Amino acid sequence of pheromone-inducible surface protein in Enterococcus faecalis, that is encoded on the conjugative plasmid pPD1.
The major pheromone-inducible protein, PD78, believed to contribute to bacterial conjugation, was purified from Enterococcus (formerly Streptococcus) faecalis cells containing the plasmid pPD1. A cloned EcoRI-BglII 3.6-kbp fragment of the plasmid pAM351(pPdl::Tn916) contained an open reading frame corresponding to 467 amino acid residues representing PD78. In a central region of the deduced protein, there is a repeated sequence of X-X-Pro that is repeated 15 times. This is analogous to the Gln-Gln-Pro repeat in the C-terminal region of TraD product encoded on the R100 plasmid in Escherichia coli.
Nakayama
J
J
Department of Agricultural Chemistry, University of Tokyo, Japan.
Nagasawa
H
H
Isogai
A
A
Clewell
D B
DB
Suzuki
A
A
D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D013293:Enterococcus faecalis / Q000235:genetics*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D010675:Pheromones; D010957:Plasmids
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D010675:Pheromones; C064923:TraF protein, Enterococcus faecalis