| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADO49547.1 | ADO50250.1 | Entcl_3302 | Entcl_4013 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | KEGG: cko:CKO_03695 FxsA; manually curated; PFAM: FxsA cytoplasmic membrane protein. | 0.741 |
| ADO49547.1 | clpB | Entcl_3302 | Entcl_1158 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | ATP-dependent 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. | 0.579 |
| ADO49547.1 | dnaJ | Entcl_3302 | Entcl_3704 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, D [...] | 0.751 |
| ADO49547.1 | groL | Entcl_3302 | Entcl_4010 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.901 |
| ADO49547.1 | groS | Entcl_3302 | Entcl_4011 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.580 |
| ADO49547.1 | grpE | Entcl_3302 | Entcl_1109 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | GrpE 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 ATP-dependent i [...] | 0.914 |
| ADO49547.1 | hslU | Entcl_3302 | Entcl_4343 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.912 |
| ADO49547.1 | hslV | Entcl_3302 | Entcl_4342 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.922 |
| ADO49547.1 | htpG | Entcl_3302 | Entcl_3317 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | Heat shock protein Hsp90-like protein; Molecular chaperone. Has ATPase activity. | 0.767 |
| ADO49547.1 | lon | Entcl_3302 | Entcl_3366 | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | ATP-dependent protease La; 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. | 0.596 |
| ADO50250.1 | ADO49547.1 | Entcl_4013 | Entcl_3302 | KEGG: cko:CKO_03695 FxsA; manually curated; PFAM: FxsA cytoplasmic membrane protein. | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | 0.741 |
| ADO50250.1 | grpE | Entcl_4013 | Entcl_1109 | KEGG: cko:CKO_03695 FxsA; manually curated; PFAM: FxsA cytoplasmic membrane protein. | GrpE 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 ATP-dependent i [...] | 0.415 |
| ADO50250.1 | hslU | Entcl_4013 | Entcl_4343 | KEGG: cko:CKO_03695 FxsA; manually curated; PFAM: FxsA cytoplasmic membrane protein. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.539 |
| ADO50250.1 | hslV | Entcl_4013 | Entcl_4342 | KEGG: cko:CKO_03695 FxsA; manually curated; PFAM: FxsA cytoplasmic membrane protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.752 |
| clpB | ADO49547.1 | Entcl_1158 | Entcl_3302 | ATP-dependent 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. | PFAM: Thioredoxin domain-containing protein; KEGG: enc:ECL_01259 putative thioredoxin-like protein. | 0.579 |
| clpB | dnaJ | Entcl_1158 | Entcl_3704 | ATP-dependent 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 DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, D [...] | 0.875 |
| clpB | groL | Entcl_1158 | Entcl_4010 | ATP-dependent 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. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.845 |
| clpB | groS | Entcl_1158 | Entcl_4011 | ATP-dependent 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. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.720 |
| clpB | grpE | Entcl_1158 | Entcl_1109 | ATP-dependent 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. | GrpE 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 ATP-dependent i [...] | 0.829 |
| clpB | hslU | Entcl_1158 | Entcl_4343 | ATP-dependent 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 HslVU, ATPase subunit HslU; 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. | 0.809 |