node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACS84857.1 | clpB | Dd703_1052 | Dd703_2848 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | ATP-dependent chaperone 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. | 0.532 |
ACS84857.1 | dnaJ | Dd703_1052 | Dd703_0582 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative 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 [...] | 0.637 |
ACS84857.1 | dnaK | Dd703_1052 | Dd703_0581 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.577 |
ACS84857.1 | groL | Dd703_1052 | Dd703_3403 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.622 |
ACS84857.1 | groS | Dd703_1052 | Dd703_3404 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.558 |
ACS84857.1 | grpE | Dd703_1052 | Dd703_3216 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | GrpE protein; 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 i [...] | 0.817 |
ACS84857.1 | hscA | Dd703_1052 | Dd703_2747 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. | 0.523 |
ACS84857.1 | hslU | Dd703_1052 | Dd703_3798 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Heat shock protein HslVU, 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. | 0.819 |
ACS84857.1 | hslV | Dd703_1052 | Dd703_3797 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.817 |
ACS85411.1 | clpB | Dd703_1614 | Dd703_2848 | KEGG: eca:ECA1820 putative chaperone. | ATP-dependent chaperone 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. | 0.858 |
ACS85411.1 | dnaJ | Dd703_1614 | Dd703_0582 | KEGG: eca:ECA1820 putative chaperone. | 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 [...] | 0.952 |
ACS85411.1 | groL | Dd703_1614 | Dd703_3403 | KEGG: eca:ECA1820 putative chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.825 |
ACS85411.1 | groS | Dd703_1614 | Dd703_3404 | KEGG: eca:ECA1820 putative chaperone. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.769 |
ACS85411.1 | grpE | Dd703_1614 | Dd703_3216 | KEGG: eca:ECA1820 putative chaperone. | GrpE protein; 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 i [...] | 0.904 |
ACS85411.1 | hslU | Dd703_1614 | Dd703_3798 | KEGG: eca:ECA1820 putative chaperone. | Heat shock protein HslVU, 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. | 0.522 |
ACS85411.1 | hslV | Dd703_1614 | Dd703_3797 | KEGG: eca:ECA1820 putative chaperone. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.509 |
clpB | ACS84857.1 | Dd703_2848 | Dd703_1052 | ATP-dependent chaperone 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. | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 0.532 |
clpB | ACS85411.1 | Dd703_2848 | Dd703_1614 | ATP-dependent chaperone 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. | KEGG: eca:ECA1820 putative chaperone. | 0.858 |
clpB | dnaJ | Dd703_2848 | Dd703_0582 | ATP-dependent chaperone 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 [...] | 0.784 |
clpB | dnaK | Dd703_2848 | Dd703_0581 | ATP-dependent chaperone 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; Belongs to the heat shock protein 70 family. | 0.969 |