COMPLETE NUCLEOTIDE-SEQUENCE OF A GENE PRTR OF PORPHYROMONAS-GINGIVALIS W50 ENCODING A 132KDA PROTEIN THAT CONTAINS AN ARGININE-SPECIFIC THIOL ENDOPEPTIDASE DOMAIN AND A HEMAGGLUTININ DOMAIN

We have purified from Porphyromonas gingivalis W50 a 45 kDa arginine-s pecific, thiol-activated, EDTA-sensitive endopeptidase, designated prt R. Oligonucleotide probes based on the N-terminal amino acid sequence were used to isolate a genomic fragment containing an open reading fra me (3654 bp) with the potential to encode a 132 kDa protein including the prtR N-terminus. Analysis of this prtR gene revealed that the pred icted nascent product contains a protease domain followed by a haemagg lutinin domain and is post-translationally processed by proteolytic (p ossibly autolytic) events to produce a 43-54 kDa arginine-specific, th iol protease and a 41-53 kDa haemagglutinin. Comparison of the prtR wi th the P. gingivalis prtH gene suggests that the prtH gene product als o contains protease and haemagglutinin domains but in the reverse orde r to that in the prtR. An overlapping but shifted reading frame at the 3' end of the prtR encodes the 5' region of the prtH. (C) 1995 Academ ic Press, Inc.