node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpA | clpP | STM0945 | STM0448 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | 0.989 |
clpA | clpX | STM0945 | STM0449 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.932 |
clpA | dnaK | STM0945 | STM0012 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Chaperone Hsp70; Acts as a chaperone. | 0.835 |
clpA | hflB | STM0945 | STM3296 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | ATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. | 0.466 |
clpA | ssrA | STM0945 | STM1392 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Secretion system regulator: Sensor component; SpiR (gi|1498305). | 0.755 |
clpP | clpA | STM0448 | STM0945 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | 0.989 |
clpP | clpX | STM0448 | STM0449 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.999 |
clpP | csrA | STM0448 | STM2826 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | Carbon storage regulator; A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). | 0.540 |
clpP | dnaK | STM0448 | STM0012 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | Chaperone Hsp70; Acts as a chaperone. | 0.957 |
clpP | fliC | STM0448 | STM1959 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.470 |
clpP | ftsZ | STM0448 | STM0133 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.570 |
clpP | hflB | STM0448 | STM3296 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | ATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. | 0.787 |
clpP | ssrA | STM0448 | STM1392 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | Secretion system regulator: Sensor component; SpiR (gi|1498305). | 0.634 |
clpX | clpA | STM0449 | STM0945 | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | 0.932 |
clpX | clpP | STM0449 | STM0448 | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. Belongs to the peptidase S14 family. | 0.999 |
clpX | csrA | STM0449 | STM2826 | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Carbon storage regulator; A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). | 0.528 |
clpX | dnaK | STM0449 | STM0012 | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Chaperone Hsp70; Acts as a chaperone. | 0.857 |
clpX | fliC | STM0449 | STM1959 | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.522 |
clpX | ftsZ | STM0449 | STM0133 | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Tubulin-like GTP-binding protein and GTPase; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.719 |
clpX | hflB | STM0449 | STM3296 | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | ATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. | 0.940 |