STRUCTURAL FEATURES, PHYSIOLOGICAL ROLES, AND BIOTECHNOLOGICAL APPLICATIONS OF THE MEMBRANE PROTEASES OF THE OMPT BACTERIAL ENDOPEPTIDASE FAMILY - A MICRO-REVIEW

The proteins of the OmpT family represent a new class of integral memb rane peptidases showing no sequence homology with other known classes of proteases, The prototype of the family, the Escherichia coli K-12 p rotein OmpT (or omptin), is an outer membrane endopeptidase with unusu al specificity; It cleaves the peptide bond between two basic amino ac ids. A second distinct characteristic of OmpT is its ability to functi on even under extreme denaturing conditions (e.g. high concentration o f urea). There is a growing number of reports that associate the prote ases of the OmpT family with pathogenicity of certain gram-negative ba cteria such as Yersinia pestis, Shigella flexneri, and pathogenic E. c oli strains. This article reviews recent developments in the field of the OmpT proteases, provides a guide for tile recognition of residues of the active site, and finally discusses potential uses of these prot eins in biotechnology applications.