| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BVIR_2005 | lon2_1 | BVIR_2005 | BVIR_2006 | Hypothetical protein; Belongs to the UPF0434 family. | Lon protease 2. | 0.851 |
| BVIR_2005 | ybbN | BVIR_2005 | BVIR_2007 | Hypothetical protein; Belongs to the UPF0434 family. | Thioredoxin C-1. | 0.820 |
| BVIR_968 | gor | BVIR_968 | BVIR_789 | Ferredoxin--NADP reductase. | Glutathione amide reductase; Maintains high levels of reduced glutathione. | 0.542 |
| BVIR_968 | trxB_1 | BVIR_968 | BVIR_867 | Ferredoxin--NADP reductase. | Thioredoxin reductase. | 0.906 |
| BVIR_968 | ybbN | BVIR_968 | BVIR_2007 | Ferredoxin--NADP reductase. | Thioredoxin C-1. | 0.797 |
| gor | BVIR_968 | BVIR_789 | BVIR_968 | Glutathione amide reductase; Maintains high levels of reduced glutathione. | Ferredoxin--NADP reductase. | 0.542 |
| gor | trxB_1 | BVIR_789 | BVIR_867 | Glutathione amide reductase; Maintains high levels of reduced glutathione. | Thioredoxin reductase. | 0.542 |
| gor | ybbN | BVIR_789 | BVIR_2007 | Glutathione amide reductase; Maintains high levels of reduced glutathione. | Thioredoxin C-1. | 0.945 |
| groL3 | groL_1 | BVIR_1299 | BVIR_2720 | 60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.900 |
| groL3 | grpE | BVIR_1299 | BVIR_2941 | 60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.957 |
| groL3 | hslU | BVIR_1299 | BVIR_3277 | 60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent protease 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. | 0.766 |
| groL3 | hslV | BVIR_1299 | BVIR_3276 | 60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.716 |
| groL3 | ybbN | BVIR_1299 | BVIR_2007 | 60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin C-1. | 0.793 |
| groL_1 | groL3 | BVIR_2720 | BVIR_1299 | 60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.900 |
| groL_1 | grpE | BVIR_2720 | BVIR_2941 | 60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.957 |
| groL_1 | hslU | BVIR_2720 | BVIR_3277 | 60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent protease 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. | 0.766 |
| groL_1 | hslV | BVIR_2720 | BVIR_3276 | 60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.716 |
| groL_1 | ybbN | BVIR_2720 | BVIR_2007 | 60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin C-1. | 0.793 |
| grpE | groL3 | BVIR_2941 | BVIR_1299 | 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 [...] | 60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.957 |
| grpE | groL_1 | BVIR_2941 | BVIR_2720 | 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 [...] | 60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.957 |