| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo0358 | azo1870 | azo0358 | azo1870 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 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 [...] | 0.729 |
| azo0358 | clpP | azo0358 | azo2071 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 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. | 0.729 |
| azo0358 | clpX | azo0358 | azo2070 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 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. | 0.543 |
| azo0358 | dnaJ1 | azo0358 | azo1062 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.961 |
| azo0358 | dnaJ2 | azo0358 | azo1266 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership. | 0.961 |
| azo0358 | grpE | azo0358 | azo1064 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | 0.758 |
| azo0358 | hslU | azo0358 | azo0424 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 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. | 0.828 |
| azo0358 | hslV | azo0358 | azo0423 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.836 |
| azo0358 | lon | azo0358 | azo2069 | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 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. | 0.754 |
| azo1870 | azo0358 | azo1870 | azo0358 | 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 two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.729 |
| 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 | grpE | azo1870 | azo1064 | 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 [...] | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | 0.627 |
| 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 | htpG | azo1870 | azo1425 | 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 [...] | Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity. | 0.421 |
| 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 |
| clpP | azo0358 | azo2071 | azo0358 | 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. | Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases). | 0.729 |
| clpP | clpX | azo2071 | azo2070 | 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. | 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. | 0.999 |
| clpP | grpE | azo2071 | azo1064 | 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. | Probable heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several round [...] | 0.627 |
| clpP | hslU | azo2071 | azo0424 | 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. | 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 |
