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Journal of Bacteriology, May 2004, p. 3266-3269, Vol. 186, No. 10
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.10.3266-3269.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Department of Biochemistry and Molecular Biology,1 Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada2
Received 22 October 2003/ Accepted 3 February 2004
The fbpABC operon in Neisseria gonorrhoeae encodes an ATP-binding cassette transporter required for iron uptake from the host ferric binding proteins. The gene for the nucleotide-binding domain (fbpC) expressed in Escherichia coli has intrinsic ATPase activity (0.5 mmol/min/mg) uncoupled from the iron transport process. The FbpC E164D mutant is found to have a 10-fold reduction in specific activity. FbpC is covalently modified by 8-azido-[
32P]ATP, indicating that FbpC is a functional ATPase that likely combines with FbpB to form a ferric iron transporter.
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