| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dnaJ | dnaK | RPA0334 | RPA0333 | Heat shock protein DnaJ (40); 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 D [...] | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL1 | RPA0334 | RPA1140 | Heat shock protein DnaJ (40); 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 D [...] | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.970 |
| dnaJ | groEL2 | RPA0334 | RPA2164 | Heat shock protein DnaJ (40); 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 D [...] | Chaperonin GroEL2, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.972 |
| dnaJ | groES1 | RPA0334 | RPA1141 | Heat shock protein DnaJ (40); 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 D [...] | Chaperonin GroES1, cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.806 |
| dnaJ | grpE | RPA0334 | RPA0331 | Heat shock protein DnaJ (40); 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 D [...] | Possible heat shock protein (HSP-70 COFACTOR), grpE; 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 c [...] | 0.975 |
| dnaJ | hslU | RPA0334 | RPA0306 | Heat shock protein DnaJ (40); 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 D [...] | Heat shock protein HslU, proteasome-related ATPase subunit; 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. | 0.970 |
| dnaJ | hslV | RPA0334 | RPA0308 | Heat shock protein DnaJ (40); 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 D [...] | Heat shock protein HslV, proteasome-related peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.964 |
| dnaJ | htpG | RPA0334 | RPA4815 | Heat shock protein DnaJ (40); 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 D [...] | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.966 |
| dnaJ | tal | RPA0334 | RPA3634 | Heat shock protein DnaJ (40); 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 D [...] | Putative Transaldolase Phosphoglucose isomerase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway; Belongs to the GPI family. | 0.460 |
| dnaK | dnaJ | RPA0333 | RPA0334 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein DnaJ (40); 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 D [...] | 0.999 |
| dnaK | groEL1 | RPA0333 | RPA1140 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.988 |
| dnaK | groEL2 | RPA0333 | RPA2164 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroEL2, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.988 |
| dnaK | groES1 | RPA0333 | RPA1141 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroES1, cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.964 |
| dnaK | grpE | RPA0333 | RPA0331 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Possible heat shock protein (HSP-70 COFACTOR), grpE; 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 c [...] | 0.997 |
| dnaK | hslU | RPA0333 | RPA0306 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein HslU, proteasome-related ATPase subunit; 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. | 0.890 |
| dnaK | hslV | RPA0333 | RPA0308 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein HslV, proteasome-related peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.773 |
| dnaK | htpG | RPA0333 | RPA4815 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.993 |
| dnaK | rplL | RPA0333 | RPA3269 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 50S ribosomal protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family. | 0.613 |
| dnaK | tal | RPA0333 | RPA3634 | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative Transaldolase Phosphoglucose isomerase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway; Belongs to the GPI family. | 0.558 |
| groEL1 | dnaJ | RPA1140 | RPA0334 | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Heat shock protein DnaJ (40); 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 D [...] | 0.970 |
