| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EDR45946.1 | EDR48410.1 | DORFOR_02548 | DORFOR_00317 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | 0.733 |
| EDR45946.1 | clpB | DORFOR_02548 | DORFOR_02181 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | ATP-dependent chaperone protein 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. | 0.733 |
| EDR45946.1 | clpP | DORFOR_02548 | DORFOR_00690 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | 0.461 |
| EDR45946.1 | groL | DORFOR_02548 | DORFOR_00901 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.957 |
| EDR45946.1 | grpE | DORFOR_02548 | DORFOR_00807 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Co-chaperone GrpE; 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-depend [...] | 0.877 |
| EDR45946.1 | lon | DORFOR_02548 | DORFOR_00688 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Endopeptidase 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. | 0.575 |
| EDR48410.1 | EDR45946.1 | DORFOR_00317 | DORFOR_02548 | ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.733 |
| EDR48410.1 | clpP | DORFOR_00317 | DORFOR_00690 | ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | 0.965 |
| EDR48410.1 | groL | DORFOR_00317 | DORFOR_00901 | ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.705 |
| EDR48410.1 | grpE | DORFOR_00317 | DORFOR_00807 | ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Co-chaperone GrpE; 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-depend [...] | 0.848 |
| EDR48410.1 | lon | DORFOR_00317 | DORFOR_00688 | ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Endopeptidase 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. | 0.602 |
| clpB | EDR45946.1 | DORFOR_02181 | DORFOR_02548 | ATP-dependent chaperone protein 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. | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.733 |
| clpB | clpP | DORFOR_02181 | DORFOR_00690 | ATP-dependent chaperone protein 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. | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | 0.964 |
| clpB | groL | DORFOR_02181 | DORFOR_00901 | ATP-dependent chaperone protein 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 GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.705 |
| clpB | grpE | DORFOR_02181 | DORFOR_00807 | ATP-dependent chaperone protein 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 GrpE; 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-depend [...] | 0.848 |
| clpB | lon | DORFOR_02181 | DORFOR_00688 | ATP-dependent chaperone protein 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; 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. | 0.602 |
| clpP | EDR45946.1 | DORFOR_00690 | DORFOR_02548 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.461 |
| clpP | EDR48410.1 | DORFOR_00690 | DORFOR_00317 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | ATPase family associated with various cellular activities (AAA); KEGG: sab:SAB0475 5.8e-223 clpC; endopeptidase K03696; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | 0.965 |
| clpP | clpB | DORFOR_00690 | DORFOR_02181 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | ATP-dependent chaperone protein 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. | 0.964 |
| clpP | clpX-2 | DORFOR_00690 | DORFOR_00689 | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; 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. | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.996 |