Vibrio anguillarum metalloprotease is an extracellular zinc metalloprotease involved in the virulence mechanism of Vibrio anguillarum. It is synthesized from the empA gene a 611- residue precursor and naturally secreted via Sec secretion pathway in Vibrio anguillarum. In this study, heterologous expression of the empA gene encoding metalloprotease and export of the recombinant metalloprotease in Escherichia coli were examined. The empA gene was subcloned into pBAD24 with arabinose promoter and sequenced. The sequence encoded a polypeptide (611 amino acids) consisting of four domains: a signal peptide, an N-terminal propeptide, a mature region and a C-terminal propeptide. The empA gene inserted in plasmid pBAD24 was overexpressed in Top10 strain of E. Coli after arabinose induction. The 36kDa polypeptide munoblotting. It was found that recombinant metalloprotease with the EmpA activity and antigenicity was exported into the periplasm of Esherichia coli cells via Sec translocation pathway, whereas it was secreted into extracellular environments in V. anguillarum. The results imply that the expression, export and processing mechanism of the protein in E. Coli are similar to those in V. anguillarum.