| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AIA74823.1 | clpB | FF32_08215 | FF32_03040 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protein disaggregation chaperone; 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. | 0.428 |
| AIA74823.1 | dnaJ | FF32_08215 | FF32_07865 | Thioredoxin; 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, [...] | 0.706 |
| AIA74823.1 | dnaK | FF32_08215 | FF32_07860 | Thioredoxin; 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. | 0.656 |
| AIA74823.1 | groEL | FF32_08215 | FF32_16240 | Thioredoxin; 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. | 0.676 |
| AIA74823.1 | groES | FF32_08215 | FF32_16235 | Thioredoxin; 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. | 0.593 |
| AIA74823.1 | grpE | FF32_08215 | FF32_07855 | Thioredoxin; 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 [...] | 0.855 |
| AIA74823.1 | hslU | FF32_08215 | FF32_02520 | Thioredoxin; 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. | 0.871 |
| AIA74823.1 | hslV | FF32_08215 | FF32_02515 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.856 |
| AIA74823.1 | htpG | FF32_08215 | FF32_17720 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.752 |
| AIA76153.1 | clpB | FF32_15295 | FF32_03040 | Energy transducer TonB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protein disaggregation chaperone; 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. | 0.627 |
| AIA76153.1 | dnaK | FF32_15295 | FF32_07860 | Energy transducer TonB; 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. | 0.971 |
| AIA76153.1 | groEL | FF32_15295 | FF32_16240 | Energy transducer TonB; 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. | 0.755 |
| AIA76153.1 | groES | FF32_15295 | FF32_16235 | Energy transducer TonB; 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. | 0.617 |
| AIA76153.1 | grpE | FF32_15295 | FF32_07855 | Energy transducer TonB; 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 [...] | 0.863 |
| AIA76153.1 | hslU | FF32_15295 | FF32_02520 | Energy transducer TonB; 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. | 0.651 |
| AIA76153.1 | hslV | FF32_15295 | FF32_02515 | Energy transducer TonB; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.555 |
| AIA76153.1 | htpG | FF32_15295 | FF32_17720 | Energy transducer TonB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.909 |
| clpB | AIA74823.1 | FF32_03040 | FF32_08215 | Protein disaggregation chaperone; 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. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.428 |
| clpB | AIA76153.1 | FF32_03040 | FF32_15295 | Protein disaggregation chaperone; 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. | Energy transducer TonB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.627 |
| clpB | dnaJ | FF32_03040 | FF32_07865 | Protein disaggregation chaperone; 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. | 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, [...] | 0.659 |