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Journal of Bacteriology, June 2001, p. 3556-3563, Vol. 183, No. 12
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.12.3556-3563.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

HreP, an In Vivo-Expressed Protease of Yersinia enterocolitica, Is a New Member of the Family of Subtilisin/Kexin-Like Proteases

Gerhard Heusipp,1,dagger Glenn M. Young,1,Dagger and Virginia L. Miller1,2,*

Department of Molecular Microbiology1 and Division of Infectious Disease, Department of Pediatrics,2 Washington University School of Medicine and St. Louis Children's Hospital, St. Louis, Missouri 63110

Received 28 December 2000/Accepted 23 March 2001

The role of proteases in pathogenesis is well established for several microorganisms but has not been described for Yersinia enterocolitica. Previously, we identified a gene, hreP, which showed significant similarity to proteases in a screen for chromosomal genes of Y. enterocolitica that were exclusively expressed during an infection of mice. We cloned this gene by chromosome capture and subsequently determined its nucleotide sequence. Like inv, the gene encoding the invasin protein of Y. enterocolitica, hreP is located in a cluster of flagellum biosynthesis and chemotaxis genes. The genomic organization of this chromosomal region is different in Escherichia coli, Salmonella, and Yersinia pestis than in Y. enterocolitica. Analysis of the distribution of hreP between different Yersinia isolates and the relatively low G+C content of the gene suggests acquisition by horizontal gene transfer. Sequence analysis also revealed that HreP belongs to a family of eukaryotic subtilisin/kexin-like proteases. Together with the calcium-dependent protease PrcA of Anabaena variabilis, HreP forms a new subfamily of bacterial subtilisin/kexin-like proteases which might have originated from a common eukaryotic ancestor. Like other proteases of this family, HreP is expressed with an N-terminal prosequence. Expression of an HreP-His6 tag fusion protein in E. coli revealed that HreP undergoes autocatalytic processing at a consensus cleavage site of subtilisin/kexin-like proteases, thereby releasing the proprotein.

* Corresponding author. Mailing address: Department of Pediatrics, Washington University School of Medicine, Campus Box 8208, 660 S. Euclid Ave., St. Louis, MO 63110-1093. Phone: (314) 286-2891. Fax: (314) 286-2896. E-mail: virginia{at}borcim.wustl.edu.

dagger Present address: ZMBE, Institut für Infektiologie, 48149 Münster, Germany.

Dagger Present address: Department for Food Science and Technology, University of California, Davis, CA 95616.

Journal of Bacteriology, June 2001, p. 3556-3563, Vol. 183, No. 12
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.12.3556-3563.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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