The gene encoding a 51 kDa polypeptide of Porphyromonas gingivalis 381
was isolated by immunoblotting using an antiserum raised against P. g
ingivalis alkaline phosphatase. DNA sequence analysis of a 2.5 kb DNA
fragment containing a gene encoding the 51 kDa protein revealed one co
mplete and two incomplete ORFs, Database searches using the FASTA prog
ram revealed significant homology between the P. gingivalis 51 kDa pro
tein and the MurC protein of Escherichia coil, which functions in pept
idoglycan synthesis. The cloned 51 kDa protein encoded a functional pr
oduct that complemented an E. coil murC mutant. Moreover, the ORF just
upstream of murC coded for a protein that was 31% homologous with the
E. coli MurG protein. The ORF just downstream of murC coded for a pro
tein that was 17% homologous with the Streptococcus pneumoniae penicil
lin-binding protein 2B (PBP2B), which functions in peptidoglycan synth
esis and is responsible for antibiotic resistance. These results sugge
st that P. gingivalis contains a homologue of the E. coli peptidoglyca
n synthesis gene murC and indicate the possibility of a cluster of gen
es responsible for cell division and cell growth, as in the E. coil mr
a region.