title: Plasmid-encoded autolysin in Bacillus anthracis: modular structure and catalytic properties.
abstract: A Bacillus anthracis virulence plasmid-encoded peptidoglycan hydrolase (AmiA) with sequence similarity to N-acetylmuramoyl-L-alanine amidases hydrolyzes peptidoglycan independently of cell wall binding. Residues H341, E355, H415, and E486 are absolutely required for catalysis. Many AmiA paralogs are fused to different sorting signals, suggesting that these modular proteins result from domain shuffling.
authors.affiliation: Toxines et Pathogénie Bactériennes (URA 2172, CNRS), Institut Pasteur, Paris, France. stephane.mesnage@bhdc.jussieu.fr
authors.forename: Stéphane
authors.initials: S
authors.lastname: Mesnage
authors.forename: Agnès
authors.initials: A
authors.lastname: Fouet
mesh_terms: D001408:Bacillus anthracis / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D020134:Catalytic Domain; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics* / Q000378:metabolism; D010957:Plasmids / Q000235:genetics*; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D009238:N-Acetylmuramoyl-L-alanine Amidase