| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CDI00998.1 | CDI01000.1 | BN873_100010 | BN873_100012 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | 0.495 |
| CDI00998.1 | cbpA | BN873_100010 | BN873_350128 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Curved DNA-binding protein. | 0.926 |
| CDI00998.1 | dnaJ | BN873_100010 | BN873_610127 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | 0.986 |
| CDI00998.1 | groL | BN873_100010 | BN873_270016 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Chaperone Hsp60 (GroEL), part of GroE chaperone system; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.908 |
| CDI00998.1 | groS | BN873_100010 | BN873_270017 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Chaperone Hsp10 (GroES), part of GroE chaperone system; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.866 |
| CDI00998.1 | grpE | BN873_100010 | BN873_610129 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Hsp 24 nucleotide exchange factor; 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 roun [...] | 0.984 |
| CDI00998.1 | hrcA | BN873_100010 | BN873_610130 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.817 |
| CDI00998.1 | hslU | BN873_100010 | BN873_240032 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | ATPase component of the HslUV protease, also functions as molecular chaperone; 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. | 0.637 |
| CDI00998.1 | hslV | BN873_100010 | BN873_240033 | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.575 |
| CDI01000.1 | CDI00998.1 | BN873_100012 | BN873_100010 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.495 |
| CDI01000.1 | cbpA | BN873_100012 | BN873_350128 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Curved DNA-binding protein. | 0.926 |
| CDI01000.1 | dnaJ | BN873_100012 | BN873_610127 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | 0.986 |
| CDI01000.1 | groL | BN873_100012 | BN873_270016 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Chaperone Hsp60 (GroEL), part of GroE chaperone system; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.908 |
| CDI01000.1 | groS | BN873_100012 | BN873_270017 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Chaperone Hsp10 (GroES), part of GroE chaperone system; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.866 |
| CDI01000.1 | grpE | BN873_100012 | BN873_610129 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Hsp 24 nucleotide exchange factor; 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 roun [...] | 0.984 |
| CDI01000.1 | hrcA | BN873_100012 | BN873_610130 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.817 |
| CDI01000.1 | hslU | BN873_100012 | BN873_240032 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | ATPase component of the HslUV protease, also functions as molecular chaperone; 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. | 0.637 |
| CDI01000.1 | hslV | BN873_100012 | BN873_240033 | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.575 |
| cbpA | CDI00998.1 | BN873_350128 | BN873_100010 | Curved DNA-binding protein. | Putative chaperone heat-shock protein; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.926 |
| cbpA | CDI01000.1 | BN873_350128 | BN873_100012 | Curved DNA-binding protein. | Putative heat-shock chaperone Hsp70/DnaK; Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the heat shock protein 70 family. | 0.926 |