| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| WI67_13835 | WL94_08925 | DM42_2502 | DM42_2503 | Co-chaperone YbbN; Thioredoxin- thioredoxin | annotation not available | 0.686 |
| WI67_13835 | WL94_15815 | DM42_2502 | DM42_1419 | Co-chaperone YbbN; Thioredoxin- thioredoxin | annotation not available | 0.980 |
| WI67_13835 | clpB | DM42_2502 | DM42_3253 | Co-chaperone YbbN; Thioredoxin- thioredoxin | Chaperone protein ClpB; 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 | 0.701 |
| WI67_13835 | dnaJ | DM42_2502 | DM42_1085 | Co-chaperone YbbN; Thioredoxin- thioredoxin | Chaperone protein 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, D [...] | 0.696 |
| WI67_13835 | dnaK | DM42_2502 | DM42_1086 | Co-chaperone YbbN; Thioredoxin- thioredoxin | Chaperone protein DnaK; Acts as a chaperone | 0.725 |
| WI67_13835 | grpE | DM42_2502 | DM42_1088 | Co-chaperone YbbN; Thioredoxin- thioredoxin | Protein 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- dependent [...] | 0.764 |
| WI67_13835 | hslU | DM42_2502 | DM42_1920 | Co-chaperone YbbN; Thioredoxin- thioredoxin | ATP-dependent protease ATPase 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 | 0.728 |
| WI67_13835 | hslV | DM42_2502 | DM42_1921 | Co-chaperone YbbN; Thioredoxin- thioredoxin | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery | 0.596 |
| WI67_13835 | htpG | DM42_2502 | DM42_2714 | Co-chaperone YbbN; Thioredoxin- thioredoxin | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity | 0.722 |
| WI67_13835 | trxB | DM42_2502 | DM42_867 | Co-chaperone YbbN; Thioredoxin- thioredoxin | TRX_reduct- thioredoxin-disulfide reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family | 0.616 |
| WL94_08925 | WI67_13835 | DM42_2503 | DM42_2502 | annotation not available | Co-chaperone YbbN; Thioredoxin- thioredoxin | 0.686 |
| WL94_15815 | WI67_13835 | DM42_1419 | DM42_2502 | annotation not available | Co-chaperone YbbN; Thioredoxin- thioredoxin | 0.980 |
| WL94_15815 | dnaK | DM42_1419 | DM42_1086 | annotation not available | Chaperone protein DnaK; Acts as a chaperone | 0.580 |
| WL94_15815 | grpE | DM42_1419 | DM42_1088 | annotation not available | Protein 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- dependent [...] | 0.479 |
| WL94_15815 | trxB | DM42_1419 | DM42_867 | annotation not available | TRX_reduct- thioredoxin-disulfide reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family | 0.629 |
| clpB | WI67_13835 | DM42_3253 | DM42_2502 | Chaperone protein ClpB; 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 | Co-chaperone YbbN; Thioredoxin- thioredoxin | 0.701 |
| clpB | dnaJ | DM42_3253 | DM42_1085 | Chaperone protein ClpB; 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 | Chaperone protein 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, D [...] | 0.919 |
| clpB | dnaK | DM42_3253 | DM42_1086 | Chaperone protein ClpB; 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 | Chaperone protein DnaK; Acts as a chaperone | 0.988 |
| clpB | grpE | DM42_3253 | DM42_1088 | Chaperone protein ClpB; 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 | Protein 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- dependent [...] | 0.968 |
| clpB | hslU | DM42_3253 | DM42_1920 | Chaperone protein ClpB; 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 | ATP-dependent protease ATPase 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 | 0.864 |
