node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Aave_3228 | Aave_4256 | Aave_3228 | Aave_4256 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like. | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | 0.958 |
Aave_3228 | dnaK | Aave_3228 | Aave_1226 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
Aave_3228 | groL | Aave_3228 | Aave_0945 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.835 |
Aave_3228 | groS | Aave_3228 | Aave_0946 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.712 |
Aave_3228 | grpE | Aave_3228 | Aave_1227 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-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 [...] | 0.962 |
Aave_3228 | hslU | Aave_3228 | Aave_0811 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-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. | 0.688 |
Aave_3228 | hslV | Aave_3228 | Aave_0810 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like. | HslV component of HslUV peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.581 |
Aave_3228 | htpG | Aave_3228 | Aave_4289 | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.948 |
Aave_3490 | groL | Aave_3490 | Aave_0945 | PFAM: diacylglycerol kinase, catalytic region; KEGG: rfr:Rfer_2359 diacylglycerol kinase. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.875 |
Aave_4256 | Aave_3228 | Aave_4256 | Aave_3228 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | PFAM: heat shock protein DnaJ domain protein; KEGG: pol:Bpro_3897 heat shock protein DnaJ-like. | 0.958 |
Aave_4256 | dnaJ | Aave_4256 | Aave_1225 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | 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 [...] | 0.983 |
Aave_4256 | groL | Aave_4256 | Aave_0945 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.816 |
Aave_4256 | groS | Aave_4256 | Aave_0946 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.721 |
Aave_4256 | grpE | Aave_4256 | Aave_1227 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | 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 [...] | 0.940 |
Aave_4256 | hslU | Aave_4256 | Aave_0811 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | 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. | 0.552 |
Aave_4256 | hslV | Aave_4256 | Aave_0810 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | HslV component of HslUV peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.502 |
Aave_4256 | htpG | Aave_4256 | Aave_4289 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.938 |
dnaJ | Aave_4256 | Aave_1225 | Aave_4256 | 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: Heat shock protein 70; KEGG: rso:RSp0521 probable chaperone transmembrane protein. | 0.983 |
dnaJ | dnaK | Aave_1225 | Aave_1226 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.994 |
dnaJ | groL | Aave_1225 | Aave_0945 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.915 |