| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABC1297 | trxA | ABC1297 | ABC2668 | Thioredoxin reductase. | Thioredoxin; Belongs to the thioredoxin family. | 0.732 |
| arsC | trxA | ABC0837 | ABC2668 | Arsenate reductase; Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. | Thioredoxin; Belongs to the thioredoxin family. | 0.794 |
| clpC | clpP | ABC0121 | ABC3026 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | 0.919 |
| clpC | clpQ | ABC0121 | ABC2275 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.703 |
| clpC | clpX | ABC0121 | ABC2636 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB 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. | 0.450 |
| clpC | clpY | ABC0121 | ABC2274 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ) ATPase subunit; 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. | 0.752 |
| clpC | trxA | ABC0121 | ABC2668 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Thioredoxin; Belongs to the thioredoxin family. | 0.598 |
| clpP | clpC | ABC3026 | ABC0121 | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 0.919 |
| clpP | clpQ | ABC3026 | ABC2275 | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.719 |
| clpP | clpX | ABC3026 | ABC2636 | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); 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. | 0.991 |
| clpP | clpY | ABC3026 | ABC2274 | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | ATP-dependent protease HslVU (ClpYQ) ATPase subunit; 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. | 0.616 |
| clpP | nfrA1 | ABC3026 | ABC1491 | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Nitro/flavin reductase; Belongs to the flavin oxidoreductase frp family. | 0.479 |
| clpP | trxA | ABC3026 | ABC2668 | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Thioredoxin; Belongs to the thioredoxin family. | 0.666 |
| clpQ | clpC | ABC2275 | ABC0121 | ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 0.703 |
| clpQ | clpP | ABC2275 | ABC3026 | ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | 0.719 |
| clpQ | clpX | ABC2275 | ABC2636 | ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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. | 0.688 |
| clpQ | clpY | ABC2275 | ABC2274 | ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent protease HslVU (ClpYQ) ATPase subunit; 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. | 0.999 |
| clpQ | trxA | ABC2275 | ABC2668 | ATP-dependent protease HslVU (ClpYQ) peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Thioredoxin; Belongs to the thioredoxin family. | 0.675 |
| clpX | clpC | ABC2636 | ABC0121 | 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. | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 0.450 |
| clpX | clpP | ABC2636 | ABC3026 | 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. | ATP-dependent Clp protease proteolytic subunit; 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. ClpXP2 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | 0.991 |