| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpP | clpQ | BL03605 | BL01278 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | 0.783 |
| clpP | clpY | BL03605 | BL01277 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.733 |
| clpP | groEL | BL03605 | BL03283 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.892 |
| clpP | groES | BL03605 | BL03284 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.783 |
| clpP | grpE | BL03605 | BL02095 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Heat-shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depen [...] | 0.716 |
| clpP | htpG | BL03605 | BL00247 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.516 |
| clpP | lonA | BL03605 | BL00621 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class III heat-shock ATP-dependent Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.503 |
| clpQ | clpP | BL01278 | BL03605 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | 0.783 |
| clpQ | clpY | BL01278 | BL01277 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.999 |
| clpQ | codY | BL01278 | BL01276 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Transcriptional regulator; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | 0.807 |
| clpQ | gid | BL01278 | BL01280 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Glucose-inhibited division protein; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. | 0.783 |
| clpQ | groEL | BL01278 | BL03283 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.872 |
| clpQ | groES | BL01278 | BL03284 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.832 |
| clpQ | grpE | BL01278 | BL02095 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Heat-shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depen [...] | 0.909 |
| clpQ | htpG | BL01278 | BL00247 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.876 |
| clpQ | lonA | BL01278 | BL00621 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class III heat-shock ATP-dependent Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.854 |
| clpQ | xerC | BL01278 | BL01279 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Site-specific integrase/recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.983 |
| clpY | clpP | BL01277 | BL03605 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | 0.733 |
| clpY | clpQ | BL01277 | BL01278 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | 0.999 |
| clpY | codY | BL01277 | BL01276 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Transcriptional regulator; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | 0.848 |
