| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PP_4849 | cbpA | PP_4849 | PP_4848 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | 0.938 |
| PP_4849 | cbpM | PP_4849 | PP_4847 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Chaperone modulatory of CbpA co-chaperone protein; Interacts with CbpA and inhibits both the DnaJ-like co- chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. | 0.669 |
| PP_4849 | clpA | PP_4849 | PP_4008 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | ATP-dependent serine protease; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides; Belongs to the ClpA/ClpB family. | 0.715 |
| PP_4849 | clpB | PP_4849 | PP_0625 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family. | 0.715 |
| PP_4849 | djlA | PP_4849 | PP_0407 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | DnaJ-like protein DjlA. | 0.704 |
| PP_4849 | groL | PP_4849 | PP_1361 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.905 |
| PP_4849 | grpE | PP_4849 | PP_4728 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Protein 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-dependent i [...] | 0.926 |
| PP_4849 | htpG | PP_4849 | PP_4179 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.898 |
| cbpA | PP_4849 | PP_4848 | PP_4849 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.938 |
| cbpA | cbpM | PP_4848 | PP_4847 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Chaperone modulatory of CbpA co-chaperone protein; Interacts with CbpA and inhibits both the DnaJ-like co- chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. | 0.995 |
| cbpA | clpA | PP_4848 | PP_4008 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | ATP-dependent serine protease; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Proteinfate : Degradation of proteins, peptides, and glycopeptides; Belongs to the ClpA/ClpB family. | 0.811 |
| cbpA | clpB | PP_4848 | PP_0625 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family. | 0.834 |
| cbpA | djlA | PP_4848 | PP_0407 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | DnaJ-like protein DjlA. | 0.804 |
| cbpA | dnaK | PP_4848 | PP_4727 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.976 |
| cbpA | groL | PP_4848 | PP_1361 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.876 |
| cbpA | grpE | PP_4848 | PP_4728 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Protein 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-dependent i [...] | 0.974 |
| cbpA | hscA | PP_4848 | PP_0846 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | DnaK-like molecular chaperone specific for IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.961 |
| cbpA | htpG | PP_4848 | PP_4179 | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.943 |
| cbpM | PP_4849 | PP_4847 | PP_4849 | Chaperone modulatory of CbpA co-chaperone protein; Interacts with CbpA and inhibits both the DnaJ-like co- chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.669 |
| cbpM | cbpA | PP_4847 | PP_4848 | Chaperone modulatory of CbpA co-chaperone protein; Interacts with CbpA and inhibits both the DnaJ-like co- chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. | Curved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. | 0.995 |
