node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
grxD | mepH | b1654 | b1655 | Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters | 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 | 0.568 |
grxD | sodB | b1654 | b1656 | Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters | Superoxide dismutase, fe-mn family; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems | 0.480 |
lhr | mepH | b1653 | b1655 | Atp-dependent helicase lhr and lhr-like helicase; Belongs to the helicase family | 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 | 0.511 |
mepA | mepH | b2328 | b1655 | Peptidoglycan dd-endopeptidase/peptidoglycan ld-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 | 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 | 0.601 |
mepA | mepM | b2328 | b1856 | Peptidoglycan dd-endopeptidase/peptidoglycan ld-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 | 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 | 0.566 |
mepA | pbpG | b2328 | b2134 | Peptidoglycan dd-endopeptidase/peptidoglycan ld-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 | Serine-type d-ala-d-ala endopeptidase (penicillin-binding protein 7); 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 | 0.646 |
mepH | grxD | b1655 | b1654 | 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 | Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters | 0.568 |
mepH | lhr | b1655 | b1653 | 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 | Atp-dependent helicase lhr and lhr-like helicase; Belongs to the helicase family | 0.511 |
mepH | mepA | b1655 | b2328 | 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 | Peptidoglycan dd-endopeptidase/peptidoglycan ld-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 | 0.601 |
mepH | mepM | b1655 | b1856 | 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 | 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 | 0.915 |
mepH | mepS | b1655 | b2175 | 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 | 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 | 0.499 |
mepH | nlpA | b1655 | b3661 | 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 | D-methionine transport system substrate-binding protein; Lipoprotein-28 | 0.561 |
mepH | nlpI | b1655 | b3163 | 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 | 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 |
mepH | pbpG | b1655 | b2134 | 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 | Serine-type d-ala-d-ala endopeptidase (penicillin-binding protein 7); 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 | 0.493 |
mepH | sodB | b1655 | b1656 | 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 | Superoxide dismutase, fe-mn family; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems | 0.566 |
mepH | tldD | b1655 | b3244 | 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 | Metalloprotease tldd; Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA) | 0.600 |
mepM | mepA | b1856 | b2328 | 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-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 | 0.566 |
mepM | mepH | b1856 | b1655 | 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, 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 | 0.915 |
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 | 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 |