| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ORV42561.1 | ORV43806.1 | AWC00_11380 | AWC00_08855 | Iron-sulfur cluster assembly scaffold protein NifU; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.886 |
| ORV42561.1 | dnaJ | AWC00_11380 | AWC00_00760 | Iron-sulfur cluster assembly scaffold protein NifU; 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, [...] | 0.696 |
| ORV42561.1 | dnaJ-2 | AWC00_11380 | AWC00_24775 | Iron-sulfur cluster assembly scaffold protein NifU; 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, [...] | 0.696 |
| ORV42561.1 | dnaK | AWC00_11380 | AWC00_24765 | Iron-sulfur cluster assembly scaffold protein NifU; 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. | 0.886 |
| ORV43806.1 | ORV42561.1 | AWC00_08855 | AWC00_11380 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Iron-sulfur cluster assembly scaffold protein NifU; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.886 |
| ORV43806.1 | dnaJ | AWC00_08855 | AWC00_00760 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 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, [...] | 0.962 |
| ORV43806.1 | dnaJ-2 | AWC00_08855 | AWC00_24775 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 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, [...] | 0.955 |
| ORV43806.1 | dnaK | AWC00_08855 | AWC00_24765 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.878 |
| ORV43806.1 | groEL | AWC00_08855 | AWC00_15275 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.917 |
| ORV43806.1 | groEL-2 | AWC00_08855 | AWC00_25710 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.916 |
| ORV43806.1 | groS | AWC00_08855 | AWC00_15270 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.899 |
| ORV43806.1 | grpE | AWC00_08855 | AWC00_24770 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 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 [...] | 0.955 |
| ORV43806.1 | htpG | AWC00_08855 | AWC00_27240 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.947 |
| ORV43806.1 | kgd | AWC00_08855 | AWC00_28325 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Alpha-ketoglutarate decarboxylase; Kgd; produces succinic semialdehyde; part of alternative pathway from alpha-ketoglutarate to succinate; essential for normal growth; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.839 |
| dnaJ | ORV42561.1 | AWC00_00760 | AWC00_11380 | 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, [...] | Iron-sulfur cluster assembly scaffold protein NifU; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.696 |
| dnaJ | ORV43806.1 | AWC00_00760 | AWC00_08855 | 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 Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.962 |
| dnaJ | dnaK | AWC00_00760 | AWC00_24765 | 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. | 0.993 |
| dnaJ | groEL | AWC00_00760 | AWC00_15275 | 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 GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.953 |
| dnaJ | groEL-2 | AWC00_00760 | AWC00_25710 | 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 GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.953 |
| dnaJ | groS | AWC00_00760 | AWC00_15270 | 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 GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.746 |
