| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| VC_1386 | dnaJ | VC_1386 | VC_0856 | Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; identified by sequence similarity; putative. | 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 [...] | 0.904 |
| VC_1386 | groL1 | VC_1386 | VC_2664 | Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; 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. | 0.881 |
| VC_1386 | groL2 | VC_1386 | VC_A0820 | Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; 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. | 0.881 |
| VC_1386 | groS1 | VC_1386 | VC_2665 | Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; 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. | 0.841 |
| VC_1386 | grpE | VC_1386 | VC_0854 | Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; 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- [...] | 0.931 |
| VC_1386 | hslU | VC_1386 | VC_2674 | Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; 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. | 0.492 |
| VC_1386 | htpG | VC_1386 | VC_0985 | Heat shock protein 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; identified by sequence similarity; putative. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family. | 0.926 |
| clpP | dnaJ | VC_1922 | VC_0856 | ATP-dependent Clp protease, proteolytic subunit; 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. | 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 [...] | 0.649 |
| clpP | dnaK | VC_1922 | VC_0855 | ATP-dependent Clp protease, proteolytic subunit; 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. | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.747 |
| clpP | groL1 | VC_1922 | VC_2664 | ATP-dependent Clp protease, proteolytic subunit; 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. | Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.742 |
| clpP | groL2 | VC_1922 | VC_A0820 | ATP-dependent Clp protease, proteolytic subunit; 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. | Chaperonin, 60 Kd subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.736 |
| clpP | groS1 | VC_1922 | VC_2665 | ATP-dependent Clp protease, proteolytic subunit; 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. | Chaperonin, 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.874 |
| clpP | grpE | VC_1922 | VC_0854 | ATP-dependent Clp protease, proteolytic subunit; 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. | 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- [...] | 0.868 |
| clpP | hslU | VC_1922 | VC_2674 | ATP-dependent Clp protease, proteolytic subunit; 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. | 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. | 0.719 |
| clpP | htpG | VC_1922 | VC_0985 | ATP-dependent Clp protease, proteolytic subunit; 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. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family. | 0.835 |
| dnaJ | VC_1386 | VC_0856 | VC_1386 | 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 70 family protein; Similar to SP:P36928 GB:U00096 PID:1788384; identified by sequence similarity; putative. | 0.904 |
| dnaJ | clpP | VC_0856 | VC_1922 | 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 [...] | ATP-dependent Clp protease, proteolytic subunit; 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. | 0.649 |
| 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 |
