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J. Biol. Chem., Vol. 277, Issue 14, 11987-11994, April 5, 2002

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The Clostridium ramosum IgA Proteinase Represents a Novel Type of Metalloendopeptidase^*

Klaudia Kosowska^§¶, Jesper Reinholdt, Lone Kjær Rasmussen^**, Artur Sabat^§, Jan Potempa^§, Mogens Kilian, and Knud Poulsen

From the  Department of Medical Microbiology and Immunology,  Department of Oral Biology, and ^** Department of Molecular and Structural Biology, University of Aarhus, Aarhus C DK-8000, Denmark and the ^§ Department of Microbiology and Immunology, Institute of Molecular Biology and Biotechnology, Jagiellonian University, Krakow 30-387, Poland

Clostridium ramosum is part of the normal flora in the human intestine. Some strains produce an IgA proteinase that specifically cleaves human IgA1 and the IgA2m(1) allotype. This prolylendopeptidase was purified from a broth culture supernatant, and N-terminal sequences of the native protein and tryptic fragments thereof were determined. A fragment of the iga gene encoding the IgA proteinase was isolated using degenerate primers in PCR, and the complete gene was obtained by inverse PCR. The identity of the iga gene was confirmed by heterologous expression in Escherichia coli. The deduced amino acid sequence indicated a signal peptide of 30 residues and a secreted proteinase of 133,828 Da. A typical Gram-positive cell wall anchor motif was identified in the C terminus. The presence of a putative zinc-binding motif His-Glu-Phe-Gly-His together with inhibition studies indicate that the proteinase belongs to the zinc-dependent metalloproteinases. However, the sequence of the C. ramosum IgA proteinase shows no overall similarity to other proteins except for significant identity around the zinc-binding motif with family M6 of metalloendopeptidases, and the unique sequence of the IgA proteinase in this area presumably establishes a new subfamily. The GC percentage of the iga gene is significantly higher than that for the entire genome of C. ramosum, suggesting that the gene was acquired recently in evolution.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY028440.

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