| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FP2_25060 | FP2_32070 | FP2_25060 | FP2_32070 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Thioredoxin; Belongs to the thioredoxin family. | 0.461 |
| FP2_25060 | dnaK | FP2_25060 | FP2_12320 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.975 |
| FP2_25060 | dnaK-2 | FP2_25060 | FP2_26120 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.977 |
| FP2_25060 | groL | FP2_25060 | FP2_04990 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.815 |
| FP2_25060 | groS | FP2_25060 | FP2_04980 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.667 |
| FP2_25060 | grpE | FP2_25060 | FP2_12330 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Molecular chaperone GrpE (heat shock 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. [...] | 0.933 |
| FP2_25060 | htpG | FP2_25060 | FP2_18560 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.943 |
| FP2_25060 | lon | FP2_25060 | FP2_06390 | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | ATP-dependent proteinase. Serine peptidase. MEROPS family S16; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.603 |
| FP2_32070 | FP2_25060 | FP2_32070 | FP2_25060 | Thioredoxin; Belongs to the thioredoxin family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain. | 0.461 |
| FP2_32070 | dnaJ | FP2_32070 | FP2_12310 | Thioredoxin; Belongs to the thioredoxin 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 [...] | 0.426 |
| FP2_32070 | groL | FP2_32070 | FP2_04990 | Thioredoxin; Belongs to the thioredoxin family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.894 |
| FP2_32070 | groS | FP2_32070 | FP2_04980 | Thioredoxin; Belongs to the thioredoxin family. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.520 |
| FP2_32070 | grpE | FP2_32070 | FP2_12330 | Thioredoxin; Belongs to the thioredoxin family. | Molecular chaperone GrpE (heat shock 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. [...] | 0.575 |
| FP2_32070 | htpG | FP2_32070 | FP2_18560 | Thioredoxin; Belongs to the thioredoxin family. | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.464 |
| dnaJ | FP2_32070 | FP2_12310 | FP2_32070 | 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 [...] | Thioredoxin; Belongs to the thioredoxin family. | 0.426 |
| dnaJ | dnaK | FP2_12310 | FP2_12320 | 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. | 0.994 |
| dnaJ | dnaK-2 | FP2_12310 | FP2_26120 | 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. | 0.987 |
| dnaJ | groL | FP2_12310 | FP2_04990 | 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 GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.828 |
| dnaJ | groS | FP2_12310 | FP2_04980 | 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-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.667 |
| dnaJ | grpE | FP2_12310 | FP2_12330 | 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 [...] | Molecular chaperone GrpE (heat shock 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. [...] | 0.973 |
