| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APC13513.1 | groL | RB151_038650 | RB151_038630 | Phage T7 F exclusion suppressor FxsA. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.457 |
| APC13513.1 | groS | RB151_038650 | RB151_038640 | Phage T7 F exclusion suppressor FxsA. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.572 |
| APC13513.1 | hslU | RB151_038650 | RB151_043290 | Phage T7 F exclusion suppressor FxsA. | 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. | 0.480 |
| APC13513.1 | hslV | RB151_038650 | RB151_043280 | Phage T7 F exclusion suppressor FxsA. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.654 |
| APC13513.1 | ibpA | RB151_038650 | RB151_025150 | Phage T7 F exclusion suppressor FxsA. | Small heat shock protein IbpA. | 0.563 |
| APC13513.1 | nfdA | RB151_038650 | RB151_041840 | Phage T7 F exclusion suppressor FxsA. | N-substituted formamide deformylase precursor. | 0.647 |
| APC13513.1 | trxA_2 | RB151_038650 | RB151_033560 | Phage T7 F exclusion suppressor FxsA. | Thioredoxin. | 0.654 |
| groL | APC13513.1 | RB151_038630 | RB151_038650 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Phage T7 F exclusion suppressor FxsA. | 0.457 |
| groL | groS | RB151_038630 | RB151_038640 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
| groL | hslU | RB151_038630 | RB151_043290 | 60 kDa chaperonin; 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. | 0.885 |
| groL | hslV | RB151_038630 | RB151_043280 | 60 kDa chaperonin; 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. | 0.797 |
| groL | trxA_2 | RB151_038630 | RB151_033560 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin. | 0.531 |
| groS | APC13513.1 | RB151_038640 | RB151_038650 | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Phage T7 F exclusion suppressor FxsA. | 0.572 |
| groS | groL | RB151_038640 | RB151_038630 | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| groS | hslU | RB151_038640 | RB151_043290 | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 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. | 0.854 |
| groS | hslV | RB151_038640 | RB151_043280 | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.801 |
| groS | ibpA | RB151_038640 | RB151_025150 | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Small heat shock protein IbpA. | 0.434 |
| groS | trxA_2 | RB151_038640 | RB151_033560 | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Thioredoxin. | 0.506 |
| hslU | APC13513.1 | RB151_043290 | RB151_038650 | 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. | Phage T7 F exclusion suppressor FxsA. | 0.480 |
| hslU | groL | RB151_043290 | RB151_038630 | 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. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.885 |