Identification and characterization of a peptidoglycan hydrolase from Rhodobacter johrii

Abstract The bacterial whole genome sequences are available in the database therefore explored for the varieties of known and unknown proteins. Bacteria harbor various peptidoglycan hydrolases that cleave peptidoglycan and play an important role in the cell division, growth, spore differentiation and development. In the present study, we report a peptidoglycan hydrolase in an endospore producing phototrophic proteobacterium Rhodobacter johrii. The Peptidoglycan Hydrolase of Rba. johrii (PgHR) can actively hydrolyze the intact spore cortex peptidoglycan (sacculi). The protein contains a pre-peptide precursor which has a Hydrolase-2 (PF07486) family conserved domain. PgHR protein has SleB like properties which are spore cortex-lytic enzymes involved in the depolymerization of cortex peptidoglycan present and characterized in Bacillus spp. The expression pattern of PgHR through qRT-PCR suggests its role in stationary phase of Rba. johrii. This is a new type of peptidoglycan hydrolase reported from a proteobacterium.