node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDG17124.1 | groL | SAMN05216605_101330 | SAMN05216605_11219 | Lipid kinase YegS; Probably phosphorylates lipids; the in vivo substrate is unknown; Belongs to the diacylglycerol/lipid kinase family. YegS lipid kinase subfamily. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.938 |
SDH11206.1 | SDH41196.1 | SAMN05216605_104357 | SAMN05216605_106166 | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | Signal transduction histidine kinase. | 0.977 |
SDH11206.1 | dnaJ | SAMN05216605_104357 | SAMN05216605_114121 | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | Molecular chaperone 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, [...] | 0.991 |
SDH11206.1 | groL | SAMN05216605_104357 | SAMN05216605_11219 | Molecular chaperone HscC; 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. | 0.930 |
SDH11206.1 | groS | SAMN05216605_104357 | SAMN05216605_11218 | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.828 |
SDH11206.1 | grpE | SAMN05216605_104357 | SAMN05216605_114124 | Molecular chaperone HscC; 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 [...] | 0.983 |
SDH11206.1 | htpG | SAMN05216605_104357 | SAMN05216605_107251 | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.961 |
SDH11206.1 | rpoH | SAMN05216605_104357 | SAMN05216605_104241 | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | RNA polymerase, sigma 32 subunit, RpoH; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.732 |
SDH41196.1 | SDH11206.1 | SAMN05216605_106166 | SAMN05216605_104357 | Signal transduction histidine kinase. | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | 0.977 |
SDH41196.1 | SDI52931.1 | SAMN05216605_106166 | SAMN05216605_11491 | Signal transduction histidine kinase. | Response regulator receiver domain-containing protein. | 0.756 |
SDH41196.1 | dnaJ | SAMN05216605_106166 | SAMN05216605_114121 | Signal transduction histidine kinase. | Molecular chaperone 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, [...] | 0.998 |
SDH41196.1 | dnaK | SAMN05216605_106166 | SAMN05216605_114123 | Signal transduction histidine kinase. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.977 |
SDH41196.1 | groL | SAMN05216605_106166 | SAMN05216605_11219 | Signal transduction histidine kinase. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.983 |
SDH41196.1 | groS | SAMN05216605_106166 | SAMN05216605_11218 | Signal transduction histidine kinase. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.891 |
SDH41196.1 | grpE | SAMN05216605_106166 | SAMN05216605_114124 | Signal transduction histidine kinase. | 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 [...] | 0.858 |
SDI52931.1 | SDH41196.1 | SAMN05216605_11491 | SAMN05216605_106166 | Response regulator receiver domain-containing protein. | Signal transduction histidine kinase. | 0.756 |
SDI52931.1 | groL | SAMN05216605_11491 | SAMN05216605_11219 | Response regulator receiver domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.936 |
SDI52931.1 | grpE | SAMN05216605_11491 | SAMN05216605_114124 | Response regulator receiver domain-containing protein. | 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 [...] | 0.402 |
dnaJ | SDH11206.1 | SAMN05216605_114121 | SAMN05216605_104357 | Molecular chaperone 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, [...] | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | 0.991 |
dnaJ | SDH41196.1 | SAMN05216605_114121 | SAMN05216605_106166 | Molecular chaperone 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, [...] | Signal transduction histidine kinase. | 0.998 |