| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SO_1850 | clpA | SO_1850 | SO_2626 | DnaJ domain protein. | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 0.708 |
| SO_1850 | clpB | SO_1850 | SO_3577 | DnaJ domain protein. | Stress-induced multi-chaperone system component 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 [...] | 0.710 |
| SO_1850 | dnaK | SO_1850 | SO_1126 | DnaJ domain protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.958 |
| SO_1850 | groEL | SO_1850 | SO_0704 | DnaJ domain protein. | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.775 |
| SO_1850 | groES | SO_1850 | SO_0703 | DnaJ domain protein. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.693 |
| SO_1850 | grpE | SO_1850 | SO_1524 | DnaJ domain protein. | Heat shock nucleotide exchange factor 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. Sev [...] | 0.902 |
| SO_1850 | hscB | SO_1850 | SO_2267 | DnaJ domain protein. | Co-chaperone Hsc20 HscB; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA; Belongs to the HscB family. | 0.770 |
| SO_1850 | htpG | SO_1850 | SO_2016 | DnaJ domain protein. | Heat shock chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.931 |
| SO_1850 | iscU | SO_1850 | SO_2265 | DnaJ domain protein. | FeS cluster assembly scaffold protein IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. | 0.524 |
| clpA | SO_1850 | SO_2626 | SO_1850 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | DnaJ domain protein. | 0.708 |
| clpA | dnaJ | SO_2626 | SO_1127 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB 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 [...] | 0.838 |
| clpA | dnaK | SO_2626 | SO_1126 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.911 |
| clpA | groEL | SO_2626 | SO_0704 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.680 |
| clpA | groES | SO_2626 | SO_0703 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.690 |
| clpA | grpE | SO_2626 | SO_1524 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | Heat shock nucleotide exchange factor 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. Sev [...] | 0.921 |
| clpA | htpG | SO_2626 | SO_2016 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | Heat shock chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.792 |
| clpB | SO_1850 | SO_3577 | SO_1850 | Stress-induced multi-chaperone system component 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 [...] | DnaJ domain protein. | 0.710 |
| clpB | dnaJ | SO_3577 | SO_1127 | Stress-induced multi-chaperone system component 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 [...] | 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 [...] | 0.917 |
| clpB | dnaK | SO_3577 | SO_1126 | Stress-induced multi-chaperone system component 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.967 |
| clpB | groEL | SO_3577 | SO_0704 | Stress-induced multi-chaperone system component 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 [...] | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.907 |
STRING v12.5 is now available!
