| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BB_0264 | BB_0602 | BB_0264 | BB_0602 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | Chaperonin, putative; Identified by match to protein family HMM PF00226. | 0.912 |
| BB_0264 | BB_0655 | BB_0264 | BB_0655 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | Heat shock protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | 0.975 |
| BB_0264 | dnaJ | BB_0264 | BB_0517 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | 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 [...] | 0.974 |
| BB_0264 | groL | BB_0264 | BB_0649 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.984 |
| BB_0264 | groS | BB_0264 | BB_0741 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.960 |
| BB_0264 | grpE | BB_0264 | BB_0519 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | 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 [...] | 0.987 |
| BB_0264 | hslU | BB_0264 | BB_0295 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | 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. | 0.747 |
| BB_0264 | hslV | BB_0264 | BB_0296 | Heat shock protein 70; Identified by match to protein family HMM PF00012. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.713 |
| BB_0602 | BB_0264 | BB_0602 | BB_0264 | Chaperonin, putative; Identified by match to protein family HMM PF00226. | Heat shock protein 70; Identified by match to protein family HMM PF00012. | 0.912 |
| BB_0602 | clpP | BB_0602 | BB_0611 | Chaperonin, putative; Identified by match to protein family HMM PF00226. | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | 0.420 |
| BB_0602 | dnaJ | BB_0602 | BB_0517 | Chaperonin, putative; Identified by match to protein family HMM PF00226. | 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 [...] | 0.504 |
| BB_0602 | dnaK | BB_0602 | BB_0518 | Chaperonin, putative; Identified by match to protein family HMM PF00226. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.912 |
| BB_0602 | groL | BB_0602 | BB_0649 | Chaperonin, putative; Identified by match to protein family HMM PF00226. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.925 |
| BB_0602 | groS | BB_0602 | BB_0741 | Chaperonin, putative; Identified by match to protein family HMM PF00226. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.753 |
| BB_0602 | grpE | BB_0602 | BB_0519 | Chaperonin, putative; 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 [...] | 0.899 |
| BB_0602 | hslU | BB_0602 | BB_0295 | Chaperonin, putative; 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. | 0.684 |
| BB_0602 | hslV | BB_0602 | BB_0296 | Chaperonin, putative; Identified by match to protein family HMM PF00226. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.595 |
| BB_0655 | BB_0264 | BB_0655 | BB_0264 | Heat shock protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | Heat shock protein 70; Identified by match to protein family HMM PF00012. | 0.975 |
| BB_0655 | clpP | BB_0655 | BB_0611 | Heat shock protein; Identified by match to protein family HMM PF00226; match to protein family HMM PF01556. | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | 0.420 |
| BB_0655 | dnaK | BB_0655 | BB_0518 | Heat shock 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. | 0.981 |
