node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ansA | pncA | b1767 | b1768 | Cytoplasmic L-asparaginase 1; Protein involved in cellular amino acid catabolic process; Belongs to the asparaginase 1 family. | Nicotinamidase/pyrazinamidase; Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide. | 0.918 |
ansA | sppA | b1767 | b1766 | Cytoplasmic L-asparaginase 1; Protein involved in cellular amino acid catabolic process; Belongs to the asparaginase 1 family. | 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. | 0.768 |
clpP | htpX | b0437 | b1829 | 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. | 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. | 0.625 |
clpP | lepB | b0437 | b2568 | 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. | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | 0.496 |
clpP | ptrB | b0437 | b1845 | 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. | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 0.402 |
clpP | sppA | b0437 | b1766 | 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. | 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. | 0.565 |
htpX | clpP | b1829 | b0437 | 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. | 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. | 0.625 |
htpX | mepM | b1829 | b1856 | 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. | 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. | 0.769 |
htpX | sppA | b1829 | b1766 | 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. | 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. | 0.708 |
lepB | clpP | b2568 | b0437 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | 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. | 0.496 |
lepB | mepM | b2568 | b1856 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 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. | 0.795 |
lepB | sppA | b2568 | b1766 | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | 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. | 0.744 |
mepM | htpX | b1856 | b1829 | 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 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. | 0.769 |
mepM | lepB | b1856 | b2568 | 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. | Leader peptidase (signal peptidase I); Belongs to the peptidase S26 family. | 0.795 |
mepM | sppA | b1856 | b1766 | 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. | 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. | 0.659 |
pncA | ansA | b1768 | b1767 | Nicotinamidase/pyrazinamidase; Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide. | Cytoplasmic L-asparaginase 1; Protein involved in cellular amino acid catabolic process; Belongs to the asparaginase 1 family. | 0.918 |
pncA | sppA | b1768 | b1766 | Nicotinamidase/pyrazinamidase; Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide. | 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. | 0.519 |
pncA | ydjA | b1768 | b1765 | Nicotinamidase/pyrazinamidase; Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide. | Putative oxidoreductase; Belongs to the nitroreductase family. | 0.601 |
pspA | sppA | b1304 | b1766 | Regulatory protein for phage-shock-protein operon; The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp- specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force. Belongs to the PspA/IM30 family. | 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. | 0.501 |
ptrA | ptrB | b2821 | b1845 | Protease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 0.784 |