| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| XF_2233 | clpB | XF_2233 | XF_0381 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | ATP-dependent Clp protease subunit; 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. | 0.700 |
| XF_2233 | dnaK | XF_2233 | XF_2340 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | DnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.995 |
| XF_2233 | groL | XF_2233 | XF_0615 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 60kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.748 |
| XF_2233 | groS | XF_2233 | XF_0616 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 10kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.653 |
| XF_2233 | grpE | XF_2233 | XF_2341 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock 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- [...] | 0.911 |
| XF_2233 | hrcA | XF_2233 | XF_2342 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat-inducible transcriptional repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.642 |
| XF_2233 | hslU | XF_2233 | XF_1485 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock protein; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.627 |
| XF_2233 | hslV | XF_2233 | XF_1484 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.458 |
| XF_2233 | htpG | XF_2233 | XF_0978 | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock protein G; Molecular chaperone. Has ATPase activity. | 0.954 |
| clpB | XF_2233 | XF_0381 | XF_2233 | ATP-dependent Clp protease subunit; 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. | DnaJ protein; Similar to SP|Q56237 (percent identity: 41 %/query alignment coverage: 99.3 %/subject alignment coverage: 103.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 0.700 |
| clpB | dnaJ | XF_0381 | XF_2339 | ATP-dependent Clp protease subunit; 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. | DnaJ protein; 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, DnaK and Gr [...] | 0.740 |
| clpB | dnaK | XF_0381 | XF_2340 | ATP-dependent Clp protease subunit; 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. | DnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.953 |
| clpB | groL | XF_0381 | XF_0615 | ATP-dependent Clp protease subunit; 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. | 60kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.511 |
| clpB | groS | XF_0381 | XF_0616 | ATP-dependent Clp protease subunit; 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. | 10kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.752 |
| clpB | grpE | XF_0381 | XF_2341 | ATP-dependent Clp protease subunit; 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. | Heat shock 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- [...] | 0.832 |
| clpB | hrcA | XF_0381 | XF_2342 | ATP-dependent Clp protease subunit; 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. | Heat-inducible transcriptional repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.473 |
| clpB | hslU | XF_0381 | XF_1485 | ATP-dependent Clp protease subunit; 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. | Heat shock protein; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.472 |
| clpB | htpG | XF_0381 | XF_0978 | ATP-dependent Clp protease subunit; 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. | Heat shock protein G; Molecular chaperone. Has ATPase activity. | 0.840 |
| dnaJ | clpB | XF_2339 | XF_0381 | DnaJ protein; 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, DnaK and Gr [...] | ATP-dependent Clp protease subunit; 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. | 0.740 |
| dnaJ | dnaK | XF_2339 | XF_2340 | DnaJ protein; 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, DnaK and Gr [...] | DnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |