| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANP63820.1 | ANP64709.1 | BAU10_01960 | BAU10_06800 | Fe-S cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.869 |
| ANP63820.1 | ANP64710.1 | BAU10_01960 | BAU10_06805 | Fe-S cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.869 |
| ANP63820.1 | dnaJ | BAU10_01960 | BAU10_02310 | Fe-S cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 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, [...] | 0.520 |
| ANP63820.1 | hscB | BAU10_01960 | BAU10_01970 | Fe-S cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | Fe-S protein assembly co-chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.999 |
| ANP64483.1 | ANP64709.1 | BAU10_05620 | BAU10_06800 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.803 |
| ANP64483.1 | ANP64710.1 | BAU10_05620 | BAU10_06805 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.803 |
| ANP64483.1 | groEL | BAU10_05620 | BAU10_14150 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.799 |
| ANP64483.1 | groEL-2 | BAU10_05620 | BAU10_16875 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.799 |
| ANP64483.1 | grpE | BAU10_05620 | BAU10_02295 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleotide exchange factor 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 [...] | 0.930 |
| ANP64483.1 | htpG | BAU10_05620 | BAU10_03165 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.927 |
| ANP64709.1 | ANP63820.1 | BAU10_06800 | BAU10_01960 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Fe-S cluster assembly scaffold IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 0.869 |
| ANP64709.1 | ANP64483.1 | BAU10_06800 | BAU10_05620 | Molecular chaperone DnaK; 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. | 0.803 |
| ANP64709.1 | ANP64710.1 | BAU10_06800 | BAU10_06805 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.819 |
| ANP64709.1 | ANP64711.1 | BAU10_06800 | BAU10_06810 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.949 |
| ANP64709.1 | dnaJ | BAU10_06800 | BAU10_02310 | Molecular chaperone DnaK; 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, [...] | 0.957 |
| ANP64709.1 | groEL | BAU10_06800 | BAU10_14150 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.826 |
| ANP64709.1 | groEL-2 | BAU10_06800 | BAU10_16875 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.826 |
| ANP64709.1 | grpE | BAU10_06800 | BAU10_02295 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleotide exchange factor 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 [...] | 0.923 |
| ANP64709.1 | hscB | BAU10_06800 | BAU10_01970 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Fe-S protein assembly co-chaperone HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.860 |
| ANP64709.1 | htpG | BAU10_06800 | BAU10_03165 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.939 |