node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
RPE_0414 | RPE_2484 | RPE_0414 | RPE_2484 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | 0.990 |
RPE_0414 | dnaJ | RPE_0414 | RPE_0348 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | 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 [...] | 0.967 |
RPE_0414 | groL1 | RPE_0414 | RPE_0861 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.934 |
RPE_0414 | groL2 | RPE_0414 | RPE_2283 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.934 |
RPE_0414 | groS | RPE_0414 | RPE_0862 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.888 |
RPE_0414 | groS-2 | RPE_0414 | RPE_2284 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.888 |
RPE_0414 | grpE | RPE_0414 | RPE_0351 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | 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 [...] | 0.987 |
RPE_0414 | hslU | RPE_0414 | RPE_0372 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | 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. | 0.741 |
RPE_0414 | htpG | RPE_0414 | RPE_4897 | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.990 |
RPE_2484 | RPE_0414 | RPE_2484 | RPE_0414 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | 0.990 |
RPE_2484 | dnaJ | RPE_2484 | RPE_0348 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | 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 [...] | 0.970 |
RPE_2484 | dnaK | RPE_2484 | RPE_0349 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.994 |
RPE_2484 | groL1 | RPE_2484 | RPE_0861 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.888 |
RPE_2484 | groL2 | RPE_2484 | RPE_2283 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.888 |
RPE_2484 | groS | RPE_2484 | RPE_0862 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.804 |
RPE_2484 | groS-2 | RPE_2484 | RPE_2284 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.804 |
RPE_2484 | grpE | RPE_2484 | RPE_0351 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | 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 [...] | 0.874 |
RPE_2484 | hslU | RPE_2484 | RPE_0372 | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | 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. | 0.872 |
dnaJ | RPE_0414 | RPE_0348 | RPE_0414 | 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 [...] | KEGG: rpc:RPC_0260 molecular chaperone, HSP70 class. | 0.967 |
dnaJ | RPE_2484 | RPE_0348 | RPE_2484 | 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 [...] | PFAM: ATP-binding region, ATPase domain protein domain protein; KEGG: rpd:RPD_3368 ATP-binding region, ATPase-like. | 0.970 |