node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BRADO0209 | BRADO0210 | BRADO0209 | BRADO0210 | Putative Aminoglycoside N(6')-acetyltransferase (aacA4); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Hypothetical protein; No homology to any previously reported sequences. | 0.775 |
BRADO0209 | hslU | BRADO0209 | BRADO0208 | Putative Aminoglycoside N(6')-acetyltransferase (aacA4); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 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. | 0.811 |
BRADO0209 | hslV | BRADO0209 | BRADO0211 | Putative Aminoglycoside N(6')-acetyltransferase (aacA4); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | ATP-dependent protease hslV (protease subunit of a proteasome-like degradation complex); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.791 |
BRADO0210 | BRADO0209 | BRADO0210 | BRADO0209 | Hypothetical protein; No homology to any previously reported sequences. | Putative Aminoglycoside N(6')-acetyltransferase (aacA4); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.775 |
BRADO0210 | hslU | BRADO0210 | BRADO0208 | Hypothetical protein; No homology to any previously reported sequences. | 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. | 0.784 |
BRADO0210 | hslV | BRADO0210 | BRADO0211 | Hypothetical protein; No homology to any previously reported sequences. | ATP-dependent protease hslV (protease subunit of a proteasome-like degradation complex); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.803 |
BRADO0321 | BRADO1403 | BRADO0321 | BRADO1403 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | Hypothetical protein; Doubtful CDS. | 0.687 |
BRADO0321 | BRADO3111 | BRADO0321 | BRADO3111 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | Putative ATP-dependent protease La; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.595 |
BRADO0321 | dnaJ | BRADO0321 | BRADO0163 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | Chaperone protein dnaJ, 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 [...] | 0.687 |
BRADO0321 | dnaK | BRADO0321 | BRADO0164 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.673 |
BRADO0321 | grpE | BRADO0321 | BRADO0171 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | Protein grpE (HSP-70 cofactor); 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 rounds [...] | 0.884 |
BRADO0321 | hslU | BRADO0321 | BRADO0208 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | 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. | 0.850 |
BRADO0321 | hslV | BRADO0321 | BRADO0211 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | ATP-dependent protease hslV (protease subunit of a proteasome-like degradation complex); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.847 |
BRADO0321 | htpG | BRADO0321 | BRADO6296 | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | Chaperone protein htpG (Heat shock protein htpG) (High temperature protein G); Molecular chaperone. Has ATPase activity. | 0.814 |
BRADO1403 | BRADO0321 | BRADO1403 | BRADO0321 | Hypothetical protein; Doubtful CDS. | Putative thioredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. | 0.687 |
BRADO1403 | BRADO3111 | BRADO1403 | BRADO3111 | Hypothetical protein; Doubtful CDS. | Putative ATP-dependent protease La; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.710 |
BRADO1403 | dnaK | BRADO1403 | BRADO0164 | Hypothetical protein; Doubtful CDS. | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.965 |
BRADO1403 | grpE | BRADO1403 | BRADO0171 | Hypothetical protein; Doubtful CDS. | Protein grpE (HSP-70 cofactor); 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 rounds [...] | 0.901 |
BRADO1403 | hslU | BRADO1403 | BRADO0208 | Hypothetical protein; Doubtful CDS. | 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. | 0.823 |
BRADO1403 | hslV | BRADO1403 | BRADO0211 | Hypothetical protein; Doubtful CDS. | ATP-dependent protease hslV (protease subunit of a proteasome-like degradation complex); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.800 |