New outer membrane-associated protease of Escherichia coli K-12.
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.
Kaufmann
A
A
Max-Planck-Institut für Biologie, Tübingen, Germany.
Stierhof
Y D
YD
Henning
U
U
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000302:isolation & purification; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics* / Q000648:ultrastructure; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D006867:Hydrolases; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics; D014158:Transcription, Genetic
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C482905:OmpX protein, E coli; D006867:Hydrolases; D012697:Serine Endopeptidases; C057840:omptin outer membrane protease