Escherichia coli protease VII (EC 3.4.21.87) (omptin) (gene ompT) [1] is an
outer-membrane associated protease with a specificity for paired basic
residues. It seems to be an aspartyl protease [2] inhibited by zinc ions.
Omptin is highly similar to the following proteins:
Salmonella typhimurium outer membrane protease E (gene pgtE) [3], also
specific for paired basic residues.
Yersinia pestis coagulase/fibrinolysin (plasminogen activator) (gene pla)
[4]. This enzyme is encoded on a plasmid required for the pathogenic
potential of the bacteria. It cleaves and activates plasminogen at the foci
of infection; this allows plasmin to degrade fibrin barriers thus promoting
the invasiveness of the plague bacteria.
The mature forms of these enzymes are proteins of about 280 to 300 amino-acid
residues. As signature patterns, we selected two well conserved regions in the
central part of these proteins.
Note:
These proteins belong to family A26 in the classification of peptidases
[6,E1].
PROSITE methods (with tools and information) covered by this documentation:
References
1
Authors
Sugimura K. Nishihara T.
Title
Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT.
Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: relationship to ompT of Escherichia coli and gene E of Salmonella typhimurium.
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