| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABD30617.1 | clpC | SAOUHSC_01536 | SAOUHSC_00505 | Scaffolding protease; Belongs to the peptidase S14 family. | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | 0.741 |
| ABD30617.1 | clpP | SAOUHSC_01536 | SAOUHSC_00790 | Scaffolding protease; Belongs to the peptidase S14 family. | ATP-dependent Clp protease, 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. | 0.631 |
| ABD30617.1 | clpX | SAOUHSC_01536 | SAOUHSC_01778 | Scaffolding protease; 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. | 0.954 |
| ABD30617.1 | hslV | SAOUHSC_01536 | SAOUHSC_01225 | Scaffolding protease; Belongs to the peptidase S14 family. | Heat shock protein HslV, putative; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.447 |
| atpD | clpX | SAOUHSC_02341 | SAOUHSC_01778 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains 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. | 0.739 |
| atpD | ftsZ | SAOUHSC_02341 | SAOUHSC_01150 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.453 |
| atpD | tig | SAOUHSC_02341 | SAOUHSC_01779 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.510 |
| clpC | ABD30617.1 | SAOUHSC_00505 | SAOUHSC_01536 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Scaffolding protease; Belongs to the peptidase S14 family. | 0.741 |
| clpC | clpP | SAOUHSC_00505 | SAOUHSC_00790 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | ATP-dependent Clp protease, 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. | 0.995 |
| clpC | clpX | SAOUHSC_00505 | SAOUHSC_01778 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | 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. | 0.866 |
| clpC | ftsH | SAOUHSC_00505 | SAOUHSC_00486 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Conserved hypothetical protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.425 |
| clpC | hslU | SAOUHSC_00505 | SAOUHSC_01226 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Heat shock protein HslVU, 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. | 0.624 |
| clpC | hslV | SAOUHSC_00505 | SAOUHSC_01225 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Heat shock protein HslV, putative; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.707 |
| clpP | ABD30617.1 | SAOUHSC_00790 | SAOUHSC_01536 | ATP-dependent Clp protease, 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. | Scaffolding protease; Belongs to the peptidase S14 family. | 0.631 |
| clpP | clpC | SAOUHSC_00790 | SAOUHSC_00505 | ATP-dependent Clp protease, 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. | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | 0.995 |
| clpP | clpX | SAOUHSC_00790 | SAOUHSC_01778 | ATP-dependent Clp protease, 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. | 0.999 |
| clpP | ftsH | SAOUHSC_00790 | SAOUHSC_00486 | ATP-dependent Clp protease, 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. | Conserved hypothetical protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.630 |
| clpP | ftsZ | SAOUHSC_00790 | SAOUHSC_01150 | ATP-dependent Clp protease, 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. | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity. | 0.718 |
| clpP | hslU | SAOUHSC_00790 | SAOUHSC_01226 | ATP-dependent Clp protease, 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. | Heat shock protein HslVU, 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. | 0.791 |
| clpP | hslV | SAOUHSC_00790 | SAOUHSC_01225 | ATP-dependent Clp protease, 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. | Heat shock protein HslV, putative; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.708 |