| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Acid_0977 | dnaJ | Acid_0977 | Acid_0734 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 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 [...] | 0.836 |
| Acid_0977 | dnaJ-2 | Acid_0977 | Acid_7483 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | Chaperone DnaJ domain protein; 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 [...] | 0.836 |
| Acid_0977 | groL | Acid_0977 | Acid_6747 | KEGG: reu:Reut_A1752 putative heat-shock chaperone 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. | 0.974 |
| Acid_0977 | groS | Acid_0977 | Acid_4789 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.809 |
| Acid_0977 | grpE | Acid_0977 | Acid_0733 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | 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 [...] | 0.964 |
| Acid_0977 | hrcA | Acid_0977 | Acid_0732 | KEGG: reu:Reut_A1752 putative heat-shock chaperone 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. | 0.488 |
| Acid_0981 | dnaJ | Acid_0981 | Acid_0734 | PFAM: Heat shock protein 70; KEGG: bur:Bcep18194_B2544 molecular chaperone-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 [...] | 0.836 |
| Acid_0981 | dnaJ-2 | Acid_0981 | Acid_7483 | PFAM: Heat shock protein 70; KEGG: bur:Bcep18194_B2544 molecular chaperone-like. | Chaperone DnaJ domain protein; 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 [...] | 0.836 |
| Acid_0981 | groL | Acid_0981 | Acid_6747 | PFAM: Heat shock protein 70; KEGG: bur:Bcep18194_B2544 molecular chaperone-like. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.974 |
| Acid_0981 | groS | Acid_0981 | Acid_4789 | PFAM: Heat shock protein 70; KEGG: bur:Bcep18194_B2544 molecular chaperone-like. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.809 |
| Acid_0981 | grpE | Acid_0981 | Acid_0733 | PFAM: Heat shock protein 70; KEGG: bur:Bcep18194_B2544 molecular chaperone-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 [...] | 0.964 |
| Acid_0981 | hrcA | Acid_0981 | Acid_0732 | PFAM: Heat shock protein 70; KEGG: bur:Bcep18194_B2544 molecular chaperone-like. | 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. | 0.488 |
| Acid_5615 | dnaJ | Acid_5615 | Acid_0734 | KEGG: mag:amb4304 molecular 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 [...] | 0.862 |
| Acid_5615 | dnaJ-2 | Acid_5615 | Acid_7483 | KEGG: mag:amb4304 molecular chaperone. | Chaperone DnaJ domain protein; 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 [...] | 0.866 |
| Acid_5615 | groL | Acid_5615 | Acid_6747 | KEGG: mag:amb4304 molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.974 |
| Acid_5615 | groS | Acid_5615 | Acid_4789 | KEGG: mag:amb4304 molecular chaperone. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.809 |
| Acid_5615 | grpE | Acid_5615 | Acid_0733 | KEGG: mag:amb4304 molecular 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 [...] | 0.964 |
| Acid_5615 | hrcA | Acid_5615 | Acid_0732 | KEGG: mag:amb4304 molecular chaperone. | 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. | 0.549 |
| Acid_6320 | dnaJ | Acid_6320 | Acid_0734 | PFAM: Heat shock protein 70; KEGG: tma:TM0373 dnaK 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 [...] | 0.962 |
| Acid_6320 | dnaJ-2 | Acid_6320 | Acid_7483 | PFAM: Heat shock protein 70; KEGG: tma:TM0373 dnaK protein. | Chaperone DnaJ domain protein; 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 [...] | 0.962 |
