node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABB56292.1 | ABB56655.1 | Synpcc7942_0260 | Synpcc7942_0623 | ATPase; Belongs to the ClpA/ClpB family. | Thioredoxin reductase. | 0.534 |
ABB56292.1 | clpP1 | Synpcc7942_0260 | Synpcc7942_1554 | ATPase; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.780 |
ABB56292.1 | clpS | Synpcc7942_0260 | Synpcc7942_0690 | ATPase; Belongs to the ClpA/ClpB family. | Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.657 |
ABB56292.1 | clpX | Synpcc7942_0260 | Synpcc7942_2526 | ATPase; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.446 |
ABB56292.1 | dnaK3 | Synpcc7942_0260 | Synpcc7942_2580 | ATPase; Belongs to the ClpA/ClpB family. | Heat shock protein Hsp70; Acts as a chaperone. | 0.739 |
ABB56292.1 | hrcA | Synpcc7942_0260 | Synpcc7942_0616 | ATPase; Belongs to the ClpA/ClpB family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.577 |
ABB56655.1 | ABB56292.1 | Synpcc7942_0623 | Synpcc7942_0260 | Thioredoxin reductase. | ATPase; Belongs to the ClpA/ClpB family. | 0.534 |
ABB56655.1 | clpB1 | Synpcc7942_0623 | Synpcc7942_1089 | Thioredoxin reductase. | ATPase; 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). Necessary for thermotolerance. | 0.534 |
ABB56655.1 | clpB2 | Synpcc7942_0623 | Synpcc7942_0637 | Thioredoxin reductase. | ATPase; 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). | 0.534 |
ABB56655.1 | clpP1 | Synpcc7942_0623 | Synpcc7942_1554 | Thioredoxin reductase. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.568 |
ABB56655.1 | clpX | Synpcc7942_0623 | Synpcc7942_2526 | Thioredoxin reductase. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.545 |
ABB56655.1 | dnaK3 | Synpcc7942_0623 | Synpcc7942_2580 | Thioredoxin reductase. | Heat shock protein Hsp70; Acts as a chaperone. | 0.480 |
ABB56655.1 | hrcA | Synpcc7942_0623 | Synpcc7942_0616 | Thioredoxin reductase. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.419 |
clpB1 | ABB56655.1 | Synpcc7942_1089 | Synpcc7942_0623 | ATPase; 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). Necessary for thermotolerance. | Thioredoxin reductase. | 0.534 |
clpB1 | clpP1 | Synpcc7942_1089 | Synpcc7942_1554 | ATPase; 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). Necessary for thermotolerance. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.793 |
clpB1 | clpS | Synpcc7942_1089 | Synpcc7942_0690 | ATPase; 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). Necessary for thermotolerance. | Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.618 |
clpB1 | clpX | Synpcc7942_1089 | Synpcc7942_2526 | ATPase; 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). Necessary for thermotolerance. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.579 |
clpB1 | dnaK3 | Synpcc7942_1089 | Synpcc7942_2580 | ATPase; 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). Necessary for thermotolerance. | Heat shock protein Hsp70; Acts as a chaperone. | 0.861 |
clpB1 | hrcA | Synpcc7942_1089 | Synpcc7942_0616 | ATPase; 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). Necessary for thermotolerance. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.726 |
clpB2 | ABB56655.1 | Synpcc7942_0637 | Synpcc7942_0623 | ATPase; 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). | Thioredoxin reductase. | 0.534 |