| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KMK92188.1 | KMK92809.1 | VL01_15940 | VL01_13875 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.909 |
| KMK92188.1 | dnaK | VL01_15940 | VL01_08420 | Molecular chaperone DnaJ; 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. | 0.980 |
| KMK92188.1 | groEL | VL01_15940 | VL01_14435 | Molecular chaperone DnaJ; 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. | 0.931 |
| KMK92188.1 | groES | VL01_15940 | VL01_14440 | Molecular chaperone DnaJ; 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. | 0.737 |
| KMK92188.1 | grpE | VL01_15940 | VL01_08425 | Molecular chaperone DnaJ; 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 |
| KMK92188.1 | hscA | VL01_15940 | VL01_04140 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.970 |
| KMK92188.1 | hslU | VL01_15940 | VL01_13720 | Molecular chaperone DnaJ; 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. | 0.844 |
| KMK92188.1 | hslV | VL01_15940 | VL01_13715 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.808 |
| KMK92188.1 | htpG | VL01_15940 | VL01_04705 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.959 |
| KMK92809.1 | KMK92188.1 | VL01_13875 | VL01_15940 | Chaperone; 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. | 0.909 |
| KMK92809.1 | dnaJ | VL01_13875 | VL01_08415 | Chaperone; 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, [...] | 0.912 |
| KMK92809.1 | groEL | VL01_13875 | VL01_14435 | Chaperone; 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. | 0.959 |
| KMK92809.1 | groES | VL01_13875 | VL01_14440 | Chaperone; 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. | 0.932 |
| KMK92809.1 | grpE | VL01_13875 | VL01_08425 | Chaperone; 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 [...] | 0.961 |
| KMK92809.1 | hslU | VL01_13875 | VL01_13720 | Chaperone; 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. | 0.535 |
| KMK92809.1 | hslV | VL01_13875 | VL01_13715 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.498 |
| KMK92809.1 | htpG | VL01_13875 | VL01_04705 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.955 |
| dnaJ | KMK92809.1 | VL01_08415 | VL01_13875 | 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, [...] | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.912 |
| dnaJ | dnaK | VL01_08415 | VL01_08420 | 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. | 0.999 |
| dnaJ | groEL | VL01_08415 | VL01_14435 | 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. | 0.987 |
