node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ97022.1 | CAZ97023.1 | ZOBELLIA_2875 | ZOBELLIA_2876 | Conserved hypothetical protein; Protein belonging to the DUF1456 family; Localized in the cytoplasm. | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 0.458 |
CAZ97023.1 | CAZ97022.1 | ZOBELLIA_2876 | ZOBELLIA_2875 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | Conserved hypothetical protein; Protein belonging to the DUF1456 family; Localized in the cytoplasm. | 0.458 |
CAZ97023.1 | CAZ97024.1 | ZOBELLIA_2876 | ZOBELLIA_2877 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | Putative protein. | 0.458 |
CAZ97023.1 | clpB1 | ZOBELLIA_2876 | ZOBELLIA_4745 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 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. | 0.638 |
CAZ97023.1 | clpB2 | ZOBELLIA_2876 | ZOBELLIA_405 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 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. | 0.638 |
CAZ97023.1 | clpC | ZOBELLIA_2876 | ZOBELLIA_469 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 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. | 0.638 |
CAZ97023.1 | dnaK | ZOBELLIA_2876 | ZOBELLIA_4708 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.576 |
CAZ97023.1 | grpE | ZOBELLIA_2876 | ZOBELLIA_2823 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 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 [...] | 0.494 |
CAZ97023.1 | htpG | ZOBELLIA_2876 | ZOBELLIA_607 | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.575 |
CAZ97024.1 | CAZ97023.1 | ZOBELLIA_2877 | ZOBELLIA_2876 | Putative protein. | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 0.458 |
clpB1 | CAZ97023.1 | ZOBELLIA_4745 | ZOBELLIA_2876 | 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. | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 0.638 |
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 | 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 |
clpB2 | CAZ97023.1 | ZOBELLIA_405 | ZOBELLIA_2876 | 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. | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 0.638 |
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 | 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 |
clpC | CAZ97023.1 | ZOBELLIA_469 | ZOBELLIA_2876 | 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. | Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership. | 0.638 |
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 |