New outer membrane-associated protease of Escherichia coli K-12.

Abstract:

:The gene for a new outer membrane-associated protease, designated OmpP, of Escherichia coli has been cloned and sequenced. The gene encodes a 315-residue precursor protein possessing a 23-residue signal sequence. Including conservative substitutions and omitting the signal peptides, OmpP is 87% identical to the outer membrane protease OmpT. OmpP possessed the same enzymatic activity as OmpT. Immuno-electron microscopy demonstrated the exposure of the protein at the cell surface. Digestion of intact cells with proteinase K removed 155 N-terminal residues of OmpP, while the C-terminal half remained protected. It is possible that much of this N-terminal part is cell surface exposed and carries the enzymatic activity. Synthesis of OmpP was found to be thermoregulated, as is the expression of ompT (i.e., there is a low rate of synthesis at low temperatures) and, in addition, was found to be controlled by the cyclic AMP system.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Kaufmann A,Stierhof YD,Henning U

doi

10.1128/jb.176.2.359-367.1994

subject

Has Abstract

pub_date

1994-01-01 00:00:00

pages

359-67

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

176

pub_type

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