| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ISM_00345 | ISM_07435 | ISM_00345 | ISM_07435 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | COG3118 Thioredoxin domain-containing protein. | 0.440 |
| ISM_00345 | ISM_10810 | ISM_00345 | ISM_10810 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Molecular chaperone, DnaK; COG0443 Molecular chaperone. | 0.951 |
| ISM_00345 | dnaK | ISM_00345 | ISM_08455 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.965 |
| ISM_00345 | groEL | ISM_00345 | ISM_05755 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.914 |
| ISM_00345 | groS | ISM_00345 | ISM_05760 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.768 |
| ISM_00345 | grpE | ISM_00345 | ISM_06685 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | 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 [...] | 0.966 |
| ISM_00345 | hrcA | ISM_00345 | ISM_06690 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | 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. | 0.714 |
| ISM_00345 | hslU | ISM_00345 | ISM_06805 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | ATP-dependent protease ATP-binding subunit; 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. | 0.751 |
| ISM_00345 | hslV | ISM_00345 | ISM_06810 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.618 |
| ISM_07435 | ISM_00345 | ISM_07435 | ISM_00345 | COG3118 Thioredoxin domain-containing protein. | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | 0.440 |
| ISM_07435 | dnaJ | ISM_07435 | ISM_08460 | COG3118 Thioredoxin domain-containing protein. | 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 [...] | 0.735 |
| ISM_07435 | dnaK | ISM_07435 | ISM_08455 | COG3118 Thioredoxin domain-containing protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.553 |
| ISM_07435 | groEL | ISM_07435 | ISM_05755 | COG3118 Thioredoxin domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.864 |
| ISM_07435 | groS | ISM_07435 | ISM_05760 | COG3118 Thioredoxin domain-containing protein. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.523 |
| ISM_07435 | grpE | ISM_07435 | ISM_06685 | COG3118 Thioredoxin domain-containing 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 [...] | 0.874 |
| ISM_07435 | hslU | ISM_07435 | ISM_06805 | COG3118 Thioredoxin domain-containing protein. | ATP-dependent protease ATP-binding subunit; 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. | 0.872 |
| ISM_07435 | hslV | ISM_07435 | ISM_06810 | COG3118 Thioredoxin domain-containing protein. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.883 |
| ISM_10810 | ISM_00345 | ISM_10810 | ISM_00345 | Molecular chaperone, DnaK; COG0443 Molecular chaperone. | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | 0.951 |
| ISM_10810 | dnaJ | ISM_10810 | ISM_08460 | Molecular chaperone, DnaK; COG0443 Molecular chaperone. | 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 [...] | 0.970 |
| ISM_10810 | groEL | ISM_10810 | ISM_05755 | Molecular chaperone, DnaK; COG0443 Molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.979 |
