| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpB1 | clpP2 | ZOBELLIA_4745 | ZOBELLIA_718 | Chaperone 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; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, peptidase subunit, family S14; 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 | clpX | ZOBELLIA_4745 | ZOBELLIA_2448 | Chaperone 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; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.447 |
| clpB1 | dnaK | ZOBELLIA_4745 | ZOBELLIA_4708 | Chaperone 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; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.958 |
| clpB1 | groL | ZOBELLIA_4745 | ZOBELLIA_1162 | Chaperone 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; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.602 |
| clpB1 | groS | ZOBELLIA_4745 | ZOBELLIA_1161 | Chaperone 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; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.632 |
| clpB1 | grpE | ZOBELLIA_4745 | ZOBELLIA_2823 | Chaperone 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; Belongs to the ClpA/ClpB family. | Co-chaperone HSP-70 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 [...] | 0.765 |
| clpB2 | clpP2 | ZOBELLIA_405 | ZOBELLIA_718 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, peptidase subunit, family S14; 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. | 0.784 |
| clpB2 | clpX | ZOBELLIA_405 | ZOBELLIA_2448 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.447 |
| clpB2 | dnaK | ZOBELLIA_405 | ZOBELLIA_4708 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.958 |
| clpB2 | groL | ZOBELLIA_405 | ZOBELLIA_1162 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.602 |
| clpB2 | groS | ZOBELLIA_405 | ZOBELLIA_1161 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.632 |
| clpB2 | grpE | ZOBELLIA_405 | ZOBELLIA_2823 | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Co-chaperone HSP-70 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 [...] | 0.765 |
| clpC | clpP2 | ZOBELLIA_469 | ZOBELLIA_718 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Endopeptidase Clp, peptidase subunit, family S14; 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. | 0.819 |
| clpC | dnaK | ZOBELLIA_469 | ZOBELLIA_4708 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.949 |
| clpC | groL | ZOBELLIA_469 | ZOBELLIA_1162 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.648 |
| clpC | groS | ZOBELLIA_469 | ZOBELLIA_1161 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.624 |
| clpC | grpE | ZOBELLIA_469 | ZOBELLIA_2823 | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | Co-chaperone HSP-70 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 [...] | 0.785 |
| clpP2 | clpB1 | ZOBELLIA_718 | ZOBELLIA_4745 | Endopeptidase Clp, peptidase subunit, family S14; 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. | Chaperone 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; Belongs to the ClpA/ClpB family. | 0.793 |
| clpP2 | clpB2 | ZOBELLIA_718 | ZOBELLIA_405 | Endopeptidase Clp, peptidase subunit, family S14; 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. | ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.784 |
| clpP2 | clpC | ZOBELLIA_718 | ZOBELLIA_469 | Endopeptidase Clp, peptidase subunit, family S14; 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. | ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. | 0.819 |
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