| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MCA1138 | groEL-1 | MCA1138 | MCA0707 | Hydrogenase subunit; Identified by similarity to SP:P77329; match to protein family HMM PF00329; match to protein family HMM PF00346. | Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.804 |
| MCA1138 | groEL-2 | MCA1138 | MCA1202 | Hydrogenase subunit; Identified by similarity to SP:P77329; match to protein family HMM PF00329; match to protein family HMM PF00346. | Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.804 |
| MCA1138 | groEL-3 | MCA1138 | MCA1704 | Hydrogenase subunit; Identified by similarity to SP:P77329; match to protein family HMM PF00329; match to protein family HMM PF00346. | Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.804 |
| MCA2614 | dnaJ | MCA2614 | MCA1855 | Thioredoxin family protein; Identified by similarity to GP:17427791; match to protein family HMM PF00085; match to protein family HMM TIGR01068. | 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 [...] | 0.816 |
| MCA2614 | groEL-1 | MCA2614 | MCA0707 | Thioredoxin family protein; Identified by similarity to GP:17427791; match to protein family HMM PF00085; match to protein family HMM TIGR01068. | Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.788 |
| MCA2614 | groEL-2 | MCA2614 | MCA1202 | Thioredoxin family protein; Identified by similarity to GP:17427791; match to protein family HMM PF00085; match to protein family HMM TIGR01068. | Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.788 |
| MCA2614 | groEL-3 | MCA2614 | MCA1704 | Thioredoxin family protein; Identified by similarity to GP:17427791; match to protein family HMM PF00085; match to protein family HMM TIGR01068. | Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.788 |
| MCA2614 | grpE | MCA2614 | MCA1857 | Thioredoxin family protein; Identified by similarity to GP:17427791; match to protein family HMM PF00085; match to protein family HMM TIGR01068. | GrpE 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 ATP-dependent i [...] | 0.856 |
| MCA2614 | htpG | MCA2614 | MCA0848 | Thioredoxin family protein; Identified by similarity to GP:17427791; match to protein family HMM PF00085; match to protein family HMM TIGR01068. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.785 |
| dnaJ | MCA2614 | MCA1855 | MCA2614 | 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 [...] | Thioredoxin family protein; Identified by similarity to GP:17427791; match to protein family HMM PF00085; match to protein family HMM TIGR01068. | 0.816 |
| dnaJ | dnaK | MCA1855 | MCA1856 | 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. | 0.997 |
| dnaJ | groEL-1 | MCA1855 | MCA0707 | 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 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.943 |
| dnaJ | groEL-2 | MCA1855 | MCA1202 | 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 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.935 |
| dnaJ | groEL-3 | MCA1855 | MCA1704 | 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 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.943 |
| dnaJ | groES-1 | MCA1855 | MCA0706 | 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 kDa subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.914 |
| dnaJ | groES-2 | MCA1855 | MCA1705 | 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 kDa subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.914 |
| dnaJ | grpE | MCA1855 | MCA1857 | 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 [...] | GrpE 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 ATP-dependent i [...] | 0.996 |
| dnaJ | htpG | MCA1855 | MCA0848 | 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 HtpG; Molecular chaperone. Has ATPase activity. | 0.974 |
| dnaK | dnaJ | MCA1856 | MCA1855 | 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 [...] | 0.997 |
| dnaK | groEL-1 | MCA1856 | MCA0707 | dnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.893 |
