| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DVU_1584 | dnaJ | DVU_1584 | DVU_3243 | Sigma 70 family protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | dnaJ 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 DnaJ, DnaK and Gr [...] | 0.857 |
| DVU_1584 | dnaK | DVU_1584 | DVU_0811 | Sigma 70 family protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.840 |
| DVU_1584 | groEL | DVU_1584 | DVU_1976 | Sigma 70 family protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.751 |
| DVU_1584 | groES | DVU_1584 | DVU_1977 | Sigma 70 family protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.473 |
| DVU_1584 | grpE | DVU_1584 | DVU_0812 | Sigma 70 family protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | Heat shock 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 ATP- [...] | 0.464 |
| DVU_1584 | hslV | DVU_1584 | DVU_1577 | Sigma 70 family protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.563 |
| clpA | dnaJ | DVU_1602 | DVU_3243 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | dnaJ 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 DnaJ, DnaK and Gr [...] | 0.886 |
| clpA | dnaK | DVU_1602 | DVU_0811 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.985 |
| clpA | groEL | DVU_1602 | DVU_1976 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.709 |
| clpA | groES | DVU_1602 | DVU_1977 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.680 |
| clpA | grpE | DVU_1602 | DVU_0812 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | Heat shock 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 ATP- [...] | 0.939 |
| clpA | hslU | DVU_1602 | DVU_1467 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | Heat shock protein HslVU, ATPase 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. | 0.667 |
| clpA | hslV | DVU_1602 | DVU_1577 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.531 |
| clpA | htpG | DVU_1602 | DVU_2643 | ATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP:P15716; match to protein family HMM PF00004; match to protein family HMM PF02861; Belongs to the ClpA/ClpB family. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family. | 0.879 |
| clpB | dnaJ | DVU_1874 | DVU_3243 | ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] | dnaJ 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 DnaJ, DnaK and Gr [...] | 0.887 |
| clpB | dnaK | DVU_1874 | DVU_0811 | ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
| clpB | groEL | DVU_1874 | DVU_1976 | ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.885 |
| clpB | groES | DVU_1874 | DVU_1977 | ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.865 |
| clpB | grpE | DVU_1874 | DVU_0812 | ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] | Heat shock 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 ATP- [...] | 0.939 |
| clpB | hslU | DVU_1874 | DVU_1467 | ATP-dependent Clp protease, ATP-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to [...] | Heat shock protein HslVU, ATPase 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. | 0.767 |
