| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB83276.1 | clpP | Alide2_0863 | Alide2_1459 | PFAM: Stringent starvation protein B; KEGG: dia:Dtpsy_0756 stringent starvation protein B. | 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. | 0.764 |
| AEB83276.1 | clpX | Alide2_0863 | Alide2_1460 | PFAM: Stringent starvation protein B; KEGG: dia:Dtpsy_0756 stringent starvation protein B. | 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. | 0.837 |
| AEB83276.1 | hfq | Alide2_0863 | Alide2_1416 | PFAM: Stringent starvation protein B; KEGG: dia:Dtpsy_0756 stringent starvation protein B. | RNA chaperone Hfq; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. | 0.465 |
| AEB83845.1 | clpP | Alide2_1446 | Alide2_1459 | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | 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. | 0.778 |
| AEB83845.1 | clpX | Alide2_1446 | Alide2_1460 | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | 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. | 0.811 |
| AEB85324.1 | clpP | Alide2_2977 | Alide2_1459 | PFAM: Bacterial bifunctional deaminase-reductase, C-terminal; KEGG: mxa:MXAN_6138 riboflavin biosynthesis protein RibD domain-containing protein. | 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. | 0.732 |
| AEB85324.1 | clpX | Alide2_2977 | Alide2_1460 | PFAM: Bacterial bifunctional deaminase-reductase, C-terminal; KEGG: mxa:MXAN_6138 riboflavin biosynthesis protein RibD domain-containing protein. | 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. | 0.772 |
| atpD | clpP | Alide2_0384 | Alide2_1459 | 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, 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. | 0.595 |
| atpD | clpX | Alide2_0384 | Alide2_1460 | 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. | 0.837 |
| atpD | ftsH | Alide2_0384 | Alide2_2059 | 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 metalloprotease FtsH; 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. | 0.566 |
| atpD | groL | Alide2_0384 | Alide2_0774 | 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. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.730 |
| atpD | lon | Alide2_0384 | Alide2_1461 | 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. | 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. | 0.493 |
| clpP | AEB83276.1 | Alide2_1459 | Alide2_0863 | 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. | PFAM: Stringent starvation protein B; KEGG: dia:Dtpsy_0756 stringent starvation protein B. | 0.764 |
| clpP | AEB83845.1 | Alide2_1459 | Alide2_1446 | 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. | Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | 0.778 |
| clpP | AEB85324.1 | Alide2_1459 | Alide2_2977 | 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. | PFAM: Bacterial bifunctional deaminase-reductase, C-terminal; KEGG: mxa:MXAN_6138 riboflavin biosynthesis protein RibD domain-containing protein. | 0.732 |
| clpP | atpD | Alide2_1459 | Alide2_0384 | 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 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. | 0.595 |
| clpP | clpX | Alide2_1459 | Alide2_1460 | 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. | 0.998 |
| clpP | ftsH | Alide2_1459 | Alide2_2059 | 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 metalloprotease FtsH; 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. | 0.445 |
| clpP | groL | Alide2_1459 | Alide2_0774 | 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. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.880 |
| clpP | hfq | Alide2_1459 | Alide2_1416 | 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. | RNA chaperone Hfq; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. | 0.594 |
