node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
amiD | ampD | b0867 | b0110 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; N-acetylmuramoyl-L-alanine amidase AmiD; Putative regulator; Not classified | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction | 0.441 |
amiD | mepS | b0867 | b2175 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; N-acetylmuramoyl-L-alanine amidase AmiD; Putative regulator; Not classified | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | 0.904 |
amiD | mpaA | b0867 | b1326 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; N-acetylmuramoyl-L-alanine amidase AmiD; Putative regulator; Not classified | Murein tripeptide 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 | 0.558 |
amiD | mpl | b0867 | b4233 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; N-acetylmuramoyl-L-alanine amidase AmiD; Putative regulator; Not classified | UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase; Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl- meso-diaminopimelate by linking it to UDP-N-acetylmuramate. The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6- diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D- glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in vitro | 0.537 |
ampD | amiD | b0110 | b0867 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; N-acetylmuramoyl-L-alanine amidase AmiD; Putative regulator; Not classified | 0.441 |
ampD | mepS | b0110 | b2175 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | 0.904 |
ampD | mltD | b0110 | b0211 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction | Putative membrane-bound lytic murein transglycosylase d; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity) | 0.696 |
ampD | mpaA | b0110 | b1326 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction | Murein tripeptide 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 | 0.834 |
ampD | mpl | b0110 | b4233 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction | UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase; Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl- meso-diaminopimelate by linking it to UDP-N-acetylmuramate. The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6- diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D- glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in vitro | 0.962 |
lpoB | mepS | b1105 | b2175 | Outer membrane lipoprotein - activator of mrcb activity; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | 0.730 |
lpoB | mltD | b1105 | b0211 | Outer membrane lipoprotein - activator of mrcb activity; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b | Putative membrane-bound lytic murein transglycosylase d; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity) | 0.566 |
lpoB | nlpI | b1105 | b3163 | Outer membrane lipoprotein - activator of mrcb activity; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b | 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) | 0.547 |
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 | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | 0.867 |
mepM | mltD | b1856 | b0211 | 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 | Putative membrane-bound lytic murein transglycosylase d; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity) | 0.830 |
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) | 0.609 |
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 | 0.608 |
mepS | amiD | b2175 | b0867 | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; N-acetylmuramoyl-L-alanine amidase AmiD; Putative regulator; Not classified | 0.904 |
mepS | ampD | b2175 | b0110 | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; Involved in cell wall peptidoglycan recycling . Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety . Is also involved in beta-lactamase induction | 0.904 |
mepS | lpoB | b2175 | b1105 | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | Outer membrane lipoprotein - activator of mrcb activity; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b | 0.730 |
mepS | mepM | b2175 | b1856 | Peptidoglycan dd-endopeptidase/peptidoglycan 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 | 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 | 0.867 |