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Journal of Bacteriology, September 2007, p. 6425-6436, Vol. 189, No. 17
0021-9193/07/$08.00+0 doi:10.1128/JB.00702-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Department of Microbiology, University of Chicago, Chicago, Illinois 60637
Received 2 May 2007/ Accepted 7 June 2007
Vegetative forms of Bacillus anthracis replicate in tissues of an infected host and precipitate lethal anthrax disease. Upon host death, bacilli form dormant spores that contaminate the environment, thereby gaining entry into new hosts where spores germinate and once again replicate as vegetative forms. We show here that sortase C, an enzyme that is required for the formation of infectious spores, anchors BasI polypeptide to the envelope of predivisional sporulating bacilli. BasI anchoring to the cell wall requires the active site cysteine of sortase C and an LPNTA motif sorting signal at the C-terminal end of the BasI precursor. The LPNTA motif of BasI is cleaved between the threonine (T) and the alanine (A) residue; the C-terminal carboxyl group of threonine is subsequently amide linked to the side chain amino group of diaminopimelic acid within the wall peptides of B. anthracis peptidoglycan.
Published ahead of print on 22 June 2007.
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