LAUSR

Morganella morganii is an opportunistic pathogen which causes a wide range of clinical infections. It is well known that metalloproteases synthesized by pathogenic microorganisms play an important role as virulence factors. In this work, we have conducted bioinformatic analysis, sequencing, and cloning of the gene encoding a putative metalloprotease from M. morganii (AN CP004345.1, MU9_1718). We detected that the amino acid sequence of putative metalloprotease from M. morganii strain KT has 37% identity to actin-specific metalloproteases grimelysin and protealysin from Serratia grimesii and Serratia proteamaculans, respectively. Based on ORF MU9_1718 sequence, we have identified a metalloprotease gene in the genome of clinical isolate M. morganii ZM. The gene was cloned under the control of arabinose promoter into pBAD/Myc-His expression vector, and Escherichia coli DH5α cells were subsequently transformed by this vector. We also provide data indicating that the metalloprotease was overexpressed in E. coli DH5α cells as a 35 kDa protein.