| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEH22235.1 | dnaK | TOPB45_0119 | TOPB45_1533 | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.525 |
| AEH22235.1 | groL | TOPB45_0119 | TOPB45_1393 | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.719 |
| AEH22235.1 | groS | TOPB45_0119 | TOPB45_1394 | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.539 |
| AEH22235.1 | grpE | TOPB45_0119 | TOPB45_1534 | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | Protein 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-dependent i [...] | 0.609 |
| AEH22235.1 | hslU | TOPB45_0119 | TOPB45_0202 | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | ATP-dependent hsl protease ATP-binding 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. | 0.611 |
| AEH22235.1 | hslV | TOPB45_0119 | TOPB45_0201 | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.608 |
| AEH23103.1 | dnaK | TOPB45_1009 | TOPB45_1533 | PFAM: Heat shock protein Hsp20; KEGG: ddf:DEFDS_1576 heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.729 |
| AEH23103.1 | grpE | TOPB45_1009 | TOPB45_1534 | PFAM: Heat shock protein Hsp20; KEGG: ddf:DEFDS_1576 heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family. | Protein 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-dependent i [...] | 0.697 |
| AEH23103.1 | hslU | TOPB45_1009 | TOPB45_0202 | PFAM: Heat shock protein Hsp20; KEGG: ddf:DEFDS_1576 heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family. | ATP-dependent hsl protease ATP-binding 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. | 0.483 |
| AEH23103.1 | hslV | TOPB45_1009 | TOPB45_0201 | PFAM: Heat shock protein Hsp20; KEGG: ddf:DEFDS_1576 heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.594 |
| dnaK | AEH22235.1 | TOPB45_1533 | TOPB45_0119 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | 0.525 |
| dnaK | AEH23103.1 | TOPB45_1533 | TOPB45_1009 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | PFAM: Heat shock protein Hsp20; KEGG: ddf:DEFDS_1576 heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family. | 0.729 |
| dnaK | groL | TOPB45_1533 | TOPB45_1393 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.980 |
| dnaK | groS | TOPB45_1533 | TOPB45_1394 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.954 |
| dnaK | grpE | TOPB45_1533 | TOPB45_1534 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Protein 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-dependent i [...] | 0.999 |
| dnaK | hslU | TOPB45_1533 | TOPB45_0202 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent hsl protease ATP-binding 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. | 0.683 |
| dnaK | hslV | TOPB45_1533 | TOPB45_0201 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.666 |
| dnaK | lon | TOPB45_1533 | TOPB45_0787 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Anti-sigma H sporulation factor, LonB; 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. | 0.590 |
| dnaK | lon-2 | TOPB45_1533 | TOPB45_0980 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Anti-sigma H sporulation factor, LonB; 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. | 0.590 |
| groL | AEH22235.1 | TOPB45_1393 | TOPB45_0119 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family. | 0.719 |