PMID:8288530
| Citation |
Kaufmann, A, Stierhof, YD and Henning, U (1994) New outer membrane-associated protease of Escherichia coli K-12. J. Bacteriol. 176:359-67 |
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| 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. |
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| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/isolation & purification; Base Sequence; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/ultrastructure; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Hydrolases; Microscopy, Immunoelectron; Molecular Sequence Data; Sequence Analysis; Sequence Homology, Amino Acid; Serine Endopeptidases/genetics; Transcription, Genetic |
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