| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EFK99350.1 | dnaJ | SSLG_01410 | SSLG_01770 | Predicted 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 [...] | 0.949 |
| EFK99350.1 | dnaK | SSLG_01410 | SSLG_03033 | Predicted protein. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| EFK99350.1 | groL | SSLG_01410 | SSLG_02363 | Predicted protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.884 |
| EFK99350.1 | groL-2 | SSLG_01410 | SSLG_02800 | Predicted protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.884 |
| EFK99350.1 | grpE | SSLG_01410 | SSLG_03032 | Predicted 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 [...] | 0.812 |
| EFK99792.1 | EFL00079.1 | SSLG_01851 | SSLG_02137 | 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. | Type II beta-Tyr adenylation domain-containing protein. | 0.909 |
| EFK99792.1 | dnaJ | SSLG_01851 | SSLG_01770 | 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 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 [...] | 0.928 |
| EFK99792.1 | groL | SSLG_01851 | SSLG_02363 | 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. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.608 |
| EFK99792.1 | groL-2 | SSLG_01851 | SSLG_02800 | 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. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.608 |
| EFK99792.1 | grpE | SSLG_01851 | SSLG_03032 | 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 [...] | 0.510 |
| EFL00079.1 | EFK99792.1 | SSLG_02137 | SSLG_01851 | Type II beta-Tyr adenylation domain-containing protein. | 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. | 0.909 |
| EFL00079.1 | EFL00877.1 | SSLG_02137 | SSLG_02935 | Type II beta-Tyr adenylation domain-containing protein. | Magnesium or manganese-dependent protein phosphatase. | 0.468 |
| EFL00079.1 | dnaJ | SSLG_02137 | SSLG_01770 | Type II beta-Tyr adenylation 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 [...] | 0.951 |
| EFL00079.1 | dnaK | SSLG_02137 | SSLG_03033 | Type II beta-Tyr adenylation domain-containing protein. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.634 |
| EFL00079.1 | groL | SSLG_02137 | SSLG_02363 | Type II beta-Tyr adenylation domain-containing protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.500 |
| EFL00079.1 | groL-2 | SSLG_02137 | SSLG_02800 | Type II beta-Tyr adenylation domain-containing protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.500 |
| EFL00877.1 | EFL00079.1 | SSLG_02935 | SSLG_02137 | Magnesium or manganese-dependent protein phosphatase. | Type II beta-Tyr adenylation domain-containing protein. | 0.468 |
| EFL00877.1 | dnaJ | SSLG_02935 | SSLG_01770 | Magnesium or manganese-dependent protein phosphatase. | 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 |
| EFL00877.1 | dnaK | SSLG_02935 | SSLG_03033 | Magnesium or manganese-dependent protein phosphatase. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.587 |
| EFL02840.1 | dnaJ | SSLG_04898 | SSLG_01770 | Heat shock 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 [...] | 0.963 |