| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RSc3436 | RSp0522 | RSc3436 | RSp0522 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Probable transmembrane protein. | 0.530 |
| RSc3436 | clpB | RSc3436 | RSc1335 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Probable chaperone clpb protein; 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. | 0.640 |
| RSc3436 | dnaJ | RSc3436 | RSc2634 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Probable 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 betwee [...] | 0.955 |
| RSc3436 | grpE | RSc3436 | RSc2639 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Probable protein grpe (hsp-70 cofactor); 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. Severa [...] | 0.745 |
| RSc3436 | hscC | RSc3436 | RSp0521 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Probable chaperone transmembrane protein; Belongs to the heat shock protein 70 family. | 0.833 |
| RSc3436 | mopA | RSc3436 | RSc0642 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Probable 60 kda chaperonin (protein cpn60) (groel protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.916 |
| RSc3436 | mopB | RSc3436 | RSc0641 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Probable 10 kda chaperonin (protein cpn10) (groes protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.766 |
| RSp0522 | RSc3436 | RSp0522 | RSc3436 | Probable transmembrane protein. | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | 0.530 |
| RSp0522 | dnaJ | RSp0522 | RSc2634 | Probable transmembrane protein. | Probable 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 betwee [...] | 0.606 |
| RSp0522 | hscC | RSp0522 | RSp0521 | Probable transmembrane protein. | Probable chaperone transmembrane protein; Belongs to the heat shock protein 70 family. | 0.957 |
| RSp0522 | htpG | RSp0522 | RSc0990 | Probable transmembrane protein. | Probable chaperone protein htpg (heat shock protein htpg) (high temperatureprotein g); Molecular chaperone. Has ATPase activity. | 0.530 |
| clpB | RSc3436 | RSc1335 | RSc3436 | Probable chaperone clpb protein; 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. | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | 0.640 |
| clpB | dnaJ | RSc1335 | RSc2634 | Probable chaperone clpb protein; 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. | Probable 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 betwee [...] | 0.879 |
| clpB | grpE | RSc1335 | RSc2639 | Probable chaperone clpb protein; 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. | Probable protein grpe (hsp-70 cofactor); 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. Severa [...] | 0.902 |
| clpB | hscC | RSc1335 | RSp0521 | Probable chaperone clpb protein; 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. | Probable chaperone transmembrane protein; Belongs to the heat shock protein 70 family. | 0.872 |
| clpB | htpG | RSc1335 | RSc0990 | Probable chaperone clpb protein; 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. | Probable chaperone protein htpg (heat shock protein htpg) (high temperatureprotein g); Molecular chaperone. Has ATPase activity. | 0.859 |
| clpB | mopA | RSc1335 | RSc0642 | Probable chaperone clpb protein; 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. | Probable 60 kda chaperonin (protein cpn60) (groel protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.803 |
| clpB | mopB | RSc1335 | RSc0641 | Probable chaperone clpb protein; 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. | Probable 10 kda chaperonin (protein cpn10) (groes protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.814 |
| dnaJ | RSc3436 | RSc2634 | RSc3436 | Probable 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 betwee [...] | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | 0.955 |
| dnaJ | RSp0522 | RSc2634 | RSp0522 | Probable 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 betwee [...] | Probable transmembrane protein. | 0.606 |
