ID   OMPP_ECOLI              Reviewed;         315 AA.
AC   P34210;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Outer membrane protease OmpP;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=ompP; Synonyms=ompX; OrderedLocusNames=ECOK12F029;
OS   Escherichia coli (strain K12).
OG   Plasmid F.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-43 AND
RP   179-192.
RC   STRAIN=K12 / ATCC 12435 / DSM 5695 / NBRC 3302 / NCIMB 9481 / W1485;
RX   PubMed=8288530; DOI=10.1128/jb.176.2.359-367.1994;
RA   Kaufmann A., Stierhof Y.-D., Henning U.;
RT   "New outer membrane-associated protease of Escherichia coli K-12.";
RL   J. Bacteriol. 176:359-367(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / CR63;
RA   Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT   "Complete nucleotide sequence of the F plasmid: its implications for
RT   organization and diversification of plasmid genomes.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=10561486; DOI=10.1016/s0014-5793(99)01418-0;
RA   Matsuo E., Sampei G., Mizobuchi K., Ito K.;
RT   "The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle
RT   to E. coli-based protein production.";
RL   FEBS Lett. 461:6-8(1999).
CC   -!- FUNCTION: Protease; also acts as a receptor for bacteriophage Ox2.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the peptidase A26 family. {ECO:0000305}.
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DR   EMBL; X74278; CAA52338.1; -; Genomic_DNA.
DR   EMBL; AP001918; BAA97899.1; -; Genomic_DNA.
DR   PIR; A36944; A36944.
DR   RefSeq; NP_061408.1; NC_002483.1.
DR   RefSeq; WP_001193612.1; NZ_AP001918.1.
DR   AlphaFoldDB; P34210; -.
DR   SMR; P34210; -.
DR   MEROPS; A26.002; -.
DR   TCDB; 9.B.50.1.2; the outer membrane beta-barrel endoprotease, omptin (omptin) family.
DR   PRIDE; P34210; -.
DR   BRENDA; 3.4.23.49; 2026.
DR   PRO; PR:P34210; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR020080; OM_adhesin/peptidase_omptin.
DR   InterPro; IPR020079; Peptidase_A26_CS.
DR   InterPro; IPR000036; Peptidase_A26_omptin.
DR   Pfam; PF01278; Omptin; 1.
DR   PIRSF; PIRSF001522; Peptidase_A26; 1.
DR   PRINTS; PR00482; OMPTIN.
DR   SUPFAM; SSF69917; SSF69917; 1.
DR   PROSITE; PS00834; OMPTIN_1; 1.
DR   PROSITE; PS00835; OMPTIN_2; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Cell outer membrane; Direct protein sequencing;
KW   Hydrolase; Membrane; Plasmid; Protease; Signal; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:8288530"
FT   CHAIN           24..315
FT                   /note="Outer membrane protease OmpP"
FT                   /id="PRO_0000025817"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  35499 MW;  45595973C6B2B149 CRC64;
     MQTKLLAIML AAPVVFSSQE ASASDFFGPE KISTEINLGT LSGKTKERVY EPEEGGRKVS
     QLDWKYSNAA ILKGAVNWEL NPWLSVGAAG WTTLNSRGGN MVDQDWMDSG TPGTWTDESR
     HPDTRLNYAN EFDLNVKGWF LKESDYRLAI MAGYQESRYS FNATGGTYIY SENGGFRNET
     GALPDKIKVI GYKQHFKIPY VGLTGNYRYD NFEFGGAFKY SGWVRGSDND EHYVRQTTFR
     SKVINQNYYS VAVNAGYYIT PEAKVYIEGV WSRLTNKKGD TSLYDRSDNT SEHNNNGAGI
     ENYNFITTAG LKYTF