| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpA | dnaJ | Atu1364 | Atu0121 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Molecular chaperone, DnaJ family; 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 betwe [...] | 0.789 |
| clpA | dnaK | Atu1364 | Atu0122 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.919 |
| clpA | grpE | Atu1364 | Atu0329 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | GRPE protein; 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-dependent i [...] | 0.750 |
| clpA | hslU | Atu1364 | Atu0045 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Heat shock chaperone; 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. | 0.600 |
| clpA | hslV | Atu1364 | Atu0044 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.482 |
| clpA | hspL | Atu1364 | Atu3887 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. | 0.712 |
| clpB | dnaJ | Atu4177 | Atu0121 | ATP-dependent Clp protease, ATP-binding 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 [...] | Molecular chaperone, DnaJ family; 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 betwe [...] | 0.751 |
| clpB | dnaK | Atu4177 | Atu0122 | ATP-dependent Clp protease, ATP-binding 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 [...] | DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.934 |
| clpB | grpE | Atu4177 | Atu0329 | ATP-dependent Clp protease, ATP-binding 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 [...] | GRPE protein; 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-dependent i [...] | 0.816 |
| clpB | hslU | Atu4177 | Atu0045 | ATP-dependent Clp protease, ATP-binding 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 [...] | Heat shock chaperone; 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. | 0.657 |
| clpB | hslV | Atu4177 | Atu0044 | ATP-dependent Clp protease, ATP-binding 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 [...] | Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.566 |
| clpB | hspL | Atu4177 | Atu3887 | ATP-dependent Clp protease, ATP-binding 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 [...] | Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. | 0.729 |
| clpB-2 | dnaJ | Atu4344 | Atu0121 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Molecular chaperone, DnaJ family; 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 betwe [...] | 0.751 |
| clpB-2 | dnaK | Atu4344 | Atu0122 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.933 |
| clpB-2 | grpE | Atu4344 | Atu0329 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | GRPE protein; 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-dependent i [...] | 0.816 |
| clpB-2 | hslU | Atu4344 | Atu0045 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Heat shock chaperone; 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. | 0.657 |
| clpB-2 | hslV | Atu4344 | Atu0044 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.566 |
| clpB-2 | hspL | Atu4344 | Atu3887 | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. | 0.729 |
| dnaJ | clpA | Atu0121 | Atu1364 | Molecular chaperone, DnaJ family; 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 betwe [...] | ATP-dependent Clp protease, ATP-binding subunit; Belongs to the ClpA/ClpB family. | 0.789 |
| dnaJ | clpB | Atu0121 | Atu4177 | Molecular chaperone, DnaJ family; 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 betwe [...] | ATP-dependent Clp protease, ATP-binding 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 [...] | 0.751 |
