node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CbpA | DnaK | PTH_2123 | PTH_0878 | DnaJ-class molecular chaperone. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
CbpA | GroL-2 | PTH_2123 | PTH_2605 | DnaJ-class molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.833 |
CbpA | GroS | PTH_2123 | PTH_2607 | DnaJ-class molecular chaperone. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.788 |
CbpA | GrpE | PTH_2123 | PTH_0877 | DnaJ-class molecular chaperone. | Molecular chaperone 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 cycle. Several rounds of ATP [...] | 0.967 |
CbpA | HtpG | PTH_2123 | PTH_0110 | DnaJ-class molecular chaperone. | Molecular chaperone; Molecular chaperone. Has ATPase activity. | 0.967 |
CbpA | PTH_0142 | PTH_2123 | PTH_0142 | DnaJ-class molecular chaperone. | Hypothetical protein; Containing predicted ATPase (COG3899), FhlA, FOG: GAF domain (COG2203), S_TKc, serine/threonine protein kinases, catalytic domain, His Kinase A (phosphoacceptor), HATPase_c, Histidine kinase-like ATPase, REC, signal receiver domain, and ArcB, FOG: HPt domain (COG2198). | 0.590 |
DnaJ | DnaK | PTH_0879 | PTH_0878 | DnaJ-class molecular chaperone; 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 [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
DnaJ | GroL-2 | PTH_0879 | PTH_2605 | DnaJ-class molecular chaperone; 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.803 |
DnaJ | GroS | PTH_0879 | PTH_2607 | DnaJ-class molecular chaperone; 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 [...] | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.758 |
DnaJ | GrpE | PTH_0879 | PTH_0877 | DnaJ-class molecular chaperone; 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 [...] | Molecular chaperone 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 cycle. Several rounds of ATP [...] | 0.988 |
DnaJ | HtpG | PTH_0879 | PTH_0110 | DnaJ-class molecular chaperone; 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 [...] | Molecular chaperone; Molecular chaperone. Has ATPase activity. | 0.961 |
DnaJ | PTH_0142 | PTH_0879 | PTH_0142 | DnaJ-class molecular chaperone; 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 [...] | Hypothetical protein; Containing predicted ATPase (COG3899), FhlA, FOG: GAF domain (COG2203), S_TKc, serine/threonine protein kinases, catalytic domain, His Kinase A (phosphoacceptor), HATPase_c, Histidine kinase-like ATPase, REC, signal receiver domain, and ArcB, FOG: HPt domain (COG2198). | 0.590 |
DnaK | CbpA | PTH_0878 | PTH_2123 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DnaJ-class molecular chaperone. | 0.997 |
DnaK | DnaJ | PTH_0878 | PTH_0879 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DnaJ-class molecular chaperone; 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 [...] | 0.998 |
DnaK | FliY | PTH_0878 | PTH_2060 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Flagellum motor switch protein. | 0.404 |
DnaK | GroL-2 | PTH_0878 | PTH_2605 | Molecular chaperone; Acts as a chaperone; 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. | 0.963 |
DnaK | GroS | PTH_0878 | PTH_2607 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.968 |
DnaK | GrpE | PTH_0878 | PTH_0877 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperone 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 cycle. Several rounds of ATP [...] | 0.999 |
DnaK | HtpG | PTH_0878 | PTH_0110 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperone; Molecular chaperone. Has ATPase activity. | 0.997 |
DnaK | PTH_0142 | PTH_0878 | PTH_0142 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical protein; Containing predicted ATPase (COG3899), FhlA, FOG: GAF domain (COG2203), S_TKc, serine/threonine protein kinases, catalytic domain, His Kinase A (phosphoacceptor), HATPase_c, Histidine kinase-like ATPase, REC, signal receiver domain, and ArcB, FOG: HPt domain (COG2198). | 0.788 |