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| | cheB | Protein-glutamate methylesterase/protein-glutamine glutaminase; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Catalyzes its own deactivation by removing the activating phosphoryl group. Belongs to the CheB family. (349 aa) |
| | cheR | Chemotaxis regulator, protein-glutamate methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (286 aa) |
| | cheA | Chemotaxis protein CheA; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. (654 aa) |
| | yedK | DUF159 family protein; Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA. May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). (222 aa) |
| | hchA | Protein/nucleic acid deglycase 1; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, [...] (283 aa) |
| | yedV | Putative sensory kinase in two-component regulatory system with YedW; Member of a two-component regulatory system HprR/HprS involved in response to hydrogen peroxide. Senses H(2)O(2), maybe via the redox state of the membrane. Activates HprR by phosphorylation. Can also phosphorylate CusR. (452 aa) |
| | mtfA | Anti-repressor for DgsA(Mlc); Involved in the regulation of ptsG expression by binding and inactivating Mlc; Belongs to the MtfA family. (265 aa) |
| | ldtA | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp; Belongs to the YkuD family. (310 aa) |
| | yeeS | CP4-44 prophage; Putative DNA repair protein, RADC family; Belongs to the UPF0758 family. (148 aa) |
| | dacD | D-alanyl-D-alanine carboxypeptidase; Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family. (388 aa) |
| | wzzB | Regulator of length of O-antigen component of lipopolysaccharide chains; Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules; Belongs to the WzzB/Cld/Rol family. (326 aa) |
| | wzc | Colanic acid production tyrosine-protein kinase; Required for the extracellular polysaccharide colanic acid synthesis. The autophosphorylated form is inactive. Probably involved in the export of colanic acid from the cell to medium. Phosphorylates udg. (720 aa) |
| | wzb | Colanic acid production protein-tyrosine-phosphatase; Dephosphorylates Wzc. Required for the extracellular polysaccharide colanic acid synthesis, probably involved in the export of colanic acid from the cell to medium. Involved in protection of cells against contact- dependent growth inhibition (CDI), probably due to the loss of a physical impediment to cell-cell contact; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. (147 aa) |
| | yegI | Protein kinase-related putative non-specific DNA-binding protein; Probable serine/threonine kinase. (648 aa) |
| | yegK | Ser/thr phosphatase-related protein; PP2C-like phosphatase that can dephosphorylate YegI. In vitro, can hydrolyze p-nitrophenyl phosphate (pNPP) to p-nitrophenol. (253 aa) |
| | baeS | Sensory histidine kinase in two-component regulatory system with BaeR; Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress. Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression. Activates BaeR by phosphorylation which then activates the mdtABCD and probably the CRISPR-Cas casABCDE-ygbT-ygbF operons. (467 aa) |
| | yegQ | Putative peptidase; Belongs to the peptidase U32 family. (453 aa) |
| | yehU | Inner membrane putative sensory kinase in two-component system with YehT; Member of the two-component regulatory system BtsS/BtsR, which is part of a nutrient-sensing regulatory network composed of BtsS/BtsR, the low-affinity pyruvate signaling system YpdA/YpdB and their respective target proteins, BtsT and YhjX. Responds to depletion of nutrients, specifically serine, and the concomitant presence of extracellular pyruvate. BtsS is a high-affinity receptor for extracellular pyruvate that activates BtsR by phosphorylation. Activation of the BtsS/BtsR signaling cascade also suppresses Yp [...] (561 aa) |
| | pbpG | D-alanyl-D-alanine endopeptidase; Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD- diaminopimelate-alanine bonds in high-molecular-mass murein sacculi; Belongs to the peptidase S11 family. (310 aa) |
| | mepS | Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds. Partially suppresses a prc disruption mutant. Belongs to the peptidase C40 family. (188 aa) |
| | ccmH | Heme lyase, CcmH subunit; May be required for the biogenesis of c-type cytochromes. Possible subunit of a heme lyase. (350 aa) |
| | rcsD | Phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Component of the Rcs signaling system, which controls transcription of numerous genes. RcsD is a phosphotransfer intermediate between the sensor kinase RcsC and the response regulator RcsB. It acquires a phosphoryl group from RcsC and transfers it to RcsB. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division. (890 aa) |
| | rcsC | Hybrid sensory kinase in two-component regulatory system with RcsB and YojN; Component of the Rcs signaling system, which controls transcription of numerous genes. RcsC functions as a membrane- associated protein kinase that phosphorylates RcsD in response to environmental signals. The phosphoryl group is then transferred to the response regulator RcsB. RcsC has also phosphatase activity. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division. (949 aa) |
| | atoS | Sensory histidine kinase in two-component regulatory system with AtoC; Member of the two-component regulatory system AtoS/AtoC. In the presence of acetoacetate, AtoS/AtoC stimulates the expression of the atoDAEB operon, leading to short chain fatty acid catabolism and activation of the poly-(R)-3-hydroxybutyrate (cPHB) biosynthetic pathway. Also induces the operon in response to spermidine. Involved in the regulation of motility and chemotaxis, via transcriptional induction of the flagellar regulon. AtoS is a membrane-associated kinase that phosphorylates and activates AtoC in response [...] (608 aa) |
| | yfaL | Adhesin; Probably an autotransporter. (1250 aa) |
| | elaD | Protease, capable of cleaving an AMC-ubiquitin model substrate; Protease that can act as an efficient and specific deubiquitinating enzyme in vitro. Does not possess desumoylating and deneddylating activities. The physiological substrate is unknown. (403 aa) |
| | yfbL | Putative aminopeptidase. (323 aa) |
| | mepA | Murein DD-endopeptidase; Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. (274 aa) |
| | dnaJ | Chaperone Hsp40, DnaK co-chaperone; Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. 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. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK t [...] (376 aa) |
| | lspA | Prolipoprotein signal peptidase (signal peptidase II); This protein specifically catalyzes the removal of signal peptides from prolipoproteins. (164 aa) |
| | fkpB | FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln. (149 aa) |
| | surA | Peptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis. (428 aa) |
| | ftsI | Transpeptidase involved in septal peptidoglycan synthesis; Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum. Required for localization of FtsN. Belongs to the transpeptidase family. FtsI subfamily. (588 aa) |
| | aceF | Pyruvate dehydrogenase, dihydrolipoyltransacetylase component E2; 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 (E3). (630 aa) |
| | mrcB | Fused glycosyl transferase and transpeptidase; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits); In the N-terminal section; belongs to the glycosyltransferase 51 family. (844 aa) |
| | degP | Serine endoprotease (protease Do), membrane-associated; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. [...] (474 aa) |
| | glnD | Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. (890 aa) |
| | map | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. (264 aa) |
| | rseP | Inner membrane zinc RIP metalloprotease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue 'Val-148' of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamas [...] (450 aa) |
| | yaeF | Putative lipoprotein. (274 aa) |
| | yafK | L,D-transpeptidase-related protein. (246 aa) |
| | yafL | Putative lipoprotein and C40 family peptidase; Putative lipoprotein. (249 aa) |
| | pepD | Cytosol non-specific dipeptidase; Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source. (485 aa) |
| | pepP | Proline aminopeptidase P II. (441 aa) |
| | loiP | Phe-Phe periplasmic metalloprotease, OM lipoprotein; Metalloprotease that cleaves substrates preferentially between Phe-Phe residues. Plays a role in response to some stress conditions. Seems to regulate the expression of speB. (252 aa) |
| | pppA | Bifunctional prepilin leader peptidase/ methylase; A pre-pilin peptidase involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane. (269 aa) |
| | hybD | Maturation protease for hydrogenase 2; Protease involved in the C-terminal processing of HybC, the large subunit of hydrogenase 2. Specifically cleaves off a 15 amino acid peptide from the C-terminus of the precursor of HybC; Belongs to the peptidase A31 family. (164 aa) |
| | qseC | Quorum sensing sensory histidine kinase in two-component regulatory system with QseB; Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation. (449 aa) |
| | glnE | Fused deadenylyltransferase/adenylyltransferase for glutamine synthetase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N- terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signa [...] (946 aa) |
| | yhbO | Stress-resistance protein; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phospha [...] (172 aa) |
| | ftsH | Protease, ATP-dependent zinc-metallo; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] (644 aa) |
| | dacB | D-alanyl-D-alanine carboxypeptidase; Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction. Belongs to the peptidase S13 family. (477 aa) |
| | arcB | Aerobic respiration control sensor protein ArcB; Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576. (778 aa) |
| | degQ | Serine endoprotease, periplasmic; DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP. (455 aa) |
| | degS | Serine endoprotease, periplasmic; A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors deal [...] (355 aa) |
| | tldD | Putative peptidase; Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA). Belongs to the peptidase U62 family. (481 aa) |
| | prmA | Methyltransferase for 50S ribosomal subunit protein L11; Methylates ribosomal protein L11. (293 aa) |
| | gspO | Bifunctional prepilin leader peptidase/ methylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue. (225 aa) |
| | fkpA | FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (270 aa) |
| | slyD | FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] (196 aa) |
| | ppiA | Peptidyl-prolyl cis-trans isomerase A (rotamase A); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (190 aa) |
| | mrcA | Penicillin-binding protein 1a, murein transglycosylase and transpeptidase; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits); In the N-terminal section; belongs to the glycosyltransferase 51 family. (850 aa) |
| | envZ | Sensory histidine kinase in two-component regulatory system with OmpR; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes. EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription. Also dephosphorylates OmpR in the presence of ATP. The cytoplasmic dimerization domain (CDD) forms an osmosensitive core; increa [...] (450 aa) |
| | glpG | Rhomboid protease GlpG; Rhomboid-type serine protease that catalyzes intramembrane proteolysis. (276 aa) |
| | ggt | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] (580 aa) |
| | prlC | Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). (680 aa) |
| | gor | Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (450 aa) |
| | yhjJ | Putative periplasmic M16 family chaperone; Belongs to the peptidase M16 family. (498 aa) |
| | yiaC | GNAT family putative N-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility. (146 aa) |
| | grxC | Glutaredoxin 3; The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. (83 aa) |
| | envC | Activator of AmiB,C murein hydrolases, septal ring factor; Activator of the cell wall hydrolases AmiA and AmiB. Required for septal murein cleavage and daughter cell separation during cell division. In vitro, exhibits weak endoproteolytic activity on beta- casein. (419 aa) |
| | yicR | UPF0758 family protein; DNA repair protein; Protein involved in DNA-dependent DNA replication and DNA repair; Belongs to the UPF0758 family. YicR subfamily. (222 aa) |
| | uhpB | Sensory histidine kinase in two-component regulatory sytem with UhpA; Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. UhpB functions as a membrane-associated protein kinase that autophosphorylates in response to interaction with UhpC, and subsequently transfers its phosphate group to the response regulator UhpA. Can also dephosphorylate UhpA. (500 aa) |
| | yifB | Magnesium chelatase family protein and putative transcriptional regulator; Putative 2-component regulator; Belongs to the Mg-chelatase subunits D/I family. ComM subfamily. (506 aa) |
| | ppiC | Peptidyl-prolyl cis-trans isomerase C (rotamase C); PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates; Belongs to the PpiC/parvulin rotamase family. (93 aa) |
| | trxA | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. (109 aa) |
| | wzzE | Entobacterial Common Antigen (ECA) polysaccharide chain length modulation protein; Modulates the polysaccharide chain length of enterobacterial common antigen (ECA). Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)). (348 aa) |
| | ubiB | Regulator of octaprenylphenol hydroxylation, ubiquinone synthesis; Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. Belongs to the ABC1 family. UbiB subfamily. (546 aa) |
| | pepQ | Proline dipeptidase; Splits dipeptides with a prolyl residue in the C-terminal position and a polar or nonpolar amino acid at the N-terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX. (443 aa) |
| | srkA | Cpx stress response Thr/Ser protein kinase; A protein kinase that (auto)phosphorylates on Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Protects cells from stress by antagonizing the MazE-MazF TA module, probably indirectly as it has not been seen to phosphorylate MazE, MazF or MazG. Probably involved in the extracytoplasmic stress response. (328 aa) |
| | dsbA | Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily. (208 aa) |
| | glnL | Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC. (349 aa) |
| | frvX | Putative peptidase; Frv operon protein; Protein involved in polysaccharide catabolic process. (356 aa) |
| | cpxA | Sensory histidine kinase in two-component regulatory system with CpxR; Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA. Activates CpxR by phosphorylation; has autokinase, phosphotransferase and (in the presence of Mg(2+) and/or ATP or ADP) phosphatase activity. The kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition. Involved in several diverse cellular processes, including the functi [...] (457 aa) |
| | hslU | Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. (443 aa) |
| | hslV | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. [...] (176 aa) |
| | birA | Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. (321 aa) |
| | thiF | Adenylyltransferase, modifies ThiS C-terminus; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS; Belongs to the HesA/MoeB/ThiF family. (251 aa) |
| | zraS | Sensory histidine kinase in two-component regulatory system with ZraR; Member of the two-component regulatory system ZraS/ZraR. May function as a membrane-associated protein kinase that phosphorylates ZraR in response to high concentrations of zinc or lead in the medium. (465 aa) |
| | yjaB | GNAT-family putative N-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Binds acetyl-CoA ; Belongs to the acetyltransferase family. (147 aa) |
| | aceK | Isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation; Belongs to the AceK family. (578 aa) |
| | pepE | Peptidase E, alpha-aspartyl dipeptidase; Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids; Belongs to the peptidase S51 family. (229 aa) |
| | lexA | Transcriptional repressor of SOS regulon; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single- stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment .The SOS response controls an apoptotic-like death (ALD) induced (in the absence [...] (202 aa) |
| | acs | acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. (652 aa) |
| | phnO | Aminoalkylphosphonate N-acetyltransferase; Aminoalkylphosphonate N-acetyltransferase which is able to acetylate a range of aminoalkylphosphonic acids, including aminomethylphosphonate, (S)-1-aminoethylphosphonate and 2- aminoethyl- and 3-aminopropylphosphonate, using acetyl-CoA as acetyl donor. Is required for the utilization of aminomethylphosphonate and (S)-1-aminoethylphosphonate as a phosphate source via the C-P lyase pathway. Is also essential for the detoxification of (S)-1- aminoethylphosphonate, a structural analog of D-alanine that has bacteriocidal properties due to inhibitio [...] (144 aa) |
| | basS | Sensory histidine kinase in two-component regulatory system with BasR; Member of the two-component regulatory system BasS/BasR Autophosphorylates and activates BasR by phosphorylation. (363 aa) |
| | dcuS | Sensor histidine kinase DcuS; Member of the two-component regulatory system DcuR/DcuS. Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4- dicarboxylate transporter dctA. Activates DcuR by phosphorylation. (543 aa) |
| | dsbD | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. (565 aa) |
| | epmA | Elongation Factor P Lys34 lysyltransferase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta- lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF- P 'Lys-34'. The substrate (R)-beta-lysine is 100-fold more efficient than either (S)-beta-lysine or L-alpha-lysine. Cannot ligate lysine to any tRNA. (325 aa) |
| | tsaE | tRNA(ANN) t(6)A37 threonylcarbamoyladenosine modification protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. Displays ATPase activity in vitro. (153 aa) |
| | yjfP | Acyl CoA esterase; Displays esterase activity toward palmitoyl-CoA and pNP- butyrate. (249 aa) |
| | ytfB | Cell division protein YtfB; Cell division protein whose function is related to the generation of a transient cell wall structure. Function is linked to the late stages of cell division. (212 aa) |
| | fklB | FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (206 aa) |
| | pmbA | Putative antibiotic peptide MccB17 maturation peptidase; Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA). (450 aa) |
| | pepA | Cytosol aminopeptidase; Probably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place. (503 aa) |
| | sgcX | Putative endoglucanase with Zn-dependent exopeptidase domain; Putative lyase/synthase. (373 aa) |
| | iadA | Isoaspartyl dipeptidase; Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu. (390 aa) |
| | rimI | ribosomal-protein-S18-alanine N-acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S18. Also acts as a N-epsilon-lysine acetyltransferase that catalyzes acetylation of several proteins. (148 aa) |
| | yjjJ | Putative protein kinase; Toxic when overexpressed in E.coli, leading to long filamentous cells. The toxic effect is neutralized by non-cognate antitoxin HipB. Does not seem to inhibit DNA, RNA or protein synthesis, and unlike paralogous toxin HipA its toxic activity is not counteracted by overexpression of GltX. Binds DNA. Might be a protein kinase (By similarity). (443 aa) |
| | lplA | Lipoate-protein ligase A; Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein. (338 aa) |
| | ykfG | CP4-6 prophage; Putative DNA repair protein; Belongs to the UPF0758 family. (158 aa) |
| | creC | Sensory histidine kinase in two-component regulatory system with CreB or PhoB; Member of the two-component regulatory system CreC/CreB involved in catabolic regulation. CreC may function as a membrane- associated protein kinase that phosphorylates CreB in response to environmental signals. CreC can also phosphorylate PhoB. (474 aa) |
| | rzoR | Prophage outer membrane lipoprotein RzoR; Component of the spanin complex that disrupts the outer membrane and causes cell lysis during virus exit. The spanin complex conducts the final step in cell lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans (By similarity). (61 aa) |
| | lgt | Phosphatidylglycerol-prolipoprotein diacylglyceryl transferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. (291 aa) |
| | ptrA | Protease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. (962 aa) |
| | tcdA | tRNA threonylcarbamoyladenosine dehydratase; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine. TcdA is also part of a sulfur transfer pathway; is able to accept sulfur from CsdA directly in vitro, but CsdE might act as the sulfur donor in vivo; Belongs to the HesA/MoeB/ThiF family. (268 aa) |
| | barA | Hybrid sensory histidine kinase, in two-component regulatory system with UvrY; Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. Phosphorylates UvrY, probably via a four-step phosphorelay. (918 aa) |
| | iap | Aminopeptidase in alkaline phosphatase isozyme conversion; This protein, presumably an aminopeptidase, mediates the conversion of E.coli alkaline phosphatase isozyme 1, to isozymes 2 and 3 by removing, one by one, the two N-terminal arginine residues. (345 aa) |
| | ygeR | tRNA-Gly; Anticodon: CCC; Belongs to the peptidase M23B family. (251 aa) |
| | pcm | L-isoaspartate protein carboxylmethyltransferase type II; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues; Belongs to the methyltransferase superfamily. L- isoaspartyl/D-aspartyl protein methyltransferase family. (208 aa) |
| | nlpD | Activator of AmiC murein hydrolase activity, lipoprotein; Activator of the cell wall hydrolase AmiC. Required for septal murein cleavage and daughter cell separation during cell division. (379 aa) |
| | pphB | Serine/threonine-specific protein phosphatase 2; Has been shown, in vitro, to act on Ser, Thr and Tyr- phosphorylated substrates; Belongs to the PPP phosphatase family. (218 aa) |
| | hycI | Protease involved in processing C-terminal end of HycE; Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3; Belongs to the peptidase A31 family. (156 aa) |
| | nrdH | Hydrogen donor for NrdEF electron transport system; Electron transport system for the ribonucleotide reductase system NrdEF; Belongs to the glutaredoxin family. (81 aa) |
| | yfjY | CP4-57 prophage; Putative DNA repair protein; Belongs to the UPF0758 family. (160 aa) |
| | pka | Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility. (886 aa) |
| | trxC | Thioredoxin 2; Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin. (139 aa) |
| | lepB | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. (324 aa) |
| | glrK | Sensor protein kinase regulating glmY sRNA in two-component system with response regulator GlrR; Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Activates GlrR by phosphorylation. (475 aa) |
| | pepB | Aminopeptidase B; Probably plays an important role in intracellular peptide degradation. (427 aa) |
| | pbpC | Penicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. (770 aa) |
| | bepA | OM protein maintenance and assembly metalloprotease and chaperone, periplasmic; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions; Belongs to the peptidase M48 family. BepA subfamily. (487 aa) |
| | narQ | Sensory histidine kinase in two-component regulatory system with NarP; Acts as a sensor for nitrate/nitrite and transduces signal of nitrate/nitrite availability to the NarL/NarP proteins. NarQ probably activates NarL and NarP by phosphorylation. NarQ probably negatively regulates the NarL protein by dephosphorylation. (566 aa) |
| | yfeW | Penicillin binding protein PBP4B; Penicillin-binding protein. Has low DD-carboxypeptidase activity; Belongs to the peptidase S12 family. YfeW subfamily. (434 aa) |
| | ypdF | Xaa-Pro aminopeptidase; Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine. (361 aa) |
| | ypdE | Aminopeptidase; Has a broad aminopeptidase activity on non-blocked peptides by progressively cleaving amino acids off the peptide substrate. Aminopeptidase activity stops at the residue before the first proline in the peptide. Cannot cleave when proline is the first N-terminal residue. (345 aa) |
| | ypdA | Sensor kinase regulating yhjX; Member of the two-component regulatory system YpdA/YpdB, which is part of a nutrient-sensing regulatory network composed of YpdA/YpdB, the high-affinity pyruvate signaling system BtsS/BtsR and their respective target proteins, YhjX and BtsT. YpdA activates YpdB by phosphorylation in response to high concentrations of extracellular pyruvate. Activation of the YpdA/YpdB signaling cascade also promotes BtsS/BtsR-mediated btsT expression. (565 aa) |
| | evgS | Hybrid sensory histidine kinase in two-component regulatory system with EvgA; Member of the two-component regulatory system EvgS/EvgA. Phosphorylates EvgA via a four-step phosphorelay in response to environmental signals. (1197 aa) |
| | sixA | Phosphohistidine phosphatase; Exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay. (161 aa) |
| | prmB | N5-glutamine methyltransferase; Specifically methylates the 50S ribosomal protein L3 on 'Gln- 150'. Does not methylate the translation termination release factors RF1 and RF2; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. (310 aa) |
| | ygeY | Putative deacetylase. (403 aa) |
| | dsbC | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. (236 aa) |
| | rclA | Reactive chlorine stress species (RCS) resistance protein; Probably involved in reactive chlorine species (RCS) stress resistance. (441 aa) |
| | ampH | D-alanyl-D-alanine- carboxypeptidase/endopeptidase; Hydrolyzes the cross-linked dimers tetrapentapeptide (D45) and tetratetrapeptide (D44). Removes the terminal D-alanine from muropeptides and disaccharide pentapeptide M5 with a C-terminal D-Ala- D-Ala dipeptide. Associated with recycling and remodeling of peptidoglycan (PG). Also displays a low beta-lactamase activity. Belongs to the beta-lactamase family. (385 aa) |
| | phoA | Alkaline phosphatase; start codon corrected; Protein involved in phosphorus metabolic process; Belongs to the alkaline phosphatase family. (471 aa) |
| | phoR | Sensory histidine kinase in two-component regulatory system with PhoB; Member of the two-component regulatory system PhoR/PhoB involved in the phosphate regulon genes expression. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoB in response to environmental signals. (431 aa) |
| | acpH | Acyl carrier protein (ACP) phosphodiesterase; Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP; Belongs to the AcpH family. (193 aa) |
| | yajL | Oxidative-stress-resistance chaperone; Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehy [...] (196 aa) |
| | tig | Peptidyl-prolyl cis/trans isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates. Binds to nascent polypeptide chains via ribosomal protein L23. Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Belongs to the FKBP-type PPIase family. Tig subfamily. (432 aa) |
| | clpP | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE. (207 aa) |
| | clpX | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized a [...] (424 aa) |
| | lon | DNA-binding ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins, including some antitoxins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator [...] (784 aa) |
| | ppiD | Periplasmic folding chaperone, has an inactive PPIase domain; PPIases accelerate the folding of proteins. Seems to be involved in the folding of outer membrane proteins. Its preference at the P1 position of the peptide substrate is Glu > Leu > Ala > His > Val > Phe > Ile > Gly > Lys > Thr. (623 aa) |
| | tesA | acyl-CoA thioesterase 1 and protease I and lysophospholipase L1; TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease. TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA. TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate. Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin [...] (208 aa) |
| | ppiB | Peptidyl-prolyl cis-trans isomerase B (rotamase B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (164 aa) |
| | rzpD | DLP12 prophage; Necessary for host cell lysis. It is believed to code for an endopeptidase that cleaves the amino-carboxyl cross-link between the diaminopimelic acid and D-alanine residues in the murein component of the bacterial cell wall (By similarity). (153 aa) |
| | ompT | DLP12 prophage; Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues. (317 aa) |
| | cusS | Copper-sensing histidine kinase in two-component regulatory system with CusR; Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Acts as a copper/silver ion sensor. Activates CusR by phosphorylation. (480 aa) |
| | fepE | Regulator of length of O-antigen component of lipopolysaccharide chains; Part of the ferric enterobactin transport system. (377 aa) |
| | dsbG | Thiol:disulfide interchange protein, periplasmic; Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro. Belongs to the thioredoxin family. DsbC subfamily. (248 aa) |
| | ahpF | Alkyl hydroperoxide reductase, F52a subunit, FAD/NAD(P)-binding; Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. (521 aa) |
| | citA | Sensory histidine kinase in two-component regulatory system with CitB; Member of the two-component regulatory system DpiA/DpiB, which is essential for expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. Could be involved in response to both the presence of citrate and external redox conditions. Functions as a sensor kinase that phosphorylates DpiA in the presence of citrate. (552 aa) |
| | lipB | Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. Belongs to the LipB family. (213 aa) |
| | dacA | D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. (403 aa) |
| | mrdA | Penicillin-binding protein 2, transpeptidase involved in peptidoglycan synthesis; Catalyzes cross-linking of the peptidoglycan cell wall. Responsible for the determination of the rod shape of the cell. Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth. Belongs to the transpeptidase family. MrdA subfamily. (633 aa) |
| | ybeY | ssRNA-specific endoribonuclease; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. Acts together with the RNase R to eliminate defective 70S ribosomes, but not properly matured 70S ribosomes or individual subunits, by a process mediated specifically by the 30S ribosomal subunit. Involved in the processing of 16S, 23S and 5S rRNAs, with a particularly strong effect on maturation at both the 5'- and 3'- ends of 16S rRNA as well as maturation of the 5'-end of 23S and 5S rRNAs. (155 aa) |
| | kdpD | Fused sensory histidine kinase in two-component regulatory system with KdpE: signal sensing protein; Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals. (894 aa) |
| | sucB | Dihydrolipoyltranssuccinase; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (405 aa) |
| | ldtB | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. Can be oxidized in vivo, its reduction depends preferentially on DsbG, although DsbC is able to partially replace DsbG; Belongs to the YkuD family. (306 aa) |
| | moeB | Molybdopterin synthase sulfurylase; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD. (249 aa) |
| | iaaA | Isoaspartyl peptidase; Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function. Belongs to the Ntn-hydrolase family. (321 aa) |
| | rimO | Ribosomal protein S12 methylthiotransferase; Catalyzes the methylthiolation of the residue Asp-89 of ribosomal protein S12. (441 aa) |
| | dacC | D-alanyl-D-alanine carboxypeptidase; Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. (400 aa) |
| | grxA | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. (85 aa) |
| | rimK | Ribosomal protein S6 modification protein; Is an L-glutamate ligase that catalyzes the ATP-dependent post-translational addition of glutamate residues to the C-terminus of ribosomal protein S6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. Belongs to the RimK family. (300 aa) |
| | clpA | ATPase and specificity subunit of ClpA-ClpP ATP-dependent serine protease, chaperone activity; ATP-dependent specificity component of the ClpAP protease. It directs the protease to specific substrates. It has unfoldase activity. The primary function of the ClpA-ClpP complex appears to be the degradation of unfolded or abnormal proteins. (758 aa) |
| | aat | leucyl/phenylalanyl-tRNA-protein transferase; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine; Belongs to the L/F-transferase family. (234 aa) |
| | trxB | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. (321 aa) |
| | ycaL | Putative peptidase-related chaperone; Involved in the degradation of the LPS-assembly protein LptD. Degrades LptD that have engaged the Bam complex but are stalled at an early step in the outer membrane protein assembly process. (254 aa) |
| | ldtD | Murein L,D-transpeptidase; Responsible, at least in part, for generating a meso- diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link. Belongs to the YkuD family. (615 aa) |
| | ycbK | M15A protease-related family periplasmic protein. (182 aa) |
| | pepN | Aminopeptidase N; Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. (870 aa) |
| | ycbZ | Putative ATP-dependent protease; Protein involved in proteolysis. (586 aa) |
| | hyaD | Hydrogenase 1 maturation protease; Protease involved in the C-terminal processing of HyaB, the large subunit of hydrogenase 1; Belongs to the peptidase A31 family. (195 aa) |
| | etk | Tyrosine-protein kinase, role in O-antigen capsule formation; Protein involved in protein modification process; Belongs to the etk/wzc family. (726 aa) |
| | etp | O-antigen capsule forming protein-tyrosine-phosphatase; Dephosphorylates etk; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. (148 aa) |
| | torS | Hybrid sensory histidine kinase in two-component regulatory system with TorR; Member of the two-component regulatory system TorS/TorR involved in the anaerobic utilization of trimethylamine-N-oxide (TMAO). Detects the presence of TMAO in the medium and, in response, activates TorR via a four-step phosphorelay. When TMAO is removed, TorS can dephosphorylate TorR, probably by a reverse phosphorelay involving His- 860 and Asp-733. (914 aa) |
| | grxB | Glutaredoxin 2 (Grx2); Involved in reducing some disulfide bonds in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase. (215 aa) |
| | ldtC | L,D-transpeptidase linking Lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp. (320 aa) |
| | cobB | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. (242 aa) |
| | pepT | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. (408 aa) |
| | phoQ | Sensory histidine kinase in two-component regulatory system with PhoP; Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP- repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulti [...] (486 aa) |
| | lit | T4 phage exclusion protein; Interacts with a short DNA sequence about one-quarter of the way into the major capsid protein gene 23 of T4; general translation inhibition occurs when this late gene of the virus is expressed. Belongs to the peptidase U49 family. (297 aa) |
| | umuD | Translesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp-complex may target Pol V to replicat [...] (139 aa) |
| | dsbB | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. (176 aa) |
| | ldcA | Murein tetrapeptide carboxypeptidase; Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essen [...] (304 aa) |
| | prmC | RF-1 and RF-2 N5-glutamine methyltransferase; Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln- 252' in RF2; Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily. (277 aa) |
| | narX | Sensory histidine kinase in two-component regulatory system with NarL; Acts as a sensor for nitrate/nitrite and transduces signal of nitrate availability to the NarL protein and of both nitrate/nitrite to the NarP protein. NarX probably activates NarL and NarP by phosphorylation in the presence of nitrate. NarX also plays a negative role in controlling NarL activity, probably through dephosphorylation in the absence of nitrate. (598 aa) |
| | sohB | Inner membrane protein, S49 peptidase family protein; Multicopy suppressor of the HtrA (DegP) null phenotype. It is possibly a protease, not essential for bacterial viability; Belongs to the peptidase S49 family. (349 aa) |
| | mpaA | Murein peptide amidase A; Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso- diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. Has weak activity with L-Ala- gamma-D-Glu-L-Lys, MurNAc-tripeptide and gamma-D-Glu-meso-Dap. Cannot hydrolyze murein tetrapeptide ; Belongs to the peptidase M14 family. (242 aa) |
| | abgB | P-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. (481 aa) |
| | abgA | P-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. (436 aa) |
| | ynbD | Putative phosphatase inner membrane protein; Putative enzymes; Belongs to the protein-tyrosine phosphatase family. (430 aa) |
| | ddpX | D-ala-D-ala dipeptidase, Zn-dependent; Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. May have a role in cell-wall turnover. (193 aa) |
| | pqqL | Putative periplasmic M16 family zinc metalloendopeptidase; Putative zinc protease. (931 aa) |
| | hipA | Serine/threonine-protein kinase toxin HipA; Toxic component of a type II toxin-antitoxin (TA) system, first identified by mutations that increase production of persister cells, a fraction of cells that are phenotypic variants not killed by antibiotics, which lead to multidrug tolerance. Persistence may be ultimately due to global remodeling of the persister cell's ribosomes. Phosphorylates Glu-tRNA-ligase (AC P04805, gltX, on 'Ser-239') in vivo. Phosphorylation of GltX prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and [...] (440 aa) |
| | dcp | Dipeptidyl carboxypeptidase II; Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides. Belongs to the peptidase M3 family. (681 aa) |
| | ydgD | Putative peptidase; Belongs to the peptidase S1B family. (273 aa) |
| | rstB | Sensory histidine kinase of RstAB two-component system; Member of the two-component regulatory system RstB/RstA. RstB functions as a membrane-associated protein kinase that phosphorylates RstA (Probable). (433 aa) |
| | grxD | Glutaredoxin-4; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters; Belongs to the glutaredoxin family. Monothiol subfamily. (115 aa) |
| | mepH | Murein DD-endopeptidase, space-maker hydrolase; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant. (271 aa) |
| | ldtE | Murein L,D-transpeptidase; Responsible, at least in part, for generating a meso- diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link. (334 aa) |
| | ppsR | PEP synthase kinase and PEP synthase pyrophosphorylase; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation. (277 aa) |
| | nlpC | Putative C40 clan peptidase lipoprotein; Lipoprotein. (154 aa) |
| | sppA | Protease IV (signal peptide peptidase); Digests cleaved signal peptides in vitro, its in vivo function is unknown. This activity is necessary to maintain proper secretion of mature proteins across the membrane. Belongs to the peptidase S49 family. (618 aa) |
| | yeaG | Protein kinase, endogenous substrate unidentified; autokinase; Belongs to the PrkA family. (644 aa) |
| | tsaB | tRNA(ANN) t(6)A37 threonylcarbamoyladenosine modification protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, can act as a protease that specifically degrades TsaD in vitro; therefore TsaB may po [...] (231 aa) |
| | htpX | Putative endopeptidase; Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Belongs to the peptidase M48B family. (293 aa) |
| | prc | Carboxy-terminal protease for penicillin-binding protein 3; Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses. (682 aa) |
| | pphA | Serine/threonine-specific protein phosphatase 1; Plays a key role in signaling protein misfolding via the CpxR/CPXA transducing system. It also modulates the phosphorylated status of many phosphoproteins in E.coli, some of which acting as major chaperones. Has been shown, in vitro, to act on Ser, Thr and Tyr- phosphorylated substrates; Belongs to the PPP phosphatase family. PP-1 subfamily. (218 aa) |
| | ptrB | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. (686 aa) |
| | mepM | Murein DD-endopeptidase, space-maker hydrolase, septation protein; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant. (440 aa) |
| | cheZ | Chemotaxis regulator, protein phosphatase for CheY; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P); Belongs to the CheZ family. (214 aa) |
