| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ClpA | ClpP | PTH_0283 | PTH_0804 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Protease subunit of ATP-dependent Clp 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. Belongs to the peptidase S14 family. | 0.934 |
| ClpA | ClpX | PTH_0283 | PTH_0805 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | ATP-dependent protease Clp, ATPase subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.479 |
| ClpA | DnaK | PTH_0283 | PTH_0878 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.961 |
| ClpA | GrpE | PTH_0283 | PTH_0877 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE; 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 [...] | 0.835 |
| ClpA | HslU | PTH_0283 | PTH_1250 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.588 |
| ClpA | HslV | PTH_0283 | PTH_1249 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ), peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.495 |
| ClpA | HtpG | PTH_0283 | PTH_0110 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Molecular chaperone; Molecular chaperone. Has ATPase activity. | 0.789 |
| ClpA | Lon | PTH_0283 | PTH_0807 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | 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. | 0.737 |
| ClpA-2 | ClpP | PTH_2122 | PTH_0804 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | Protease subunit of ATP-dependent Clp 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. Belongs to the peptidase S14 family. | 0.935 |
| ClpA-2 | ClpX | PTH_2122 | PTH_0805 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | ATP-dependent protease Clp, ATPase subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.479 |
| ClpA-2 | DnaK | PTH_2122 | PTH_0878 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.961 |
| ClpA-2 | GrpE | PTH_2122 | PTH_0877 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE; 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 [...] | 0.835 |
| ClpA-2 | HslU | PTH_2122 | PTH_1250 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.588 |
| ClpA-2 | HslV | PTH_2122 | PTH_1249 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ), peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.495 |
| ClpA-2 | HtpG | PTH_2122 | PTH_0110 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | Molecular chaperone; Molecular chaperone. Has ATPase activity. | 0.789 |
| ClpA-2 | Lon | PTH_2122 | PTH_0807 | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | 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. | 0.737 |
| ClpP | ClpA | PTH_0804 | PTH_0283 | Protease subunit of ATP-dependent Clp 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. Belongs to the peptidase S14 family. | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | 0.934 |
| ClpP | ClpA-2 | PTH_0804 | PTH_2122 | Protease subunit of ATP-dependent Clp 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. Belongs to the peptidase S14 family. | ATPase with chaperone activity, ATP-binding subunit; 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; Belongs to the ClpA/ClpB family. | 0.935 |
| ClpP | ClpX | PTH_0804 | PTH_0805 | Protease subunit of ATP-dependent Clp 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. Belongs to the peptidase S14 family. | ATP-dependent protease Clp, ATPase subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.998 |
| ClpP | DnaK | PTH_0804 | PTH_0878 | Protease subunit of ATP-dependent Clp 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. Belongs to the peptidase S14 family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.846 |