node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BF93_05825 | BF93_08965 | BF93_05825 | BF93_08965 | Chaperone HscA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.656 |
BF93_05825 | BF93_08970 | BF93_05825 | BF93_08970 | Chaperone HscA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.969 |
BF93_05825 | clpB | BF93_05825 | BF93_08750 | Chaperone HscA; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase AAA; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.937 |
BF93_05825 | dnaJ | BF93_05825 | BF93_06150 | Chaperone HscA; Derived by automated computational 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, [...] | 0.971 |
BF93_05825 | groEL | BF93_05825 | BF93_13760 | Chaperone HscA; Derived by automated computational 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. | 0.861 |
BF93_05825 | groEL-2 | BF93_05825 | BF93_16965 | Chaperone HscA; Derived by automated computational 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. | 0.861 |
BF93_05825 | groS | BF93_05825 | BF93_13755 | Chaperone HscA; Derived by automated computational 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. | 0.865 |
BF93_05825 | grpE | BF93_05825 | BF93_08975 | Chaperone HscA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular 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 [...] | 0.986 |
BF93_05825 | hrcA | BF93_05825 | BF93_06145 | Chaperone HscA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.812 |
BF93_08965 | BF93_05825 | BF93_08965 | BF93_05825 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone HscA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.656 |
BF93_08965 | BF93_08970 | BF93_08965 | BF93_08970 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.928 |
BF93_08965 | clpB | BF93_08965 | BF93_08750 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase AAA; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.478 |
BF93_08965 | dnaJ | BF93_08965 | BF93_06150 | Transcriptional regulator; Derived by automated computational 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, [...] | 0.800 |
BF93_08965 | dnaK | BF93_08965 | BF93_08980 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.795 |
BF93_08965 | groEL | BF93_08965 | BF93_13760 | Transcriptional regulator; Derived by automated computational 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. | 0.437 |
BF93_08965 | groEL-2 | BF93_08965 | BF93_16965 | Transcriptional regulator; Derived by automated computational 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. | 0.437 |
BF93_08965 | groS | BF93_08965 | BF93_13755 | Transcriptional regulator; Derived by automated computational 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. | 0.473 |
BF93_08965 | grpE | BF93_08965 | BF93_08975 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular 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 [...] | 0.957 |
BF93_08965 | hrcA | BF93_08965 | BF93_06145 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.675 |
BF93_08970 | BF93_05825 | BF93_08970 | BF93_05825 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone HscA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.969 |