| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EFL37539.1 | EFL37540.1 | SSRG_00343 | SSRG_00344 | Condensation domain-containing protein; Unextendable partial coding region. | Condensation domain-containing protein. | 0.999 |
| EFL37539.1 | EFL43486.1 | SSRG_00343 | SSRG_06290 | Condensation domain-containing protein; Unextendable partial coding region. | Non-ribosomal peptide synthetase/polyketide synthase Ta1; Truncated CDS; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.999 |
| EFL37539.1 | dnaJ | SSRG_00343 | SSRG_03024 | Condensation domain-containing protein; Unextendable partial coding region. | Chaperone 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, DnaK and [...] | 0.950 |
| EFL37539.1 | dnaK | SSRG_00343 | SSRG_00795 | Condensation domain-containing protein; Unextendable partial coding region. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.409 |
| EFL37539.1 | dnaK-2 | SSRG_00343 | SSRG_03026 | Condensation domain-containing protein; Unextendable partial coding region. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.409 |
| EFL37539.1 | groL | SSRG_00343 | SSRG_02447 | Condensation domain-containing protein; Unextendable partial coding region. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.537 |
| EFL37539.1 | groL-2 | SSRG_00343 | SSRG_03503 | Condensation domain-containing protein; Unextendable partial coding region. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.537 |
| EFL37540.1 | EFL37539.1 | SSRG_00344 | SSRG_00343 | Condensation domain-containing protein. | Condensation domain-containing protein; Unextendable partial coding region. | 0.999 |
| EFL37540.1 | EFL43486.1 | SSRG_00344 | SSRG_06290 | Condensation domain-containing protein. | Non-ribosomal peptide synthetase/polyketide synthase Ta1; Truncated CDS; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.999 |
| EFL37540.1 | dnaJ | SSRG_00344 | SSRG_03024 | Condensation domain-containing protein. | Chaperone 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, DnaK and [...] | 0.950 |
| EFL37540.1 | dnaK | SSRG_00344 | SSRG_00795 | Condensation domain-containing protein. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.409 |
| EFL37540.1 | dnaK-2 | SSRG_00344 | SSRG_03026 | Condensation domain-containing protein. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.409 |
| EFL37540.1 | groL | SSRG_00344 | SSRG_02447 | Condensation domain-containing protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.537 |
| EFL37540.1 | groL-2 | SSRG_00344 | SSRG_03503 | Condensation domain-containing protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.537 |
| EFL40219.1 | dnaJ | SSRG_03023 | SSRG_03024 | Transcriptional regulator HspR. | Chaperone 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, DnaK and [...] | 0.982 |
| EFL40219.1 | dnaK | SSRG_03023 | SSRG_00795 | Transcriptional regulator HspR. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.781 |
| EFL40219.1 | dnaK-2 | SSRG_03023 | SSRG_03026 | Transcriptional regulator HspR. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.922 |
| EFL40219.1 | groL | SSRG_03023 | SSRG_02447 | Transcriptional regulator HspR. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.505 |
| EFL40219.1 | groL-2 | SSRG_03023 | SSRG_03503 | Transcriptional regulator HspR. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.511 |
| EFL40219.1 | grpE | SSRG_03023 | SSRG_03025 | Transcriptional regulator HspR. | GrpE (HSP-70 cofactor); 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-d [...] | 0.992 |