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Journal of Bacteriology, January 2002, p. 331-334, Vol. 184, No. 1
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.1.331-334.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Plasmid-Encoded Autolysin in Bacillus anthracis: Modular Structure and Catalytic Properties

Stéphane Mesnage* and Agnès Fouet

Toxines et Pathogénie Bactériennes (URA 2172, CNRS), Institut Pasteur, Paris, France

Received 3 July 2001/ Accepted 11 October 2001

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.

* Corresponding author. Present address: L.R.M.A. (INSERM E0004), Université Paris VI, 75270 Paris Cédex 06, France. Phone: 33 1 42 34 68 62. Fax: 33 1 43 25 68 12. E-mail: stephane.mesnage{at}bhdc.jussieu.fr.

Journal of Bacteriology, January 2002, p. 331-334, Vol. 184, No. 1
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.1.331-334.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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