| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BF49_0250 | BF49_0800 | BF49_0250 | BF49_0800 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | Chaperone protein HtpG. | 0.766 |
| BF49_0250 | dnaJ | BF49_0250 | BF49_0161 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | 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 [...] | 0.802 |
| BF49_0250 | dnaK | BF49_0250 | BF49_0162 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.669 |
| BF49_0250 | groS | BF49_0250 | BF49_3065 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | Heat shock protein 60 family cochaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.607 |
| BF49_0250 | groS-2 | BF49_0250 | BF49_6029 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | Heat shock protein 60 family cochaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.652 |
| BF49_0250 | grpE | BF49_0250 | BF49_0166 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | 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- [...] | 0.890 |
| BF49_0250 | hslU | BF49_0250 | BF49_0197 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | ATPdependent hsl protease ATPbinding 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. | 0.847 |
| BF49_0250 | hslV | BF49_0250 | BF49_0194 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | ATPdependent protease HslV EC 3425; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.865 |
| BF49_0250 | htpG | BF49_0250 | BF49_3215 | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.766 |
| BF49_0800 | BF49_0250 | BF49_0800 | BF49_0250 | Chaperone protein HtpG. | FIG000875 Thioredoxin domaincontaining protein ECYbbN. | 0.766 |
| BF49_0800 | dnaJ | BF49_0800 | BF49_0161 | Chaperone protein HtpG. | 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 [...] | 0.961 |
| BF49_0800 | dnaK | BF49_0800 | BF49_0162 | Chaperone protein HtpG. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.978 |
| BF49_0800 | groS | BF49_0800 | BF49_3065 | Chaperone protein HtpG. | Heat shock protein 60 family cochaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.789 |
| BF49_0800 | groS-2 | BF49_0800 | BF49_6029 | Chaperone protein HtpG. | Heat shock protein 60 family cochaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.789 |
| BF49_0800 | grpE | BF49_0800 | BF49_0166 | Chaperone protein HtpG. | 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- [...] | 0.844 |
| BF49_0800 | hslU | BF49_0800 | BF49_0197 | Chaperone protein HtpG. | ATPdependent hsl protease ATPbinding 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. | 0.838 |
| BF49_0800 | hslV | BF49_0800 | BF49_0194 | Chaperone protein HtpG. | ATPdependent protease HslV EC 3425; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.845 |
| BF49_0800 | htpG | BF49_0800 | BF49_3215 | Chaperone protein HtpG. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.644 |
| clpX | dnaJ | BF49_6616 | BF49_0161 | ATPdependent Clp protease ATPbinding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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 [...] | 0.448 |
| clpX | dnaK | BF49_6616 | BF49_0162 | ATPdependent Clp protease ATPbinding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.601 |
