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 membrane peptidases showing no sequence homology with other known classes of proteases. The prototype of the family, the Escherichia coli K-12 protein OmpT (or omptin), is an outer membrane endopeptidase with unusual specificity: it cleaves the peptide bond between two basic amino acids. A second distinct characteristic of OmpT is its ability to function even under extreme denaturing conditions (e.g. high concentration of urea). There is a growing number of reports that associate the proteases of the OmpT family with pathogenicity of certain gram-negative bacteria such as Yersinia pestis, Shigella flexneri, and pathogenic E. coli strains. This article reviews recent developments in the field of the OmpT proteases, provides a guide for the recognition of residues of the active site, and finally discusses potential uses of these proteins in biotechnology applications.
Stathopoulos
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Department of Biology, Washington University, St. Louis, MO 63130, USA. cstatho@biodec.wustl.edu
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D001665:Binding Sites; D001709:Biotechnology / Q000379:methods; D002462:Cell Membrane / Q000201:enzymology; D004755:Enterobacteriaceae / Q000201:enzymology / Q000472:pathogenicity; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000472:pathogenicity; D005810:Multigene Family; D011487:Protein Conformation; D011489:Protein Denaturation; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D001425:Bacterial Outer Membrane Proteins; D011993:Recombinant Fusion Proteins; D012697:Serine Endopeptidases; C057840:omptin outer membrane protease