node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpP | prlC | b0437 | b3498 | 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. | 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). | 0.517 |
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 |
dcp | ptrB | b1538 | b1845 | Dipeptidyl carboxypeptidase II; Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides. Belongs to the peptidase M3 family. | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 0.451 |
elaD | ptrB | b2269 | b1845 | 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. | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 0.785 |
pqqL | ptrA | b1494 | b2821 | Putative periplasmic M16 family zinc metalloendopeptidase; Putative zinc protease. | Protease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. | 0.517 |
pqqL | ptrB | b1494 | b1845 | Putative periplasmic M16 family zinc metalloendopeptidase; Putative zinc protease. | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 0.503 |
prlC | clpP | b3498 | b0437 | 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). | 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. | 0.517 |
prlC | ptrB | b3498 | b1845 | 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). | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 0.501 |
ptrA | pqqL | b2821 | b1494 | Protease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. | Putative periplasmic M16 family zinc metalloendopeptidase; Putative zinc protease. | 0.517 |
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 |
ptrA | sppA | b2821 | b1766 | Protease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. | 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. | 0.544 |
ptrB | clpP | b1845 | b0437 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A 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. | 0.402 |
ptrB | dcp | b1845 | b1538 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | Dipeptidyl carboxypeptidase II; Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides. Belongs to the peptidase M3 family. | 0.451 |
ptrB | elaD | b1845 | b2269 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 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. | 0.785 |
ptrB | pqqL | b1845 | b1494 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | Putative periplasmic M16 family zinc metalloendopeptidase; Putative zinc protease. | 0.503 |
ptrB | prlC | b1845 | b3498 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | 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). | 0.501 |
ptrB | ptrA | b1845 | b2821 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | Protease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. | 0.784 |
ptrB | rlpA | b1845 | b0633 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. | Septal ring protein, suppressor of prc, minor lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides; Belongs to the RlpA family. | 0.432 |
ptrB | sppA | b1845 | b1766 | Protease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A 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. | 0.521 |