| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | 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 |
| clpB1 | htpG | ZOBELLIA_4745 | ZOBELLIA_607 | 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. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.680 |
| clpB1 | lonA | ZOBELLIA_4745 | ZOBELLIA_509 | 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 La, family S16; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.704 |
| 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 | 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 |
| clpB2 | htpG | ZOBELLIA_405 | ZOBELLIA_607 | 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. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.680 |
| clpB2 | lonA | ZOBELLIA_405 | ZOBELLIA_509 | 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 La, family S16; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.704 |
| clpX | clpB1 | ZOBELLIA_2448 | ZOBELLIA_4745 | 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. | 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. | 0.447 |
| clpX | clpB2 | ZOBELLIA_2448 | ZOBELLIA_405 | 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. | 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. | 0.447 |
| clpX | ftsH | ZOBELLIA_2448 | ZOBELLIA_693 | 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. | Cell division protein FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.757 |
| clpX | groL | ZOBELLIA_2448 | ZOBELLIA_1162 | 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. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.699 |
| clpX | grpE | ZOBELLIA_2448 | ZOBELLIA_2823 | 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. | 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 [...] | 0.440 |
| clpX | lonA | ZOBELLIA_2448 | ZOBELLIA_509 | 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. | Endopeptidase La, family S16; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.816 |
| clpX | rcaA | ZOBELLIA_2448 | ZOBELLIA_3859 | 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. | Respiratory chain complexes assembly ATP-dependent metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.757 |
| cmk | lonA | ZOBELLIA_508 | ZOBELLIA_509 | Cytidylate kinase is involved in pyrimidine nucleotide metabolism. It catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP. Localized in the cytoplasm; High confidence in function and specificity. | Endopeptidase La, family S16; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.796 |