node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SRU_2059 | dnaK | SRU_2059 | SRU_1300 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.985 |
SRU_2059 | groL | SRU_2059 | SRU_0237 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.714 |
SRU_2059 | groL-2 | SRU_2059 | SRU_2122 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.715 |
SRU_2059 | groS | SRU_2059 | SRU_0862 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperonin, 10 kDa; Identified by match to protein family HMM PF00166. | 0.529 |
SRU_2059 | groS-2 | SRU_2059 | SRU_2121 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.603 |
SRU_2059 | grpE | SRU_2059 | SRU_2352 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | 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 [...] | 0.898 |
SRU_2059 | hslU | SRU_2059 | SRU_1644 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | 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. | 0.622 |
SRU_2059 | hslV | SRU_2059 | SRU_1642 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Heat shock protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.538 |
dnaJ | dnaK | SRU_0467 | SRU_1300 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
dnaJ | groL | SRU_0467 | SRU_0237 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.801 |
dnaJ | groL-2 | SRU_0467 | SRU_2122 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.802 |
dnaJ | groS | SRU_0467 | SRU_0862 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | Chaperonin, 10 kDa; Identified by match to protein family HMM PF00166. | 0.529 |
dnaJ | groS-2 | SRU_0467 | SRU_2121 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.696 |
dnaJ | grpE | SRU_0467 | SRU_2352 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | 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 [...] | 0.915 |
dnaJ | hslU | SRU_0467 | SRU_1644 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | 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. | 0.622 |
dnaJ | hslV | SRU_0467 | SRU_1642 | dnaJ protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | Heat shock protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.538 |
dnaJ-2 | dnaK | SRU_2351 | SRU_1300 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.991 |
dnaJ-2 | groL | SRU_2351 | SRU_0237 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.794 |
dnaJ-2 | groL-2 | SRU_2351 | SRU_2122 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.794 |
dnaJ-2 | groS | SRU_2351 | SRU_0862 | 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 [...] | Chaperonin, 10 kDa; Identified by match to protein family HMM PF00166. | 0.529 |