| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KB13_1241 | clpA | KB13_1241 | KB13_754 | [R] COG0457 FOG: TPR repeat. | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | 0.443 |
| KB13_1241 | clpB | KB13_1241 | KB13_935 | [R] COG0457 FOG: TPR repeat. | ATP-dependent 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. | 0.443 |
| KB13_1241 | dnaJ | KB13_1241 | KB13_927 | [R] COG0457 FOG: TPR repeat. | Chaperone protein DnaJ; 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 DnaJ, D [...] | 0.903 |
| KB13_1241 | dnaK | KB13_1241 | KB13_1276 | [R] COG0457 FOG: TPR repeat. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.933 |
| KB13_1241 | groL | KB13_1241 | KB13_1300 | [R] COG0457 FOG: TPR repeat. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.667 |
| KB13_1241 | grpE | KB13_1241 | KB13_600 | [R] COG0457 FOG: TPR repeat. | Co-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-depend [...] | 0.616 |
| KB13_1241 | htpG | KB13_1241 | KB13_427 | [R] COG0457 FOG: TPR repeat. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.972 |
| clpA | KB13_1241 | KB13_754 | KB13_1241 | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | [R] COG0457 FOG: TPR repeat. | 0.443 |
| clpA | dnaJ | KB13_754 | KB13_927 | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | Chaperone protein DnaJ; 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 DnaJ, D [...] | 0.804 |
| clpA | dnaK | KB13_754 | KB13_1276 | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.920 |
| clpA | groL | KB13_754 | KB13_1300 | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.507 |
| clpA | groS | KB13_754 | KB13_857 | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.543 |
| clpA | grpE | KB13_754 | KB13_600 | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | Co-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-depend [...] | 0.783 |
| clpA | htpG | KB13_754 | KB13_427 | ATP-dependent Clp protease ATP-binding subunit ClpA; [O] COG0466 ATP-dependent Lon protease, bacterial type; Belongs to the ClpA/ClpB family. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.669 |
| clpB | KB13_1241 | KB13_935 | KB13_1241 | ATP-dependent 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. | [R] COG0457 FOG: TPR repeat. | 0.443 |
| clpB | dnaJ | KB13_935 | KB13_927 | ATP-dependent 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; 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 DnaJ, D [...] | 0.837 |
| clpB | dnaK | KB13_935 | KB13_1276 | ATP-dependent 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; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.941 |
| clpB | groL | KB13_935 | KB13_1300 | ATP-dependent 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 GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.564 |
| clpB | groS | KB13_935 | KB13_857 | ATP-dependent 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 GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.604 |
| clpB | grpE | KB13_935 | KB13_600 | ATP-dependent 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 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-depend [...] | 0.830 |