892167.1 catalyzes the formation of nucleoside triphosphate from ATP and nucleoside diphosphate NP_892168.1 Citation: Mirand-Rios et al. (1997) J. Bacteriol. 179:6887-6893 NP_892169.1 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_892170.1 catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A; involved in coenzyme A biosynthesis NP_892171.1 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_892181.1 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_892185.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892189.1 cleaves off formyl group from N-terminal methionine residues of newly synthesized proteins; binds iron(2+) NP_892194.1 with SufCD activates cysteine desulfurase SufS NP_892197.1 catalyzes the interconversion of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate NP_892200.1 peroxiredoxin (Prx) family; thio-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family protein; Citation: Kong et al. (2000) Biochem. J. 351:107-114. NP_892202.1 catalyzes the reduction of 3'-phosphoadenylyl sulfate into sulfite NP_892214.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892221.1 assignment YP_654186.1 Ycf7; cytochrome b6-f complex subunit 6 NP_892228.1 catalyzes the formation of shikimate 3-phosphate from shikimate in aromatic amino acid biosynthesis NP_892250.1 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_892251.1 catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to thymidine monophosphate (dTMP) to form thymidine diphosphate (dTDP) NP_892254.1 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_892256.1 involved in acylation of glycerol-3-phosphate to form 1-acyl-glycerol-3 phosphate for use in phospholipid biosynthesis; functions with PlsY NP_892257.1 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_892262.1 Citation: Kushner (2002) J. Bacteriol. 184:4658-4665 NP_892270.1 Catalyzes the transfer of electrons from NADH to ubiquinone NP_892271.1 Shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain NP_892277.1 catalyzes the phosphorylation of NAD to NADP NP_892278.1 Catalyzes the transfer of electrons from NADH to quinone NP_892279.1 Catalyzes the transfer of electrons from NADH to quinone NP_892280.1 Catalyzes the transfer of electrons from NADH to quinone NP_892281.1 Catalyzes the transfer of electrons from NADH to quinone NP_892282.1 catalyzes the formation of citrate from acetyl-CoA and oxaloacetate NP_892285.1 catalyzes the formation of L-tryptophan from L-serine and 1-(indol-3-yl)glycerol 3-phosphate NP_892289.1 catalyzes the formation of Mg-protoporphyrin IX methyl ester and S-adenosyl-L-homocysteine from Mg-protoporphyrin IX and S-adenosyl-L-methionine NP_892293.1 shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain; couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradien NP_892297.1 catalyzes the formation of dimethylmenaquinone from 1,4-dihydroxy-2-naphthoate NP_892299.1 catalyzes the second step in the glutathione biosynthesis pathway, where it synthesizes ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione NP_892301.1 recognizes the termination signals UGA 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 RF2; in some organisms control of PrfB protein levels is maintained through a +1 ribosomal frameshifting mechanism; this protein is similar to release factor 1 NP_892305.1 CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kapland and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410 NP_892307.1 conserved hypothetical assignment NP_892308.1 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_892310.1 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_892315.1 essential GTPase; functions in ribosome assembly; binds a unique part of the 23S rRNA; interacts with ribosomal protein L25(Ctc) NP_892316.1 Converts 3-phospho-D-glycerate to 3-phospho-D-glyceroyl phosphate during the glycolysis pathway NP_892319.1 Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979 NP_892320.1 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_892322.1 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_892323.1 binds the two ribosomal protein L7/L12 dimers and anchors them to the large ribosomal subunit NP_892324.1 in Escherichia coli and Methanococcus, this protein autoregulates expression; the binding site in the mRNA mimics the binding site in the 23S rRNA NP_892325.1 binds directly to 23S ribosomal RNA NP_892326.1 Modulates Rho-dependent transcription termination NP_892327.1 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_892329.1 enolase; catalyzes the formation of phosphoenolpyruvate from 2-phospho-D-glycerate in glycolysis NP_892334.1 Citation: Shibata M, Katoh H, Sonoda M, Ohkawa H, Shimoyama M, Fukuzawa H, Kaplan A, Ogawa T (2002) J. Biol. Chem. 277:18658-18644 NP_892336.1 catalyzes the formation of porphobilinogen from 5-aminolevulinate NP_892339.1 essential GTPase; exhibits high exchange rate for GTP/GDP; associates with 50S ribosomal subunit; involved in regulation of chromosomal replication YP_654187.1 CP12 domain-containing protein NP_892342.1 catalyzes the conversion of N-acetyl_L-aspartic acid (NAA) to aspartate and acetate NP_892344.1 catalyzes the formation of chorismate from 5-O-(1-carboxyvinyl)-3-phosphoshikimate in aromatic amino acid biosynthesis NP_892349.1 he dfp (coaBC) gene codes for a bifunctional protein that catalyzes two sequential reactions in the pantothenate and coenzyme A biosynthetic pathway. The two activities are p-pantothenate cysteine ligase and p-pantothenenoylcysteine decarboxylase.; Citation: Strauss et al. (2001) J. Biol. Chem. 276:13513-13516 NP_892353.1 catalyzes the transfer of the carbamoyl moiety from carbamoyl phosphate to L- aspartate in pyrimidine biosynthesis NP_892355.1 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_892357.1 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 type 1 subfamily; some organisms carry two different copies of this enzyme NP_892359.1 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_892362.1 flavin dependent thymidylate synthase; ThyX; thymidylate synthase complementing protein; catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate; the enzyme from Mycobacterium tuberculosis forms homotetramers; uses FAD as a cofactor NP_892363.1 Catalyzes the formation of dUTP from dCTP in thymidylate biosynthesis NP_892369.1 Enables the recycling of peptidyl-tRNAs produced at termination of translation NP_892370.1 may be involved in regulating PSII assembly and/or stability NP_892372.1 4.8-kDa protein; may be involved in assembling and stabilizing of PSII dimers NP_892375.1 dehydratase component, catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate NP_892377.1 catalyzes the reaction of glycine with 5,10-methylenetetrahydrofolate to form L-serine and tetrahydrofolate NP_892381.1 Regulatory factor involved in maltose metabolism NP_892383.1 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_892385.1 involved in de novo purine biosynthesis NP_892389.1 Citation: Roth et al. (1993) J. Bacteriol. 175:3303-3316 NP_892390.1 Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr) NP_892391.1 may be involved in binding plastoquinone and maintaining PSII dimers NP_892398.1 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_892400.1 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_892401.1 NADH-dependent; catalyzes a key regulatory step in fatty acid biosynthesis NP_892403.1 Members of the DegT/DnrJ/EryC1/StrS family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. NP_892406.1 Citation: Talarico et al. (1992) J. Bacteriol. 174:5971-5977 NP_892411.1 catalyzes the transfer of electrons from NADH to quinones NP_892412.1 The point of entry for the majority of electrons that traverse the respiratory chain eventually resulting in the reduction of oxygen NP_892413.1 Catalyzes the transfer of electrons from NADH to quinone NP_892415.1 similar to Arabidopsis thaliana photosystem II assembly protein NP_892416.1 photosystem II reaction center subunit VI; associated with the reaction center of photosystem II NP_892417.1 photosystem II reaction center subunit VI; associated with the reaction center of photosystem II NP_892418.1 may have a role in PSII core assembly, maintaining PSII dimers and donor side electron transfer NP_892419.1 may be involved in assembling and maintaining PSII complexes in the thylakoid membrane NP_892430.1 methionine adenosyltransferase; catalyzes the formation of S-adenosylmethionine from methionine and ATP; methionine adenosyltransferase NP_892431.1 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_892433.1 Ycf8; may be involved in the formation and/or stabilization of PSII system complexes NP_892439.1 works in conjunction with MinC and MinD to enable cell division at the midpoint of the long axis of the cell NP_892444.1 electron transport protein NP_892445.1 PetD, with cytochrome b6, cytochrome F, and the Rieske protein, makes up the large subunit of the cytochrome b6-f complex; cytochrome b6-f mediates electron transfer between photosystem II and photosystem I NP_892447.1 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_892448.1 Stabilizes the interaction between PsaC and the photosystem I core NP_892462.1 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_892464.1 possible thiol peroxidase NP_892477.1 Citation: Peterson and Downs (1997) J. Bacteriol. 179:4894-4900 NP_892492.1 catalyzes the reaction of cyanate and bicarbonate to produce ammonia and carbon dioxide NP_892505.1 catalyzes the formation of 3-dehydroshikimate from 3-dehydroquinate in chorismate biosynthesis NP_892507.1 Cobalamin biosynthesis; Citation: Crouzet et al. (1990) J. Bacteriol. 172:5980-5990; Roth et al. (1993) J. Bacteriol. 175:3303-3316 NP_892509.1 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_892519.1 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_892523.1 Catalyzes the transfer of acetyl from acetyldihydrolipoamide to coenzyme A to form acetyl CoA NP_892528.1 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_892531.1 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_892533.1 Citation: Leibrecht and Kessler (1997) J. Biol. Chem. 272:10442-10447 NP_892537.2 malate dehydrogenase; catalyzes the oxidation of malate to oxaloacetate NP_892538.1 binds to the ribosome on the universally-conserved alpha-sarcin loop NP_892544.1 In E. coli, Sun (Fmu) protein is a small subunit (16S) ribosomal RNA methyltransferase.; Citation: Gu et al. (1999) Biochemistry 38:4053-4057 NP_892548.1 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_892551.1 Citation: Howard et al. (1985) Gene 35:321-331 NP_892553.1 transfers electrons from NAD(P)H to quinons in the respiratory chain NP_892554.1 catalyzes the ATP-dependent breakage of single-stranded DNA followed by passage and rejoining, maintains net negative superhelicity NP_892560.1 catalyzes the formation of riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine NP_892566.1 converts protoheme IX and farnesyl diphosphate to heme O NP_892570.1 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 expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is not essential for growth NP_892572.1 4-diphosphocytidyl-2C-methyl-D-erythritol synthase; MEP cytidylyltransferase; MCT; catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate; involved in isoprenoid and isopentenyl-PP biosynthesis; forms homodimers NP_892574.1 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_892577.1 Citation: Crouzet et al. (1990) J. Bacteriol. 172:5980-5990; Debussche et al. (1993) J. Bacteriol. 175:7430-7440 NP_892578.1 transfers the N-acyl diglyceride moiety to the prospective N-terminal cysteine in prolipoprotein NP_892579.1 cytochrome f, with cytochrome b6, subunit IV, and the Rieske protein, makes up the large subunit of the cytochrome b6-f complex; cytochrome b6-f mediates electron transfer between photosystem II and photosystem I NP_892580.1 Rieske protein, with cytochrome b6, cytochrome f, and subunit IV, makes up the large subunit of the cytochrome b6-f complex; cytochrome b6-f mediates electron transfer between photosystem II and photosystem I NP_892585.1 Essential for recycling GMP and indirectly, cGMP NP_892586.1 Enables the organization of the psaE and psaF subunits NP_892588.1 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_892589.1 has EXXNGXXAXXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892591.1 Charges one glutamine molecule and pairs it to its corresponding RNA trinucleotide during protein translation NP_892593.1 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_892595.1 catalyzes the removal of N-terminal amino acids from peptides and arylamides; generally Co(II) however activity has been shown for some methionine aminopeptidases with Zn, Fe, or Mnin Bacillus subtilis the protein in this cluster is considered non-essential NP_892599.1 nucleotide binding property based on structural studies of Haemophilus influenzae crystallized protein in PDB Accession Number 1IN0 and NMR studies of Escherichia coli YajQ; the YajQ protein from Pseudomonas synringae appears to play a role in activation of bateriophage phi6 segment L transcription NP_892601.1 Converts (S)-4-amino-5-oxopentanoate to 5-aminolevulinate during the porphyrin biosynthesis pathway NP_892609.1 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_892613.1 transformation of porphobilinogen to hydroxymethylbilane in porphyrin biosynthesis NP_892614.1 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_892617.1 catalyzes the phosphorylation of N-acetyl-L-glutamate to form N-acetyl-L-glutamate 5-phosphate NP_892624.1 catalyzes the formation of N6-(1,2,-dicarboxyethyl)-AMP from L-aspartate, inosine monophosphate and GTP in AMP biosynthesis NP_892626.1 catalyzes the formation of prolyl-tRNA(Pro) from proline and tRNA(Pro) NP_892633.1 phosphatase involved in the assembly of the nucleotide loop of cobalamin; Citation: O'Toole et al. (1994) J. Biol. Chem. 269:26503-26511 NP_892637.1 Maintains the balance of metabolites in the pentose-phosphate pathway NP_892639.1 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_892640.1 Catalyzes the phosphorylation of UMP to UDP NP_892641.1 Citation: Lundrigan and Kadner (1989) J. Bacteriol. 171:154-161; Fonseca and Escalente-Semerena (2001) J. Biol. Chem. 276:32101-32108 NP_892642.1 in addition to BLAST hits ... contains the applicable subsitutions in the R-H-R-Y motif identified by Nunes-Duby et al 1998 NP_892643.1 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_892644.1 catalyzes the formation of 2-acetolactate from pyruvate; also known as acetolactate synthase large subunit NP_892648.1 Citation: Sugita, C., Sugiura, M. & Sugita, M. (2000) Mol. Gen. Genet. 263:655-663 NP_892652.1 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_892654.1 Citation: Katzenmeier et al. (1991) Biol. Chem. Hoppe-Seyler 372:991-997 NP_892660.1 Converts chlorophyllide a into protochlorophyllide; light dependent NP_892661.1 light-independent; with chlN(bchN) and chlB(bchB) reduces ring D of protochlorophyllide to form chlorophyllide a in chlorophyll/bacteriochlorophyll production NP_892662.1 light-independent reduction of protochlorophyllide to form chlorophyllide a NP_892663.1 light-independent reduction of protochlorophyllide to form chlorophyllide a NP_892668.1 type III RuBisCO; involved in carbon fixation NP_892678.1 short form of enzyme; requires HisZ for function; catalyzes the formation of N'-5'-phosphoribosyl-ATP from phosphoribosyl pyrophosphate; crucial role in histidine biosynthesis; forms heteromultimer of HisG and HisZ NP_892683.1 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_892687.1 catalyzes the formation of N-carbamoyl-L-aspartate from (S)-dihydroorotate in pyrimidine biosynthesis NP_892688.1 essential for inorganic carbon transport in Synechocystis PCC6803 NP_892690.1 catalyzes the formation of indole and glyceraldehyde 3-phosphate from indoleglycerol phosphate in tryptophan biosynthesis NP_892692.1 unknown function; YciI from Haemophilus influenzae has a crystal structure similar to a muconolactone isomerase, but does not seem to catalyze any of the reactions predicted from the sequence or structure similarity NP_892695.1 alternative sigma factor NP_892696.1 catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribosyl)-ATP and the subsequent formation of 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide from 1-(5-phosphoribosyl)-AMP in histidine biosynthesis NP_892699.1 participates in electron transfer in photosystem I NP_892701.1 catalyzes the formation of coproporphyrinogen from uroporphyrinogen III NP_892702.1 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_892708.1 Catalyzes the phosphorylation of L-glutamate during the proline biosynthesis pathway NP_892709.1 Citation: Haussmann et al. (1998) J. Biol. Chem. 273:17418-17424 NP_892712.2 shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain; subunit D, with NdhB and NdhF are core membrane components NP_892713.1 catalyzes the formation of O-phospho-L-homoserine from L-homoserine in threonine biosynthesis from asparate NP_892715.1 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_892716.1 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_892726.1 catalyzes the formation of 1,4-dihydroxy-2-naphthoate from O-succinylbenzoyl-CoA NP_892727.1 catalyzes the formation of alpha-1,4-glucan chains from ADP-glucose NP_892728.1 assignment NP_892729.1 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_892731.1 catalyzes the formation of 5-O-(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate and 3-phosphoshikimate in tryptophan biosynthesis NP_892732.1 catalyzes the formation of (2R)-3-sulfolactate from (2R)-2-phospho-3-sulfolactate NP_892741.1 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_892745.1 Citation: La Roche et al. (1996) Proc, Natl. Acad. Sci. USA 93:15244-15248 NP_892779.1 Citation: Gleason and Olszewski (2002) J. Bacteriol. 184:6544-6550 NP_892781.1 stimulates the release of release factors 1 and 2 from the ribosome after hydrolysis of the ester bond in peptidyl-tRNA has occurred; GDP/GTP-binding protein NP_892783.1 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_892786.1 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_892792.1 possible role in phosphonate metabolism NP_892794.1 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_892796.1 3 different subfamilies; catalyzes the formation of quinolinate from iminoaspartate and dihydroxyacetone phosphate NP_892800.1 catalyzes the formation of 3-dehydroquinate from 3-deoxy-arabino-heptulonate 7-phosphate; functions in aromatic amino acid biosynthesis NP_892801.1 With PurE catalyzes the conversion of aminoimidazole ribonucleotide to carboxyaminoimidazole ribonucleotide in the de novo purine nucleotide biosynthetic pathway NP_892807.1 has EXXNGXXAMXG motif; Citation: Bahya, D. et al. 2002. Analysis of the hli gene family in marine and freshwater cyanobacteria FEMS Microbiol Lett In Press NP_892808.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892843.1 ATP-binding protein; PstABCS is an ATP dependent phosphate uptake system which is responsible for inorganic phosphate uptake during phosphate starvation NP_892847.1 catalyzes the ATP-dependent formation of a phosphodiester at the site of a single strand break in duplex DNA NP_892858.1 subunit VIII; plays a crucial role in complex assembly and/or stability; with PetL, PetG and PetM makes up the small subunit of the cytochrome b6-f complex; cytochrome b6-f mediates electron transfer between photosystem II and photosystem I NP_892859.1 Psb29; involved in biogenesis of the photosystem II; in Arabidopsis it interacts with the heterotrimeric G-protein (GPA1) and seems to be involved in a D-glucose signaling mechanism between plastid and the plasma membranes NP_892860.1 hydrolyzes proteins to small peptides; with the ATPase subunits ClpA or ClpX, ClpP degrades specific substrates; in Synechococcus this protein (ClpP1)is constitutive and levels increased with the increase of light. NP_892861.1 Synechocystis sp. PCC6803 ortholog (slr0228) involved in PSI biogenesis.; Citation: Mann et al. (2000) FEBS Lett. 479:72-77 NP_892865.1 catalyzes the reduction of biliverdin IX-alpha producing (3Z)-phycocyanobilin and oxidized ferredoxin NP_892871.1 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_892872.1 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_892874.1 catalyzes branch migration in Holliday junction intermediates NP_892876.1 hemoprotein; NADPH dependent; with the alpha subunit (a flavoprotein) catalyzes the reduction of sulfite to sulfide NP_892885.1 type II fructose 1,6-bisphosphatae; in Escherichia coli this protein forms a dimer and binds manganese NP_892886.1 catalyzes the formation of glutamate-1-semialdehyde from glutamyl-tRNA(Glu) and NADPH; the second step of the pathway is catalyzed by glutamate-1-semialdehyde aminomutase which results in the formation of 5-aminolevulinic acid; functions in porphyrin (tetrapyrroles) biosynthesis; the crystal structure showed a C-terminal dimerization domain that appears to be absent in Chlamydial proteins NP_892887.1 catalyzes the formation of ADP-glucose and diphosphate from ATP and alpha-D-glucose 1-phosphate NP_892888.1 catalyzes the formation of D-ribulose 5-phosphate from 6-phospho-D-gluconate NP_892892.1 catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis NP_892898.1 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_892899.1 class II aldolase; catalyzes the reversible aldol condensation of dihydroxyacetonephosphate and glyceraldehyde 3-phosphate in the Calvin cycle, glycolysis and gluconeogenesis NP_892902.1 catalyzes the carboxylation of acetyl-CoA to malonyl-CoA; forms a tetramer of AccA2D2 subunits NP_892904.1 catalyzes the oxidation of 3-isopropylmalate to 3-carboxy-4-methyl-2-oxopentanoate in leucine biosynthesis NP_892905.1 adds the O-linked and N-linked 3(R)-hydroxy fatty acids to the glucosamine disaccharide during lipid A biosynthesis NP_892906.1 catalyzes the formation of glutamate 5-phosphate from glutamate in proline biosynthesis NP_892914.1 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_892933.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892934.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892935.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892936.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_892947.2 Reversibly isomerizes the ketone sugar dihydroxyacetone phosphate to the aldehyde sugar glyceraldehyde-3-phosphate NP_892948.1 Citation: Dallas et al. (1992) J. Bacteriol. 174:5961-5970 NP_892949.1 catalyzes the formation of Mg-protoporphyrin IX from protoporphyrin IX and Mg(2+); first committed step of chlorophyll biosynthesis NP_892950.1 catalyzes the reduction of 2,3-dihydrodipicolinate to 2,3,4,5-tetrahydrodipicolinate in lysine and diaminopimelate biosynthesis NP_892962.1 oxidative; catalyzes the formation of divinylprotochlorophyllide from magnesium-protoporphyrin IX 13-monomethyl ester in isocyclic ring formation in chlorophyll biosynthesis NP_892965.1 Citation: Beuf et al. (1995) Plant Mol. Biol. 27:779-788 NP_892971.1 some L32 proteins have zinc finger motifs consisting of CXXC while others do not NP_892981.1 Citation: O'Toole and Excalante-Semerena (1995) J. Biol. Chem. 270:23560-23569; Thomas et al. (2000) J. Biol. Chem. 275:27576-27586 NP_892985.1 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_892987.1 binds as a heterodimer with protein S6 to the central domain of the 16S rRNA; helps stabilize the platform of the 30S subunit NP_892988.1 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_892989.1 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_892995.1 B-12 dependent isozyme NP_892996.1 catalyzes the transamination of the branched-chain amino acids to their respective alpha-keto acids NP_892997.1 Citation: Crouzet et al. (1991) J. Bacteriol. 173:6074-6087 NP_893000.1 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_893002.1 Catalyzes the conversion of ATP and pantetheine 4'-phosphate to diphosphate and 3'-dephospho-coA NP_893006.1 involved in lysine biosynthesis; DAP epimerase; produces DL-diaminopimelate from LL-diaminopimelate NP_893007.1 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_893008.1 functions in sugar metabolism in glycolysis and the Embden-Meyerhof pathways (EMP) and in gluconeogenesis; catalyzes reversible isomerization of glucose-6-phosphate to fructose-6-phosphate; member of PGI family NP_893010.1 catalyzes the reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde in arginine biosynthesis and the reduction of N-acetyl-gamma-aminoadipyl-phosphate to N-acetyl-L-aminoadipate-semialdehyde in lysine biosynthesis; involved in both the arginine and lysine biosynthetic pathways; lysine is produced via the AAA pathway, lysine from alpha-aminoadipate NP_893011.1 bifunctional enzyme DHBP synthase/GTP cyclohydrolase II; functions in riboflavin synthesis; converts GTP to 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine; converts ribulose 5-phopshate to 3,4-dihydroxy-2-butanone 4-phosphate; note this protein has an additional C-terminal tail of unknown function as compared to similar bifunctional enzymes NP_893015.1 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_893018.1 May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine NP_893019.1 molecular chaperone NP_893020.1 required for 70S ribosome assembly NP_893025.1 catalyzes the formation of 1-deoxy-D-xylulose 5-phosphate from pyruvate and D-glyceraldehyde 3-phosphate NP_893026.1 threonine deaminase; threonine dehydratase; in Escherichia coli, IlvA is part of the isoleucine biosynthetic pathway NP_893030.1 catalyzes the formation of phosphoenolpyruvate from pyruvate NP_893033.1 lipoprotein signal peptidase; integral membrane protein that removes signal peptides from prolipoproteins during lipoprotein biosynthesis NP_893037.1 Class-V aminotransferase NP_893043.1 catalyzes the selenophosphate-dependent transfer of selenium from selenophosphate for conversion of 2-thiouridine to 2-selenouridine at the wobble position in tRNA NP_893044.1 PsbW; part of the phosystem II reaction center NP_893046.1 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_893047.1 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_893050.1 catalyzes the phosphorylation of 4-diphosphocytidyl-2-C-methyl-D-erythritol in the nonmevalonate pathway of isoprenoid biosynthesis NP_893051.1 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_893057.1 synthesizes RNA primers at the replication forks NP_893061.1 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_893063.1 catalyzes DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time; main replicative polymerase NP_893064.1 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 YP_654188.1 antagonist of anti-sigma factor RsbW NP_893068.1 catalyzes production of carbamoyl phosphate from bicarbonate and glutamine in pyrimidine and arginine biosynthesis pathways; forms an octamer composed of four CarAB dimers NP_893069.1 Catalyzes the conversion of N-(5-phospho-D-ribosyl)-anthranilate and diphosphate to anthranilate and 5-phospho-alpha-D-ribose 1-diphosphate NP_893077.1 catalyzes the hydrolysis of mannosyl-3-phosphoglycerate to form the osmolyte mannosylglycerate NP_893080.1 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_893081.1 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_893082.1 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_893083.1 Citation: Paulinska et al. (2000) Microbiology 146:3099-3107 NP_893084.1 involved in the assembly of the urease metallocenter; possible nickel donor NP_893085.1 Citation: Palinska et al. (2000) Microbiology 146:3099-3107 NP_893086.1 Citation: Palinska et al. (2000) Microbiology 146:3099-3107 NP_893087.1 NtcA binding site of form GTTN8TACN22TAN3T beginning 93 bases upstream of start point; Citation: Valladares, A, ML Montesinos, A. Herrero, E. Flores (2002) Mol. Microbiol. 43:703-715 NP_893088.1 Citation: Valladares, A, ML Montesinos, A. Herrero, E. Flores (2002) Mol. Microbiol. 43:703-715 NP_893089.1 Citation: Valladares, A, ML Montesinos, A. Herrero, E. Flores (2002) Mol. Microbiol. 43:703-715 NP_893090.1 Citation: Valladares, A, ML Montesinos, A. Herrero, E. Flores (2002) Mol. Microbiol. 43:703-715 NP_893091.1 Citation: Valladares, A, ML Montesinos, A. Herrero, E. Flores (2002) Mol. Microbiol. 43:703-715 NP_893104.1 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_893121.1 non-folate utilizing enzyme, catalyzes the production of beta-formyl glycinamide ribonucleotide from formate, ATP, and beta-GAR and a side reaction producing acetyl phosphate and ADP from acetate and ATP; involved in de novo purine biosynthesis NP_893168.1 catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine NP_893171.1 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_893175.1 cytochrome b6-f complex subunit 5; plastohydroquinone/plastocyanin oxidoreductase; with PetL, PetM and PetN makes up the small subunit of the cytochrome b6-f complex; cytochrome b6-f mediates electron transfer between photosystem II and photosystem I NP_893176.1 has F-G-G motif of methylases NP_893177.1 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_893179.1 catalyzes the synthesis of xanthosine monophosphate by the NAD+ dependent oxidation of inosine monophosphate NP_893180.1 negatively supercoils closed circular double-stranded DNA NP_893183.1 catalyzes the formation of 2-isopropylmalate from acetyl-CoA and 2-oxoisovalerate in leucine biosynthesis NP_893186.1 catalyzes the formation of 5,10-methenyltetrahydrofolate from 5,10-methylenetetrahydrofolate and subsequent formation of 10-formyltetrahydrofolate from 5,10-methenyltetrahydrofolate NP_893189.1 BELONGS TO THE SIRTUIN FAMILY; Citation: Tsang and Escalante-Semerena (1996) J. Bacteriol. 178:7016-7019 NP_893191.1 catalyzes the formation of D-glucono-1,5-lactone 6-phosphate from D-glucose 6-phosphate NP_893194.1 interacts with the circadian clock regulator KaiC to maintain circadian rhythms NP_893197.1 catalyzes the formation of 5-phospho-alpha-D-ribose 1-phosphate from D-ribose 5-phosphate and ATP NP_893198.1 amylomaltase; acts to release glucose from maltodextrins NP_893201.1 possible assignment NP_893205.1 regulatory subunit of ATP-dependent Clp protease NP_893207.1 assignment NP_893209.1 catalyzes the formation of undecaprenyl pyrophosphate from isopentenyl pyrophosphate NP_893210.1 Citation: Otsuka et al. (1988) J. Biol. Chem. 263:19577-19585 NP_893213.1 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_893214.1 involved in a recombinational process of DNA repair, independent of the recBC complex NP_893224.1 involved in the de novo synthesis of pyridoxine (Vitamin B6) NP_893233.1 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_893234.1 component of photosystem II; manganese-binding polypeptide with arginine metablolizing activity NP_893235.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893239.1 catalyzes a salvage reaction resulting in the formation of AMP which is metabolically less costly than a de novo synthesis NP_893245.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893252.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893255.1 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_893257.1 has 3'-5' exonuclease, 5'-3' exonuclease and 5'-3'polymerase activities, primarily functions to fill gaps during DNA replication and repair NP_893258.1 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_893259.1 catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate YP_654190.1 Ycf31; cytochrome b6-f complex subunit 7; with PetL, PetG and PetN makes up the small subunit of the cytochrome b6-f complex; cytochrome b6-f mediates electron transfer between photosystem II and photosystem I NP_893271.1 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_893273.1 required for the assembly of photosystem I complex NP_893275.1 Citation: Garczarek et al. (2001) Plant Mol. Biol. 46:683-693 NP_893277.1 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_893282.1 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_893288.1 An electron-transfer protein; flavodoxin binds one FMN molecule, which serves as a redox-active prosthetic group NP_893298.1 conserved hypothetical assignment NP_893300.1 in Escherichia coli transcription of this gene is enhanced by polyamines NP_893303.1 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_893305.1 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_893307.1 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_893380.1 catalyzes the formation of L-citrulline from carbamoyl phosphate and L-ornithine in arginine biosynthesis and degradation NP_893382.1 Citation: Richter et al. (1997) J. Bacteriol. 179:2022-2028 NP_893385.1 Citation: Blanche et al. (1992) J. Bacteriol. 174:1050-1052 NP_893386.1 catalyzes the phosphorylation of NAD to NADP NP_893387.1 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_893388.1 catalyzes the conversion of a phosphate monoester to an alcohol and a phosphate NP_893390.1 Citation: Gupta et al. (1999) FEMS Microbiol Lett 179:501-506 NP_893391.1 catalyzes the formation of thiamine monophosphate from 4-methyl-5-(beta-hydroxyethyl)-thiazole monophosphate and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate NP_893398.1 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_893402.1 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_893406.1 Type II alternative sigma factor NP_893408.1 catalyzes a sulfuration reaction to synthesize 2-thiouridine at the U34 position of tRNAs NP_893409.1 possible assignment NP_893414.1 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_893415.1 E3 component of pyruvate complex; catalyzes the oxidation of dihydrolipoamide to lipoamide NP_893417.1 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_893418.1 catalyzes the formation of N-acetyl-l-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine NP_893419.1 Citation: Bogner et al. (1987) J. Biol. Chem. 262:12337-12343 NP_893422.1 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_893423.1 D-alanine--D-alanine ligase; DdlA; DdlB; cytoplasmic; catalyzes the formation of D-alanyl-D-alanine from two D-alanines in peptidoglycan synthesis; there are two forms of this enzyme in Escherichia coli NP_893426.1 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_893427.1 catalyzes the formation of tetrahydrofolate and 2-dehydropantoate from 5,10-methylenetetrahydrofolate and 3-methyl-2-oxobutanoate NP_893430.1 ClpR variant present in an operon with ClpP3 in Synechococcus PCC7942; ClpR is missing the catalytic triad Ser-His-Asp characteristic of serine-type proteases; the exact function of ClpR and ClpP3 is unknown however they appear to be necessary for cell viability; hydrolyzes proteins to small peptides; with the ATPase subunits ClpA or ClpX, ClpP degrades specific substrates NP_893431.1 hydrolyzes proteins to small peptides; with the ATPase subunits ClpA or ClpX, ClpP degrades specific substrates NP_893432.1 catalyzes the formation of (R)-2,3-dihydroxy-3-methylbutanoate from (S)-2-hydroxy-2-methyl-3-oxobutanoate in valine and isoleucine biosynthesis NP_893433.1 Citation: Crouzet et al. (1990) J. Bacteriol. 172:5968-5979 NP_893434.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893446.1 catalyzes the formation of tyrosyl-tRNA(Tyr) from tyrosine and tRNA(Tyr) NP_893449.1 catalyzes the removal of N-terminal amino acids preferably leucine from various peptides NP_893451.1 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_893452.1 catalyzes the addition of (R)-3-hydroxytetradecanoyl to the glucosamine disaccharide in lipid A biosynthesis NP_893453.1 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_893454.1 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_893456.1 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_893459.1 acts as a promotor non-specific transcription repressor NP_893460.1 Decreases the phosphorylation of KaiC, a component of the main circadian regulator in cyanobacteria NP_893462.1 involved in the peptidyltransferase reaction during translation NP_893470.1 methylates ribosomal protein L11 at multiple amino acid positions; mutations of these genes in Escherichia coli or Thermus thermophilus has no apparent phenotype NP_893471.1 catalyzes the formation of 3-phosphonooxypyruvate from 3-phospho-D-glycerate in serine biosynthesis; can also reduce alpha ketoglutarate to form 2-hydroxyglutarate NP_893481.1 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_893501.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893502.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893507.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893513.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893514.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893515.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893516.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893521.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893548.1 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_893550.1 regulates pyrimidine biosynthesis by binding to the mRNA of the pyr genes, also has been shown to have uracil phosphoribosyltransferase activity NP_893551.1 catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate NP_893553.1 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 expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth NP_893554.1 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_893555.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. The beta chain is a regulatory subunit NP_893556.1 part of catalytic core of ATP synthase; alpha(3)beta(3)gamma(1)delta(1)epsilon(1); involved in producing ATP from ADP in the presence of the proton motive force across the membrane NP_893562.1 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_893567.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is a regulatory subunit NP_893568.1 produces ATP from ADP in the presence of a proton gradient across the membrane; the alpha chain is a catalytic subunit NP_893569.1 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_893570.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit B' is part of the membrane proton channel. NP_893571.1 Produces ATP from ADP in the presence of a proton gradient across the membrane. Subunit B is part of the membrane proton channel. NP_893572.1 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_893573.1 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_893577.1 Citation: Inoue et al. (1997) J. Biol. Chem. 272:31747-31754 NP_893578.1 NADPH-dependent; catalyzes the reduction of 7-cyano-7-deazaguanine to 7-aminomethyl-7-deazaguanine in queuosine biosynthesis NP_893582.1 Catalyzes two discrete reactions in the de novo synthesis of purines: the cleavage of adenylosuccinate and succinylaminoimidazole carboxamide ribotide NP_893583.1 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_893585.1 Citation: Otsuka et al. (1988) J. Biol. Chem. 263:19577-19585; Alexeev et al. (1998) J. Mol. Biol. 284:401-419 NP_893587.1 possible SAM-dependent methyltransferase NP_893588.1 Citation: Otsuka et al. (1988) J. Biol. Chem. 263:19577-19585; Yang et al. (1997) Biochemistry 36:4751-4760 NP_893589.1 Citation: Otsuka et al. (1988) J. Biol. Chem. 263:19577-19585; Kack et al. (1999) J. Mol. Biol. 291:857-876 NP_893592.1 Citation: Romanowski et al. (2002) Proteins 47:563-567 NP_893598.1 23S rRNA m2A2503 methyltransferase; methylates the C2 position of the A2530 nucleotide in 23S rRNA; may be involved in antibiotic resistance NP_893599.1 has EXXNGXXAMXG motif; Citation: Bhaya et al. (2002) FEMS Microbiol Lett 215:209-219 NP_893600.1 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_893601.1 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates NP_893602.1 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_893604.1 binds directly to the 16S rRNA and is involved in post-translational inhibition of arginine and ornithine decarboxylase NP_893605.1 catalyzes the oxidation of L-histidinol to L-histidinaldehyde and then to L-histidine in histidine biosynthesis; functions as a dimer NP_893606.1 Catalyzes D-ribose 5-phosphate --> D-ribulose 5-phosphate in the nonoxidative branch of the pentose phosphate pathway NP_893609.1 modifies transcription through interactions with RNA polymerase affecting elongation, readthrough, termination, and antitermination NP_893611.1 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_893616.1 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_893617.1 catalyzes the interconversion of tetrahydrodipicolinate and L,L-diaminopimelate in lysine biosynthesis NP_893619.1 RNH2; RNase HII; binds manganese; endonuclease which specifically degrades the RNA of RNA-DNA hybrids NP_893621.1 assignment NP_893624.1 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_893625.1 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_893626.1 EF-G; promotes GTP-dependent translocation of the ribosome during translation; many organisms have multiple copies of this gene NP_893627.1 binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit NP_893628.1 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_893631.1 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_893637.1 Citation: van de Staay et al. (1998) Photosynthesis Research 57:183-191 NP_893640.1 with PsaA binds the primary electron donor of photosystem I, P700, and subsequent electron acceptors as part of photosystem I NP_893641.1 with PsaB binds the primary electron donor of photosystem I, P700, and subsequent electron acceptors as part of photosystem I NP_893642.1 Citation: Debussche et al. (1993) J. Bacteriol. 175:7430-7440; Roth et al. (1993) J. Bacteriol. 175:3303-3316 NP_893644.1 converts L-alanine to D-alanine which is used in cell wall biosynthesis; binds one pyridoxal phosphate per monomer; forms a homodimer NP_893646.1 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_893647.1 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_893648.1 forms a direct contact with the tRNA during translation NP_893649.1 in Escherichia coli this protein is one of the earliest assembly proteins in the large subunit NP_893650.1 mediates pseudouridylation (positions 38, 39, 40) at the tRNA anticodon region which contributes to the structural stability NP_893651.1 is a component of the macrolide binding site in the peptidyl transferase center NP_893652.1 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_893653.1 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_893654.1 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_893655.1 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 have the motif NP_893657.1 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_893658.1 late assembly protein NP_893659.1 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_893660.1 binds 5S rRNA along with protein L5 and L25 NP_893661.1 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_893662.1 binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit NP_893663.1 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_893664.1 assembly initiator protein; binds to 5' end of 23S rRNA and nucleates assembly of the 50S; surrounds polypeptide exit tunnel NP_893665.1 binds to the 23S rRNA between the centers for peptidyl transferase and GTPase NP_893666.1 primary binding protein; helps mediate assembly; involved in translation fidelity NP_893667.1 one of the stabilizing components for the large ribosomal subunit NP_893668.1 located in the peptidyl transferase center and may be involved in peptidyl transferase activity; similar to archaeal L10e NP_893669.1 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_893670.1 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_893671.1 protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA NP_893672.1 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_893673.1 binds third domain of 23S rRNA and protein L29; part of exit tunnel NP_893674.1 L4 is important during the early stages of 50S assembly; it initially binds near the 5' end of the 23S rRNA NP_893675.1 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_893679.1 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_893682.1 catalyzes the formation of tyrosine from arogenate NP_893686.1 BELONGS TO THE HESA/MOEB/THIF FAMILY; Citation: Nohno et al (1988) J. Bacteriol. 170:4097-4102 NP_893687.1 catalyzes the formation of adenosylcob(III)yrinic acid a,c-diamide from cob(I)yrinic acid a,c-diamide NP_893689.1 Decarboxylation of S-adenosylmethionine provides the aminopropyl moiety required for spermidine biosynthesis from putrescine NP_893692.1 catalyzes the formation of oxaloacetate from phosphoenolpyruvate NP_893694.1 definite assignment NP_893699.1 catalyzes the conversion of the propionic acid groups of rings I and III to vinyl groups during heme synthesis NP_893706.1 catalyzes the formation of 1-(5-phosphoribosyl)-5-aminoimidazole from 2-(formamido)-N1-(5-phosphoribosyl)acetamidine and ATP in purine biosynthesis NP_893707.1 catalyzes the formation of pantothenate from pantoate and beta-alanine and the formation of cytidine diphosphate from cytidine monophosphate NP_893709.1 catalyzes the reduction of 15,16-dihydrobiliverdin to (3Z)-phycoerythrobilin NP_893710.1 catalyzes the reduction of biliverdin IX-alpha to 15,16-dihydrobiliverdin NP_893713.1 Converts isocitrate to alpha ketoglutarate NP_893722.1 Essential for efficient processing of 16S rRNA NP_893723.1 Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source NP_893724.1 part of the core of the reaction center of photosystem I NP_893725.1 carries the fatty acid chain in fatty acid biosynthesis NP_893727.1 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_893728.1 required for the synthesis of the hydromethylpyrimidine moiety of thiamine NP_893732.1 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_893733.1 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_893735.1 class II; LysRS2; 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, LysRS2 charges both tRNA molecules for lysine that exist in this organism and in addition can charge the tRNAPyl with lysine in the presence of LysRS1 NP_893738.1 in some organisms this protein is a transmembrane protein while in others it is periplasmic; involved in some organisms with other components of the MreBCD complex and with penicillin binding proteins in the periplasm or cell wall NP_893739.1 functions in MreBCD complex in some organisms NP_893740.1 binds to single stranded DNA and may facilitate the binding and interaction of other proteins to DNA NP_893742.1 catalyzes the formation of L-homocysteine from S-adenosyl-L-homocysteine NP_893746.1 Type II alternative sigma factor NP_893751.1 negatively supercoils closed circular double-stranded DNA NP_893752.1 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_893753.1 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_893756.1 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; in some organisms, there are paralogous proteins that have been found to be nonessential but do function in secretion of a subset of exported proteins NP_893760.1 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_893762.1 This protein performs the mismatch recognition step during the DNA repair process NP_893763.1 Citation: Thibaut et al. (1992) J. Bacteriol. 174:1043-1049 NP_893764.1 required for the assembly and function of the DNAX complex which are required for the assembly of the beta subunit onto primed DNA NP_893765.1 catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP NP_893766.1 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_893770.1 catalyzes the formation of dihydrodipicolinate from L-aspartate 4-semialdehyde and pyruvate in lysine and diaminopimelate biosynthesis NP_893771.1 assignment NP_893772.1 Tig; RopA; peptidyl-prolyl cis/trans isomerase; promotes folding of newly synthesized proteins; binds ribosomal 50S subunit; forms a homodimer NP_893774.1 binds and unfolds substrates as part of the ClpXP protease NP_893779.1 binds directly to 23S ribosomal RNA prior to in vitro assembly of the 50S ribosomal subunit NP_893781.1 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_893785.1 acts in conjunction with GvcH to form H-protein-S-aminomethyldihydrolipoyllysine from glycine NP_893786.1 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_893790.1 in Escherichia coli this protein is wrapped around the base of the L1 stalk NP_893791.1 similar to Nostoc sp. PCC7120 (Q8YZA1|DNAB_ANASP) dnaB and Synechocystis sp. PCC6803 (Q55418|DNAB_SYNY3) dnaB but does NOT contain an intein. NP_893792.1 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_893799.1 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_893801.1 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_893802.1 catalyzes the formation of spermidine from putrescine and S-adenosylmethioninamine NP_893804.1 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_893805.1 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_893806.1 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_893809.1 Citation: Goncharodd and Nichols (1984) J. Bacteriol. 159:57-62 NP_893810.1 hypothetical aminotransferase NP_893811.1 2 S-ADENOSYL-L-METHIONINE + UROPORPHYRIN III = 2 S-ADENOSYL-L-HOMOCYSTEINE + SIROHYDROCHLORIN; Citation: Crouzet et al. (199) J. Bacteriol. 172:5968-5979; Blanche et al. (1989) J. Bacteriol. 171:4222-4231 (1989) NP_893813.1 catalyzes the reversible transfer of the terminal phosphate of ATP to form a long chain polyphosphate NP_893814.1 alternative sigma factor NP_893816.1 catalyzes the formation of 3-deoxy-D-arabino-hept-2-ulosonate 7 phosphate from phosphoenolpyruvate and D-erythrose 4-phosphate, phenylalanine sensitive NP_893817.1 catalyzes the conversion of citrate to isocitrate and the conversion of 2-methylaconitate to 2-methylisocitrate NP_893819.1 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_893821.1 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_893822.1 AroE; catalyzes the conversion of shikimate to 3-dehydroshikimate NP_893823.1 binds cooperatively with S18 to the S15-16S complex, allowing platform assembly to continue with S11 and S21 NP_893824.1 catalyzes the formation of 2-N(omega)-(L-arginino)succinate from L-citrulline and L-aspartate in arginine biosynthesis, AMP-forming NP_893826.1 First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan NP_893829.1 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_893830.1 MAY BE INVOLVED IN RECOMBINATIONAL REPAIR OF DAMAGED DNA NP_893833.1 catalyzes the formation of L-threonine from O-phospho-L-homoserine