Structural homology between virulence-associated bacterial adenylate cyclases.
The primary structure of the calmodulin-sensitive adenylate cyclase toxin from Bacillus anthracis has been determined from the corresponding nucleotide sequence and compared to that of the homologous toxin secreted by Bordetella pertussis. The cya gene of Bacillus anthracis encodes an 800 amino acid (aa) protein beginning with an N-terminal signal peptide. The central part of the B. anthracis adenylate cyclase includes a region of striking homology with the N-terminal part of the B. pertussis enzyme. In this region a particularly well conserved 24-aa peptide and two other less homologous peptides have been identified. These data corroborate the immunological relatedness of the two enzymes and suggest that the two prokaryotic calmodulin-sensitive adenylate cyclases originate from a common ancestor.
Escuyer
V
V
Unité des Antigènes Bactériens, Institut Pasteur, Paris, France.
Duflot
E
E
Sezer
O
O
Danchin
A
A
Mock
M
M
D000262:Adenylyl Cyclases / Q000235:genetics*; D001408:Bacillus anthracis / Q000201:enzymology / Q000235:genetics* / Q000472:pathogenicity; D001483:Base Sequence; D005075:Biological Evolution; D001886:Bordetella pertussis / Q000201:enzymology / Q000235:genetics* / Q000472:pathogenicity; D002147:Calmodulin / Q000502:physiology; D003470:Culture Media; D005796:Genes; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D014774:Virulence
D002147:Calmodulin; D003470:Culture Media; D000262:Adenylyl Cyclases