| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CBH21170.1 | clpB-3 | CLOST_1047 | CLOST_1982 | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Protein disaggregation chaperone; 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. | 0.671 |
| CBH21170.1 | clpP | CLOST_1047 | CLOST_0590 | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine 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. | 0.693 |
| CBH21170.1 | dnaJ | CLOST_1047 | CLOST_1792 | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.520 |
| CBH21170.1 | dnaK | CLOST_1047 | CLOST_1793 | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chaperone Hsp70, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.565 |
| CBH21170.1 | hscC | CLOST_1047 | CLOST_0384 | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Hsp70 family chaperone Hsc62, binds to RpoD and inhibits transcription; Function of homologous gene experimentally demonstrated in an other organism; factor; Belongs to the heat shock protein 70 family. | 0.565 |
| CBH21170.1 | htpG | CLOST_1047 | CLOST_1987 | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.413 |
| CBH21170.1 | yeiI | CLOST_1047 | CLOST_1984 | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.641 |
| clpB-3 | CBH21170.1 | CLOST_1982 | CLOST_1047 | Protein disaggregation chaperone; 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. | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.671 |
| clpB-3 | clpP | CLOST_1982 | CLOST_0590 | Protein disaggregation chaperone; 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. | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine 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. | 0.910 |
| clpB-3 | dnaJ | CLOST_1982 | CLOST_1792 | Protein disaggregation chaperone; 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 Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.821 |
| clpB-3 | dnaK | CLOST_1982 | CLOST_1793 | Protein disaggregation chaperone; 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 Hsp70, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.872 |
| clpB-3 | grpE | CLOST_1982 | CLOST_1794 | Protein disaggregation chaperone; 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. | 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-dependent interacti [...] | 0.751 |
| clpB-3 | hscC | CLOST_1982 | CLOST_0384 | Protein disaggregation chaperone; 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. | Hsp70 family chaperone Hsc62, binds to RpoD and inhibits transcription; Function of homologous gene experimentally demonstrated in an other organism; factor; Belongs to the heat shock protein 70 family. | 0.839 |
| clpB-3 | htpG | CLOST_1982 | CLOST_1987 | Protein disaggregation chaperone; 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. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.748 |
| clpB-3 | mcsB | CLOST_1982 | CLOST_0159 | Protein disaggregation chaperone; 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. | McsB; Catalyzes the specific phosphorylation of arginine residues in proteins; Belongs to the ATP:guanido phosphotransferase family. | 0.752 |
| clpB-3 | psuG | CLOST_1982 | CLOST_1983 | Protein disaggregation chaperone; 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. | Conserved protein of unknown function; Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway; Belongs to the pseudouridine-5'-phosphate glycosidase family. | 0.678 |
| clpB-3 | yeiI | CLOST_1982 | CLOST_1984 | Protein disaggregation chaperone; 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. | Putative kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.699 |
| clpP | CBH21170.1 | CLOST_0590 | CLOST_1047 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine 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. | Putative Histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.693 |
| clpP | clpB-3 | CLOST_0590 | CLOST_1982 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine 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. | Protein disaggregation chaperone; 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 | dnaJ | CLOST_0590 | CLOST_1792 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine 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. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.613 |
