| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| VC_A0788 | dnaK | VC_A0788 | VC_0855 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.891 |
| VC_A0788 | groL1 | VC_A0788 | VC_2664 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.859 |
| VC_A0788 | groL2 | VC_A0788 | VC_A0820 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.859 |
| VC_A0788 | groS1 | VC_A0788 | VC_2665 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | Chaperonin, 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.621 |
| VC_A0788 | groS2 | VC_A0788 | VC_A0819 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | Chaperonin, 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.621 |
| VC_A0788 | grpE | VC_A0788 | VC_0854 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | 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- [...] | 0.946 |
| VC_A0788 | hscA | VC_A0788 | VC_0752 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | Chaperone protein HscA; Probable chaperone. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (By similarity). | 0.891 |
| VC_A0788 | hslU | VC_A0788 | VC_2674 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | Protease 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. | 0.740 |
| VC_A0788 | hslV | VC_A0788 | VC_2675 | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | Protease HslVU, subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.616 |
| dnaJ | dnaK | VC_0856 | VC_0855 | 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 [...] | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL1 | VC_0856 | VC_2664 | 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 [...] | Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.975 |
| dnaJ | groL2 | VC_0856 | VC_A0820 | 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 [...] | Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.973 |
| dnaJ | groS1 | VC_0856 | VC_2665 | 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 [...] | Chaperonin, 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.910 |
| dnaJ | groS2 | VC_0856 | VC_A0819 | 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 [...] | Chaperonin, 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.827 |
| dnaJ | grpE | VC_0856 | VC_0854 | 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 [...] | 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- [...] | 0.998 |
| dnaJ | hscA | VC_0856 | VC_0752 | 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 [...] | Chaperone protein HscA; Probable chaperone. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (By similarity). | 0.984 |
| dnaJ | hslU | VC_0856 | VC_2674 | 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 [...] | Protease 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. | 0.971 |
| dnaJ | hslV | VC_0856 | VC_2675 | 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 [...] | Protease HslVU, subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.958 |
| dnaK | VC_A0788 | VC_0855 | VC_A0788 | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DnaJ-related protein; Similar to SP:P48207 PID:893246; identified by sequence similarity; putative. | 0.891 |
| dnaK | dnaJ | VC_0855 | VC_0856 | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 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 [...] | 0.999 |
