node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DM42_1340 | clpB | DM42_1340 | DM42_3253 | annotation not available | Atp-dependent clp protease atp-binding subunit 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 | 0.604 |
DM42_1340 | dnaJ | DM42_1340 | DM42_1085 | annotation not available | 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, DnaK and GrpE are require [...] | 0.864 |
DM42_1340 | groL | DM42_1340 | DM42_4542 | annotation not available | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.818 |
DM42_1340 | grpE | DM42_1340 | DM42_1088 | annotation not available | 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 interactions be [...] | 0.947 |
DM42_1340 | hrcA | DM42_1340 | DM42_1092 | annotation not available | Heat-inducible transcription repressor hrca; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons | 0.786 |
DM42_1340 | hslU | DM42_1340 | DM42_1920 | annotation not available | Atp-dependent hsluv 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 | 0.442 |
DM42_4488 | DM42_4489 | DM42_4488 | DM42_4489 | annotation not available | Hsp70 family protein; Belongs to the heat shock protein 70 family | 0.904 |
DM42_4488 | clpB | DM42_4488 | DM42_3253 | annotation not available | Atp-dependent clp protease atp-binding subunit 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 | 0.513 |
DM42_4488 | dnaJ | DM42_4488 | DM42_1085 | annotation not available | 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, DnaK and GrpE are require [...] | 0.798 |
DM42_4488 | groL | DM42_4488 | DM42_4542 | annotation not available | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.793 |
DM42_4488 | grpE | DM42_4488 | DM42_1088 | annotation not available | 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 interactions be [...] | 0.939 |
DM42_4488 | hrcA | DM42_4488 | DM42_1092 | annotation not available | Heat-inducible transcription repressor hrca; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons | 0.768 |
DM42_4488 | hslU | DM42_4488 | DM42_1920 | annotation not available | Atp-dependent hsluv 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 | 0.442 |
DM42_4489 | DM42_4488 | DM42_4489 | DM42_4488 | Hsp70 family protein; Belongs to the heat shock protein 70 family | annotation not available | 0.904 |
DM42_4489 | clpB | DM42_4489 | DM42_3253 | Hsp70 family protein; Belongs to the heat shock protein 70 family | Atp-dependent clp protease atp-binding subunit 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 | 0.513 |
DM42_4489 | dnaJ | DM42_4489 | DM42_1085 | Hsp70 family protein; Belongs to the heat shock protein 70 family | 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, DnaK and GrpE are require [...] | 0.798 |
DM42_4489 | groL | DM42_4489 | DM42_4542 | Hsp70 family protein; Belongs to the heat shock protein 70 family | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.793 |
DM42_4489 | grpE | DM42_4489 | DM42_1088 | Hsp70 family protein; Belongs to the heat shock protein 70 family | 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 interactions be [...] | 0.939 |
DM42_4489 | hrcA | DM42_4489 | DM42_1092 | Hsp70 family protein; Belongs to the heat shock protein 70 family | Heat-inducible transcription repressor hrca; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons | 0.768 |
DM42_4489 | hslU | DM42_4489 | DM42_1920 | Hsp70 family protein; Belongs to the heat shock protein 70 family | Atp-dependent hsluv 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 | 0.442 |