Plasmid-encoded autolysin in Bacillus anthracis: modular structure and catalytic properties.
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.
Mesnage
Stéphane
S
Toxines et Pathogénie Bactériennes (URA 2172, CNRS), Institut Pasteur, Paris, France. stephane.mesnage@bhdc.jussieu.fr
Fouet
Agnès
A
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
D009238:N-Acetylmuramoyl-L-alanine Amidase