| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo2132 | clpX | azo2132 | azo2070 | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | 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. | 0.622 |
| azo2132 | dnaJ1 | azo2132 | azo1062 | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | 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 [...] | 0.735 |
| azo2132 | dnaJ2 | azo2132 | azo1266 | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | 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. | 0.769 |
| azo2132 | grpE | azo2132 | azo1064 | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | 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 [...] | 0.797 |
| azo2132 | hslU | azo2132 | azo0424 | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | 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. | 0.843 |
| azo2132 | hslV | azo2132 | azo0423 | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.805 |
| azo2132 | htpG | azo2132 | azo1425 | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity. | 0.774 |
| clpX | azo2132 | azo2070 | azo2132 | 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. | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | 0.622 |
| clpX | groES1 | azo2070 | azo0973 | 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. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.451 |
| clpX | groES2 | azo2070 | azo2365 | 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. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.431 |
| clpX | grpE | azo2070 | azo1064 | 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. | 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 [...] | 0.458 |
| clpX | hslU | azo2070 | azo0424 | 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. | 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. | 0.927 |
| clpX | hslV | azo2070 | azo0423 | 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. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.934 |
| clpX | lon | azo2070 | azo2069 | 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. | 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. | 0.834 |
| dnaJ1 | azo2132 | azo1062 | azo2132 | 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 [...] | Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein. | 0.735 |
| dnaJ1 | groES1 | azo1062 | azo0973 | 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 [...] | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.718 |
| dnaJ1 | groES2 | azo1062 | azo2365 | 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 [...] | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.718 |
| dnaJ1 | grpE | azo1062 | azo1064 | 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 [...] | 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 [...] | 0.983 |
| dnaJ1 | hslU | azo1062 | azo0424 | 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 [...] | 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. | 0.863 |
| dnaJ1 | hslV | azo1062 | azo0423 | 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 [...] | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.837 |
