| 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 | dnaJ | PP_4849 | PP_4726 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 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 |
| PP_4849 | groS | PP_4849 | PP_1360 | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.871 |
| 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 |
| 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 | groS | PP_4848 | PP_1360 | 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. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.693 |
| 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 | hslR | PP_4848 | PP_0250 | 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. | Heat shock protein Hsp15 involved in ribosome recycling; Function of homologous gene experimentally demonstrated in an other organism; factor; Cellularprocesses : Adaptations to atypical conditions; Belongs to the HSP15 family. | 0.641 |
| cbpA | htpX | PP_4848 | PP_1871 | 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. | Protease HtpX; Belongs to the peptidase M48B family. | 0.579 |
| 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 |
| cbpM | dnaJ | PP_4847 | PP_4726 | 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. | 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 [...] | 0.581 |
| cbpM | groS | PP_4847 | PP_1360 | 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. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.430 |
| cbpM | grpE | PP_4847 | PP_4728 | 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. | 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 [...] | 0.535 |
| cbpM | hslR | PP_4847 | PP_0250 | 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. | Heat shock protein Hsp15 involved in ribosome recycling; Function of homologous gene experimentally demonstrated in an other organism; factor; Cellularprocesses : Adaptations to atypical conditions; Belongs to the HSP15 family. | 0.743 |
| cbpM | htpX | PP_4847 | PP_1871 | 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. | Protease HtpX; Belongs to the peptidase M48B family. | 0.505 |
| dnaJ | PP_4849 | PP_4726 | PP_4849 | 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 [...] | Putative DnaK protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.862 |
| dnaJ | cbpM | PP_4726 | PP_4847 | 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 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. | 0.581 |
