| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Swit_0771 | Swit_4377 | Swit_0771 | Swit_4377 | Molecular chaperone-like protein. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.576 |
| Swit_0771 | Swit_4767 | Swit_0771 | Swit_4767 | Molecular chaperone-like protein. | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein. | 0.833 |
| Swit_0771 | dnaJ | Swit_0771 | Swit_1249 | Molecular chaperone-like 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 [...] | 0.891 |
| Swit_0771 | groL | Swit_0771 | Swit_3376 | Molecular chaperone-like protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.968 |
| Swit_0771 | groS | Swit_0771 | Swit_3375 | Molecular chaperone-like protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.934 |
| Swit_0771 | grpE | Swit_0771 | Swit_1253 | Molecular chaperone-like protein. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.976 |
| Swit_0771 | hrcA | Swit_0771 | Swit_0566 | Molecular chaperone-like protein. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.667 |
| Swit_0771 | hslV | Swit_0771 | Swit_4376 | Molecular chaperone-like protein. | 20S proteasome, A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.494 |
| Swit_3667 | Swit_4377 | Swit_3667 | Swit_4377 | PFAM: Thioredoxin domain. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.891 |
| Swit_3667 | Swit_4767 | Swit_3667 | Swit_4767 | PFAM: Thioredoxin domain. | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein. | 0.622 |
| Swit_3667 | dnaJ | Swit_3667 | Swit_1249 | PFAM: Thioredoxin domain. | 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 [...] | 0.749 |
| Swit_3667 | dnaK | Swit_3667 | Swit_1250 | PFAM: Thioredoxin domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.606 |
| Swit_3667 | groL | Swit_3667 | Swit_3376 | PFAM: Thioredoxin domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.861 |
| Swit_3667 | groS | Swit_3667 | Swit_3375 | PFAM: Thioredoxin domain. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.561 |
| Swit_3667 | grpE | Swit_3667 | Swit_1253 | PFAM: Thioredoxin domain. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.874 |
| Swit_3667 | hslV | Swit_3667 | Swit_4376 | PFAM: Thioredoxin domain. | 20S proteasome, A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.886 |
| Swit_4377 | Swit_0771 | Swit_4377 | Swit_0771 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone-like protein. | 0.576 |
| Swit_4377 | Swit_3667 | Swit_4377 | Swit_3667 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | PFAM: Thioredoxin domain. | 0.891 |
| Swit_4377 | Swit_4767 | Swit_4377 | Swit_4767 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein. | 0.642 |
| Swit_4377 | dnaJ | Swit_4377 | Swit_1249 | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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 [...] | 0.940 |