node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
degP | nlpI | b0161 | b3163 | 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. [...] | Lipoprotein involved in osmotic sensitivity and filamentation; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA). | 0.478 |
degP | prc | b0161 | b1830 | 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. [...] | 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. | 0.808 |
degP | rseP | b0161 | b0176 | 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. [...] | 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 [...] | 0.870 |
ftsI | mepM | b0084 | b1856 | 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. | 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. | 0.635 |
ftsI | mepS | b0084 | b2175 | 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. | 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. | 0.554 |
ftsI | prc | b0084 | b1830 | 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. | 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. | 0.671 |
ftsI | rseP | b0084 | b0176 | 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. | 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 [...] | 0.403 |
hisS | prc | b2514 | b1830 | Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. | 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. | 0.635 |
hisS | rseP | b2514 | b0176 | Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation. | 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 [...] | 0.426 |
mepM | ftsI | b1856 | b0084 | 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. | 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. | 0.635 |
mepM | mepS | b1856 | b2175 | 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. | 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. | 0.903 |
mepM | nlpI | b1856 | b3163 | 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. | Lipoprotein involved in osmotic sensitivity and filamentation; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA). | 0.790 |
mepM | prc | b1856 | b1830 | 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. | 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. | 0.682 |
mepM | rseP | b1856 | b0176 | 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. | 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 [...] | 0.677 |
mepS | ftsI | b2175 | b0084 | 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. | 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. | 0.554 |
mepS | mepM | b2175 | b1856 | 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. | 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. | 0.903 |
mepS | nlpI | b2175 | b3163 | 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. | Lipoprotein involved in osmotic sensitivity and filamentation; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division. Negatively controls the production of extracellular DNA (eDNA). | 0.895 |
mepS | prc | b2175 | b1830 | 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. | 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. | 0.895 |
msrC | prc | b1832 | b1830 | Free methionine-(R)-sulfoxide reductase; Catalyzes the reversible oxidation-reduction of the R- enantiomer of free methionine sulfoxide to methionine. Specific for free L-methionine-(R)-S-oxide. | 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. | 0.638 |
msrC | proQ | b1832 | b1831 | Free methionine-(R)-sulfoxide reductase; Catalyzes the reversible oxidation-reduction of the R- enantiomer of free methionine sulfoxide to methionine. Specific for free L-methionine-(R)-S-oxide. | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | 0.912 |