| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpB | clpP | LCA_1040 | LCA_0531 | Chaperone ClpB; 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 Clp protease, proteolytic subunit ClpP; 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. | 0.910 |
| clpB | dnaJ | LCA_1040 | LCA_1235 | Chaperone ClpB; 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. | Chaperone protein DnaJ (heat-shock protein Hsp40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent i [...] | 0.784 |
| clpB | dnaK | LCA_1040 | LCA_1236 | Chaperone ClpB; 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. | Chaperone protein DnaK (heat-shock protein Hsp70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.948 |
| clpB | groL | LCA_1040 | LCA_0359 | Chaperone ClpB; 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. | Chaperonin GroEL (60 kDa chaperonin) (Protein Cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.839 |
| clpB | groS | LCA_1040 | LCA_0358 | Chaperone ClpB; 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. | Co-chaperonin GroES (10 kD chaperonin) (Protein Cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.763 |
| clpB | grpE | LCA_1040 | LCA_1237 | Chaperone ClpB; 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. | Co-chaperone protein 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 AT [...] | 0.839 |
| clpB | hrcA | LCA_1040 | LCA_1238 | Chaperone ClpB; 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. | Transcriptional regulator of heat-shock/chaperone genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.754 |
| clpC | clpP | LCA_1779 | LCA_0531 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | 0.927 |
| clpC | dnaJ | LCA_1779 | LCA_1235 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | Chaperone protein DnaJ (heat-shock protein Hsp40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent i [...] | 0.717 |
| clpC | dnaK | LCA_1779 | LCA_1236 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK (heat-shock protein Hsp70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.908 |
| clpC | groL | LCA_1779 | LCA_0359 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | Chaperonin GroEL (60 kDa chaperonin) (Protein Cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.745 |
| clpC | groS | LCA_1779 | LCA_0358 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | Co-chaperonin GroES (10 kD chaperonin) (Protein Cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.820 |
| clpC | grpE | LCA_1779 | LCA_1237 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | Co-chaperone protein 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 AT [...] | 0.767 |
| clpC | hrcA | LCA_1779 | LCA_1238 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | Transcriptional regulator of heat-shock/chaperone genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.512 |
| clpC | hslU | LCA_1779 | LCA_0984 | ATPase/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | ATP-dependent Hsl protease, ATP-binding subunit HslU; 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. | 0.423 |
| clpP | clpB | LCA_0531 | LCA_1040 | ATP-dependent Clp protease, proteolytic subunit ClpP; 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 ClpB; 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. | 0.910 |
| clpP | clpC | LCA_0531 | LCA_1779 | ATP-dependent Clp protease, proteolytic subunit ClpP; 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/chaperone ClpC, putative specificity factor for ClpP protease; Belongs to the ClpA/ClpB family. | 0.927 |
| clpP | dnaJ | LCA_0531 | LCA_1235 | ATP-dependent Clp protease, proteolytic subunit ClpP; 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 protein DnaJ (heat-shock protein Hsp40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent i [...] | 0.656 |
| clpP | dnaK | LCA_0531 | LCA_1236 | ATP-dependent Clp protease, proteolytic subunit ClpP; 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 protein DnaK (heat-shock protein Hsp70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.802 |
| clpP | groL | LCA_0531 | LCA_0359 | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | Chaperonin GroEL (60 kDa chaperonin) (Protein Cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.810 |