| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BCOR_0158 | BCOR_0896 | BCOR_0158 | BCOR_0896 | Molecular chaperone DnaJ. | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.778 |
| BCOR_0158 | dnaK | BCOR_0158 | BCOR_0156 | Molecular chaperone DnaJ. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| BCOR_0158 | groL | BCOR_0158 | BCOR_0926 | Molecular chaperone DnaJ. | GroEL 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.773 |
| BCOR_0158 | groS | BCOR_0158 | BCOR_1200 | Molecular chaperone DnaJ. | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.675 |
| BCOR_0158 | grpE | BCOR_0158 | BCOR_0157 | Molecular chaperone DnaJ. | 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 [...] | 0.965 |
| BCOR_0158 | hrcA | BCOR_0158 | BCOR_0692 | Molecular chaperone DnaJ. | Heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.675 |
| BCOR_0896 | BCOR_0158 | BCOR_0896 | BCOR_0158 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | Molecular chaperone DnaJ. | 0.778 |
| BCOR_0896 | dnaJ | BCOR_0896 | BCOR_0691 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 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 [...] | 0.778 |
| BCOR_0896 | groL | BCOR_0896 | BCOR_0926 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | GroEL 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.737 |
| BCOR_0896 | groS | BCOR_0896 | BCOR_1200 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | Chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.501 |
| BCOR_0896 | grpE | BCOR_0896 | BCOR_0157 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 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 [...] | 0.406 |
| BCOR_0927 | dnaK | BCOR_0927 | BCOR_0156 | Cold shock protein. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.562 |
| BCOR_0927 | groL | BCOR_0927 | BCOR_0926 | Cold shock protein. | GroEL 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.728 |
| BCOR_0927 | grpE | BCOR_0927 | BCOR_0157 | Cold shock protein. | 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 [...] | 0.548 |
| BCOR_1122 | groL | BCOR_1122 | BCOR_0926 | Hypothetical protein. | GroEL 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.765 |
| dnaJ | BCOR_0896 | BCOR_0691 | BCOR_0896 | 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 [...] | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.778 |
| dnaJ | dnaK | BCOR_0691 | BCOR_0156 | 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. | 0.993 |
| dnaJ | groL | BCOR_0691 | BCOR_0926 | 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 [...] | GroEL 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.872 |
| dnaJ | groS | BCOR_0691 | BCOR_1200 | 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 GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.675 |
| dnaJ | grpE | BCOR_0691 | BCOR_0157 | 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 [...] | 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 [...] | 0.919 |
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