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Journal of Bacteriology, June 1999, p. 3578-3581, Vol. 181, No. 11
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of Colicin S4 and Its Receptor, OmpW, a Minor Protein of the Escherichia coli Outer Membrane

Holger Pilsl,* David Smajs,dagger and Volkmar Braun

Mikrobiologie/Membranphysiologie, Universität Tübingen, Tübingen, Germany

Received 10 February 1999/Accepted 5 April 1999

Analysis of the nucleotide sequence of an Escherichia coli colicin S4 determinant revealed 76% identity to the pore-forming domain of the colicin A protein, 77% identity to the colicin A immunity protein, and 82% identity to the colicin A lysis protein. The N-terminal region, which is responsible for the Tol-dependent uptake of colicin S4, has 94% identity to the N-terminal region of colicin K. By contrast, the predicted receptor binding domain shows no sequence similarities to other colicins. Mutants that lacked the OmpW protein were resistant to colicin S4.

* Corresponding author. Mailing address: Mikrobiologie/Membranphysiologie, Auf der Morgenstelle 28, 72076 Tübingen, Germany. Phone: (49) 7071 2974620. Fax: (49) 7071 294634. E-mail: Holger.Pilsl{at}mikrobio.uni-tuebingen.de.

dagger Present address: Microbiology and Molecular Genetics, University of Texas Medical School, Houston, Texas.

Journal of Bacteriology, June 1999, p. 3578-3581, Vol. 181, No. 11
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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