node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EMR02161.1 | clpB | ADICEAN_02723 | ADICEAN_03237 | Heat shock protein 90. | Heat shock protein F84.1; 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. | 0.683 |
EMR02161.1 | clpC | ADICEAN_02723 | ADICEAN_00832 | Heat shock protein 90. | Negative regulator of genetic competence ClpC/MecB; Belongs to the ClpA/ClpB family. | 0.689 |
EMR02161.1 | clpY | ADICEAN_02723 | ADICEAN_02869 | Heat shock protein 90. | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.823 |
EMR02161.1 | dnaK | ADICEAN_02723 | ADICEAN_02620 | Heat shock protein 90. | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |
EMR02161.1 | groL | ADICEAN_02723 | ADICEAN_02421 | Heat shock protein 90. | Hypothetical protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.891 |
EMR02161.1 | grpE | ADICEAN_02723 | ADICEAN_03112 | Heat shock protein 90. | HSP-70 cofactor; 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-dependen [...] | 0.801 |
EMR02161.1 | hslV | ADICEAN_02723 | ADICEAN_02409 | Heat shock protein 90. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.828 |
EMR02161.1 | lon2 | ADICEAN_02723 | ADICEAN_02867 | Heat shock protein 90. | Lon protease 2; 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. | 0.786 |
clpB | EMR02161.1 | ADICEAN_03237 | ADICEAN_02723 | Heat shock protein F84.1; 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 90. | 0.683 |
clpB | clpY | ADICEAN_03237 | ADICEAN_02869 | Heat shock protein F84.1; 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. | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.591 |
clpB | dnaK | ADICEAN_03237 | ADICEAN_02620 | Heat shock protein F84.1; 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 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
clpB | groL | ADICEAN_03237 | ADICEAN_02421 | Heat shock protein F84.1; 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. | Hypothetical protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.667 |
clpB | grpE | ADICEAN_03237 | ADICEAN_03112 | Heat shock protein F84.1; 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. | HSP-70 cofactor; 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-dependen [...] | 0.866 |
clpB | hslV | ADICEAN_03237 | ADICEAN_02409 | Heat shock protein F84.1; 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. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.522 |
clpB | htpG | ADICEAN_03237 | ADICEAN_02726 | Heat shock protein F84.1; 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. | High temperature protein G; Molecular chaperone. Has ATPase activity. | 0.683 |
clpB | lon2 | ADICEAN_03237 | ADICEAN_02867 | Heat shock protein F84.1; 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. | Lon protease 2; 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. | 0.777 |
clpC | EMR02161.1 | ADICEAN_00832 | ADICEAN_02723 | Negative regulator of genetic competence ClpC/MecB; Belongs to the ClpA/ClpB family. | Heat shock protein 90. | 0.689 |
clpC | clpY | ADICEAN_00832 | ADICEAN_02869 | Negative regulator of genetic competence ClpC/MecB; Belongs to the ClpA/ClpB family. | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.591 |
clpC | dnaK | ADICEAN_00832 | ADICEAN_02620 | Negative regulator of genetic competence ClpC/MecB; Belongs to the ClpA/ClpB family. | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
clpC | groL | ADICEAN_00832 | ADICEAN_02421 | Negative regulator of genetic competence ClpC/MecB; Belongs to the ClpA/ClpB family. | Hypothetical protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.647 |