| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| accADCB | dnaK | SO_0840 | SO_1126 | acetyl-CoA carboxylase multifunctional enzyme AccADCB. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.489 |
| accADCB | hslV | SO_0840 | SO_4162 | acetyl-CoA carboxylase multifunctional enzyme AccADCB. | HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.477 |
| accADCB | ibpA | SO_0840 | SO_2277 | acetyl-CoA carboxylase multifunctional enzyme AccADCB. | 16 kDa heat shock protein A IbpA; Belongs to the small heat shock protein (HSP20) family. | 0.700 |
| 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 | 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 | hslU | SO_2626 | SO_4163 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | HlsVU protease ATPase component HslU; 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. | 0.626 |
| clpA | hslV | SO_2626 | SO_4162 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.507 |
| 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 |
| clpA | ibpA | SO_2626 | SO_2277 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 16 kDa heat shock protein A IbpA; Belongs to the small heat shock protein (HSP20) family. | 0.900 |
| 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 | groES | SO_3577 | SO_0703 | 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 [...] | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.910 |
| clpB | grpE | SO_3577 | SO_1524 | 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 [...] | 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 [...] | 0.962 |
| clpB | hslU | SO_3577 | SO_4163 | 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 [...] | HlsVU protease ATPase component HslU; 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. | 0.809 |
| clpB | hslV | SO_3577 | SO_4162 | 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 [...] | HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.692 |
| clpB | htpG | SO_3577 | SO_2016 | 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 [...] | Heat shock chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.923 |
| clpB | ibpA | SO_3577 | SO_2277 | 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 [...] | 16 kDa heat shock protein A IbpA; Belongs to the small heat shock protein (HSP20) family. | 0.964 |
| dnaJ | clpA | SO_1127 | SO_2626 | 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 [...] | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 0.838 |