node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clgR | clpB | Rv2745c | Rv0384c | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | 0.450 |
clgR | clpC1 | Rv2745c | Rv3596c | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | 0.765 |
clgR | clpP1 | Rv2745c | Rv2461c | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); 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 (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.852 |
clgR | clpP2 | Rv2745c | Rv2460c | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); 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 (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.405 |
clgR | clpS | Rv2745c | Rv1331 | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.683 |
clgR | clpX | Rv2745c | Rv2457c | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.497 |
clpB | clgR | Rv0384c | Rv2745c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | 0.450 |
clpB | clpP1 | Rv0384c | Rv2461c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); 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 (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.940 |
clpB | clpP2 | Rv0384c | Rv2460c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); 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 (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.916 |
clpB | clpS | Rv0384c | Rv1331 | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.864 |
clpB | clpX | Rv0384c | Rv2457c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.649 |
clpB | ftsH | Rv0384c | Rv3610c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | Membrane-bound protease FtsH (cell division protein); 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. | 0.537 |
clpB | groES | Rv0384c | Rv3418c | Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...] | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.891 |
clpC1 | clgR | Rv3596c | Rv2745c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Transcriptional regulatory protein ClgR; Overexpression leads to expression of the clp regulon (ClpP1, ClpP2 and ClpC1). | 0.765 |
clpC1 | clpP1 | Rv3596c | Rv2461c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease proteolytic subunit 1 ClpP1 (endopeptidase CLP); 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 (By similarity). Degrades anti-sigma-D factor (rsdA) when present in a complex with ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). Belongs to the peptidase S14 family. | 0.997 |
clpC1 | clpP2 | Rv3596c | Rv2460c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease proteolytic subunit 2 ClpP2 (endopeptidase CLP 2); 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 (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. Belongs to the peptidase S14 family. | 0.996 |
clpC1 | clpS | Rv3596c | Rv1331 | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.955 |
clpC1 | clpX | Rv3596c | Rv2457c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Probable ATP-dependent CLP protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. | 0.822 |
clpC1 | ftsH | Rv3596c | Rv3610c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | Membrane-bound protease FtsH (cell division protein); 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. | 0.777 |
clpC1 | groES | Rv3596c | Rv3418c | Probable ATP-dependent protease ATP-binding subunit ClpC1; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Degrades anti-sigma-E factor RseA in the presence of ClpP2. | 10 kDa chaperonin GroES (protein CPN10) (protein GroES) (BCG-a heat shock protein) (10 kDa antigen); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.721 |