node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpB | clpE | lp_1903 | lp_1269 | ATP-dependent Clp protease, ATP-binding subunit 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 [...] | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | 0.686 |
clpB | clpP | lp_1903 | lp_0786 | ATP-dependent Clp protease, ATP-binding subunit 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 [...] | Endopeptidase Clp, proteolytic subunit; 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. | 0.959 |
clpB | dnaK | lp_1903 | lp_2027 | ATP-dependent Clp protease, ATP-binding subunit 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, heat shock protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.977 |
clpB | groEL | lp_1903 | lp_0728 | ATP-dependent Clp protease, ATP-binding subunit 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 [...] | GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.864 |
clpB | groES | lp_1903 | lp_0727 | ATP-dependent Clp protease, ATP-binding subunit 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 [...] | GroES co-chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.872 |
clpB | grpE | lp_1903 | lp_2028 | ATP-dependent Clp protease, ATP-binding subunit 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 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- [...] | 0.925 |
clpB | hsp3 | lp_1903 | lp_3352 | ATP-dependent Clp protease, ATP-binding subunit 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 [...] | Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. | 0.773 |
clpC | clpE | lp_1019 | lp_1269 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | 0.631 |
clpC | clpP | lp_1019 | lp_0786 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, proteolytic subunit; 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. | 0.955 |
clpC | dnaK | lp_1019 | lp_2027 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Chaperone, heat shock protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.970 |
clpC | groEL | lp_1019 | lp_0728 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.790 |
clpC | groES | lp_1019 | lp_0727 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | GroES co-chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.824 |
clpC | grpE | lp_1019 | lp_2028 | ATP-dependent Clp protease, ATP-binding subunit ClpC; 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- [...] | 0.872 |
clpC | hsp3 | lp_1019 | lp_3352 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. | 0.731 |
clpE | clpB | lp_1269 | lp_1903 | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease, ATP-binding subunit 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 [...] | 0.686 |
clpE | clpC | lp_1269 | lp_1019 | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease, ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 0.631 |
clpE | clpL | lp_1269 | lp_3583 | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease, ATP-binding subunit ClpL; Belongs to the ClpA/ClpB family. | 0.471 |
clpE | clpP | lp_1269 | lp_0786 | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, proteolytic subunit; 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. | 0.986 |
clpE | dnaK | lp_1269 | lp_2027 | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | Chaperone, heat shock protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.972 |
clpE | groEL | lp_1269 | lp_0728 | ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family. | GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.869 |