| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACP32744.1 | ACP33441.1 | cauri_1151 | cauri_1848 | Zinc finger protein 768. | Hypothetical protein; FOG: Ankyrin repeat. | 0.825 |
| ACP32744.1 | dnaJ1 | cauri_1151 | cauri_2319 | Zinc finger protein 768. | Molecular chaperone protein; 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 interactions between Dn [...] | 0.772 |
| ACP32744.1 | dnaK | cauri_1151 | cauri_2321 | Zinc finger protein 768. | Molecular chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.650 |
| ACP32744.1 | groEL1 | cauri_1151 | cauri_0475 | Zinc finger protein 768. | Molecular chaperone protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.413 |
| ACP32744.1 | groEL2 | cauri_1151 | cauri_2263 | Zinc finger protein 768. | Molecular chaperone protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.413 |
| ACP33441.1 | ACP32744.1 | cauri_1848 | cauri_1151 | Hypothetical protein; FOG: Ankyrin repeat. | Zinc finger protein 768. | 0.825 |
| ACP33441.1 | dnaJ1 | cauri_1848 | cauri_2319 | Hypothetical protein; FOG: Ankyrin repeat. | Molecular chaperone protein; 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 interactions between Dn [...] | 0.772 |
| ACP33441.1 | dnaK | cauri_1848 | cauri_2321 | Hypothetical protein; FOG: Ankyrin repeat. | Molecular chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.815 |
| clpB | dnaJ1 | cauri_2310 | cauri_2319 | ATP-dependent Clp protease, 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 protein; 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 interactions between Dn [...] | 0.888 |
| clpB | dnaK | cauri_2310 | cauri_2321 | ATP-dependent Clp protease, 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 protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
| clpB | groEL1 | cauri_2310 | cauri_0475 | ATP-dependent Clp protease, 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 protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.871 |
| clpB | groEL2 | cauri_2310 | cauri_2263 | ATP-dependent Clp protease, 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 protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.870 |
| clpB | grpE | cauri_2310 | cauri_2320 | ATP-dependent Clp protease, 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 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 [...] | 0.951 |
| clpB | hspR | cauri_2310 | cauri_2318 | ATP-dependent Clp protease, 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. | Heat shock protein regulator HspR; Predicted transcriptional regulators. | 0.765 |
| dnaJ1 | ACP32744.1 | cauri_2319 | cauri_1151 | Molecular chaperone protein; 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 interactions between Dn [...] | Zinc finger protein 768. | 0.772 |
| dnaJ1 | ACP33441.1 | cauri_2319 | cauri_1848 | Molecular chaperone protein; 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 interactions between Dn [...] | Hypothetical protein; FOG: Ankyrin repeat. | 0.772 |
| dnaJ1 | clpB | cauri_2319 | cauri_2310 | Molecular chaperone protein; 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 interactions between Dn [...] | ATP-dependent Clp protease, 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. | 0.888 |
| dnaJ1 | dnaK | cauri_2319 | cauri_2321 | Molecular chaperone protein; 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 interactions between Dn [...] | Molecular chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ1 | groEL1 | cauri_2319 | cauri_0475 | Molecular chaperone protein; 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 interactions between Dn [...] | Molecular chaperone protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.857 |
| dnaJ1 | groEL2 | cauri_2319 | cauri_2263 | Molecular chaperone protein; 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 interactions between Dn [...] | Molecular chaperone protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.886 |
