| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FtsH | atpD | azo1387 | azo0159 | Probable cell division protein 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. | ATP synthase beta chain; 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. | 0.507 |
| FtsH | clpX | azo1387 | azo2070 | Probable cell division protein 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. | ATP-dependent Clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.880 |
| FtsH | hfq | azo1387 | azo0932 | Probable cell division protein 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. | RNA-binding regulatory protein; 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. | 0.581 |
| FtsH | hslU | azo1387 | azo0424 | Probable cell division protein 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. | ATP-dependent Hsl protease ATP-binding 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. | 0.479 |
| FtsH | hslV | azo1387 | azo0423 | Probable cell division protein 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. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.565 |
| FtsH | lon | azo1387 | azo2069 | Probable cell division protein 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. | ATP-dependent protease La; 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. | 0.726 |
| FtsH | tig | azo1387 | azo2072 | Probable cell division protein 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. | 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. | 0.583 |
| atpD | FtsH | azo0159 | azo1387 | ATP synthase beta chain; 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. | Probable cell division protein 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. | 0.507 |
| atpD | azo1870 | azo0159 | azo1870 | ATP synthase beta chain; 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. | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | 0.423 |
| atpD | clpP | azo0159 | azo2071 | ATP synthase beta chain; 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. | Endopeptidase Clp; 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. | 0.423 |
| atpD | clpX | azo0159 | azo2070 | ATP synthase beta chain; 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; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.841 |
| atpD | lon | azo0159 | azo2069 | ATP synthase beta chain; 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 protease La; 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. | 0.458 |
| atpD | tig | azo0159 | azo2072 | ATP synthase beta chain; 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. | 0.631 |
| azo1870 | atpD | azo1870 | azo0159 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | ATP synthase beta chain; 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. | 0.423 |
| azo1870 | clpX | azo1870 | azo2070 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | ATP-dependent Clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.990 |
| azo1870 | hfq | azo1870 | azo0932 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | RNA-binding regulatory protein; 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. | 0.426 |
| azo1870 | hslU | azo1870 | azo0424 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | ATP-dependent Hsl protease ATP-binding 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. | 0.756 |
| azo1870 | hslV | azo1870 | azo0423 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.811 |
| azo1870 | lon | azo1870 | azo2069 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | ATP-dependent protease La; 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. | 0.472 |
| azo1870 | sspB | azo1870 | azo0964 | Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...] | Putative stringent starvation protein B. Homology to sspB of E. coli of 38% (sprot|SSPB_ECOLI) Seems to act in concert with sspA in the regulation of several proteins during exponential and stationary-phase growth. The exact function of sspB is not yet known. Pfam: Stringent starvation protein B no signal peptide no TMHs. | 0.876 |
