node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
IW20_01640 | atpD | IW20_01640 | IW20_14410 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.621 |
IW20_01640 | clpP | IW20_01640 | IW20_01645 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Clp protease; 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. | 0.704 |
IW20_01640 | clpX | IW20_01640 | IW20_01650 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase AAA; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.580 |
IW20_01640 | ftsH | IW20_01640 | IW20_13190 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M41; 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. | 0.536 |
IW20_01640 | groS | IW20_01640 | IW20_14210 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.503 |
IW20_01640 | metK | IW20_01640 | IW20_06200 | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | 0.537 |
atpD | IW20_01640 | IW20_14410 | IW20_01640 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.621 |
atpD | clpX | IW20_14410 | IW20_01650 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | ATPase AAA; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.725 |
atpD | ftsH | IW20_14410 | IW20_13190 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Peptidase M41; 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. | 0.490 |
atpD | groEL | IW20_14410 | IW20_14220 | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.598 |
clpP | IW20_01640 | IW20_01645 | IW20_01640 | Clp protease; 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. | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.704 |
clpP | clpX | IW20_01645 | IW20_01650 | Clp protease; 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. | ATPase AAA; 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 | groEL | IW20_01645 | IW20_14220 | Clp protease; 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. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.927 |
clpP | groS | IW20_01645 | IW20_14210 | Clp protease; 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. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.925 |
clpP | lon | IW20_01645 | IW20_21910 | Clp protease; 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. | Lon protease; 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. | 0.778 |
clpX | IW20_01640 | IW20_01650 | IW20_01640 | ATPase AAA; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Peptidylprolyl isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.580 |
clpX | atpD | IW20_01650 | IW20_14410 | ATPase AAA; 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 synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.725 |
clpX | clpP | IW20_01650 | IW20_01645 | ATPase AAA; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Clp protease; 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. | 0.999 |
clpX | ftsH | IW20_01650 | IW20_13190 | ATPase AAA; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Peptidase M41; 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. | 0.838 |
clpX | ftsZ | IW20_01650 | IW20_22610 | ATPase AAA; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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. | 0.596 |