| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SPRI_3610 | SPRI_6202 | SPRI_3610 | SPRI_6202 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | 0.735 |
| SPRI_3610 | dnaJ | SPRI_3610 | SPRI_3611 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular 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, [...] | 0.968 |
| SPRI_3610 | dnaJ-2 | SPRI_3610 | SPRI_4968 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular 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, [...] | 0.735 |
| SPRI_3610 | dnaK | SPRI_3610 | SPRI_3613 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.899 |
| SPRI_3610 | dnaK-2 | SPRI_3610 | SPRI_6203 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.700 |
| SPRI_3610 | groL | SPRI_3610 | SPRI_3124 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.508 |
| SPRI_3610 | groL-2 | SPRI_3610 | SPRI_4111 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.515 |
| SPRI_3610 | groS | SPRI_3610 | SPRI_3125 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.616 |
| SPRI_3610 | grpE | SPRI_3610 | SPRI_3612 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | 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 [...] | 0.988 |
| SPRI_3610 | hrcA | SPRI_3610 | SPRI_4967 | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | HrcA family transcriptional regulator; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.702 |
| SPRI_6202 | SPRI_3610 | SPRI_6202 | SPRI_3610 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | 0.735 |
| SPRI_6202 | dnaK | SPRI_6202 | SPRI_3613 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.949 |
| SPRI_6202 | dnaK-2 | SPRI_6202 | SPRI_6203 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.974 |
| SPRI_6202 | groL | SPRI_6202 | SPRI_3124 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.731 |
| SPRI_6202 | groL-2 | SPRI_6202 | SPRI_4111 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.731 |
| SPRI_6202 | groS | SPRI_6202 | SPRI_3125 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.689 |
| SPRI_6202 | grpE | SPRI_6202 | SPRI_3612 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | 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 [...] | 0.912 |
| SPRI_6202 | hrcA | SPRI_6202 | SPRI_4967 | Molecular chaperone DnaJ; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | HrcA family transcriptional regulator; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.811 |
| dnaJ | SPRI_3610 | SPRI_3611 | SPRI_3610 | Molecular 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, [...] | Heat-shock protein HspR; Derived by Prodigal V2.6.2 analysis using gene prediction method: Protein Homology. | 0.968 |
| dnaJ | dnaK | SPRI_3611 | SPRI_3613 | Molecular 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, [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |