node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AKH37162.1 | AKH37163.1 | AAW31_03955 | AAW31_03960 | 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. | 0.800 |
AKH37162.1 | dnaJ | AAW31_03955 | AAW31_14635 | 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, [...] | 0.950 |
AKH37162.1 | groEL | AAW31_03955 | AAW31_05965 | Molecular chaperone DnaK; 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. | 0.853 |
AKH37162.1 | groS | AAW31_03955 | AAW31_05970 | Molecular chaperone DnaK; 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. | 0.837 |
AKH37162.1 | grpE | AAW31_03955 | AAW31_14645 | Molecular chaperone DnaK; 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 [...] | 0.968 |
AKH37162.1 | hslU | AAW31_03955 | AAW31_08475 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.683 |
AKH37162.1 | htpG | AAW31_03955 | AAW31_03810 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.989 |
AKH37163.1 | AKH37162.1 | AAW31_03960 | AAW31_03955 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.800 |
AKH37163.1 | dnaJ | AAW31_03960 | AAW31_14635 | Molecular chaperone DnaK; 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, [...] | 0.950 |
AKH37163.1 | groEL | AAW31_03960 | AAW31_05965 | Molecular chaperone DnaK; 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. | 0.853 |
AKH37163.1 | groS | AAW31_03960 | AAW31_05970 | Molecular chaperone DnaK; 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. | 0.837 |
AKH37163.1 | grpE | AAW31_03960 | AAW31_14645 | Molecular chaperone DnaK; 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 [...] | 0.968 |
AKH37163.1 | hslU | AAW31_03960 | AAW31_08475 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.683 |
AKH37163.1 | htpG | AAW31_03960 | AAW31_03810 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.989 |
AKH37170.1 | AKH37213.1 | AAW31_03995 | AAW31_04335 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
AKH37170.1 | dnaJ | AAW31_03995 | AAW31_14635 | Hypothetical protein; 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, [...] | 0.956 |
AKH37170.1 | groEL | AAW31_03995 | AAW31_05965 | Hypothetical protein; 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. | 0.500 |
AKH37170.1 | groS | AAW31_03995 | AAW31_05970 | Hypothetical protein; 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. | 0.589 |
AKH37213.1 | AKH37170.1 | AAW31_04335 | AAW31_03995 | NADP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
AKH37213.1 | dnaJ | AAW31_04335 | AAW31_14635 | NADP oxidoreductase; 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, [...] | 0.910 |