ID   OMPT_ECOLI              Reviewed;         317 AA.
AC   P09169;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Protease 7;
DE            EC=3.4.23.49;
DE   AltName: Full=Omptin;
DE   AltName: Full=Outer membrane protein 3B;
DE   AltName: Full=Protease A;
DE   AltName: Full=Protease VII;
DE   Flags: Precursor;
GN   Name=ompT; OrderedLocusNames=b0565, JW0554;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-36.
RC   STRAIN=K12;
RX   PubMed=3278297; DOI=10.1093/nar/16.3.1209;
RA   Grodberg J., Lundrigan M.D., Toledo D.L., Mangel W.F., Dunn J.J.;
RT   "Complete nucleotide sequence and deduced amino acid sequence of the ompT
RT   gene of Escherichia coli K-12.";
RL   Nucleic Acids Res. 16:1209-1209(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-40, AND
RP   CHARACTERIZATION.
RX   PubMed=3056908; DOI=10.1128/jb.170.12.5625-5632.1988;
RA   Sugimura K., Nisihihara T.;
RT   "Purification, characterization, and primary structure of Escherichia coli
RT   protease VII with specificity for paired basic residues: identity of
RT   protease VII and OmpT.";
RL   J. Bacteriol. 170:5625-5632(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-16.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [7]
RP   PROTEIN SEQUENCE OF 21-24.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9629924; DOI=10.1002/elps.1150190539;
RA   Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
RA   Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
RT   "Extraction of membrane proteins by differential solubilization for
RT   separation using two-dimensional gel electrophoresis.";
RL   Electrophoresis 19:837-844(1998).
RN   [8]
RP   FUNCTION.
RX   PubMed=9683502; DOI=10.1128/jb.180.15.4002-4006.1998;
RA   Stumpe S., Schmid R., Stephens D.L., Georgiou G., Bakker E.P.;
RT   "Identification of OmpT as the protease that hydrolyzes the antimicrobial
RT   peptide protamine before it enters growing cells of Escherichia coli.";
RL   J. Bacteriol. 180:4002-4006(1998).
RN   [9]
RP   CHARACTERIZATION, PROTEIN SEQUENCE OF 21-25, AND MUTAGENESIS OF GLY-236 AND
RP   LYS-237.
RC   STRAIN=BL21-DE3, and K12 / DH5-alpha;
RX   PubMed=10651827; DOI=10.1046/j.1432-1327.2000.01073.x;
RA   Kramer R.A., Zandwijken D., Egmond M.R., Dekker N.;
RT   "In vitro folding, purification and characterization of Escherichia coli
RT   outer membrane protease ompT.";
RL   Eur. J. Biochem. 267:885-893(2000).
RN   [10]
RP   ACTIVE SITE, AND MUTAGENESIS OF ASP-103; ASP-105 AND ASP-230.
RC   STRAIN=BL21-DE3, and K12 / DH5-alpha;
RX   PubMed=11576541; DOI=10.1016/s0014-5793(01)02863-0;
RA   Kramer R.A., Vandeputte-Rutten L., de Roon G.J., Gros P., Dekker N.,
RA   Egmond M.R.;
RT   "Identification of essential acidic residues of outer membrane protease
RT   OmpT supports a novel active site.";
RL   FEBS Lett. 505:426-430(2001).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=11566868; DOI=10.1093/emboj/20.18.5033;
RA   Vandeputte-Rutten L., Kramer R.A., Kroon J., Dekker N., Egmond M.R.,
RA   Gros P.;
RT   "Crystal structure of the outer membrane protease OmpT from Escherichia
RT   coli suggests a novel catalytic site.";
RL   EMBO J. 20:5033-5039(2001).
CC   -!- FUNCTION: Protease that can cleave T7 RNA polymerase, ferric
CC       enterobactin receptor protein (FEP), antimicrobial peptide protamine
CC       and other proteins. This protease has a specificity for paired basic
CC       residues. {ECO:0000269|PubMed:9683502}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Has a virtual requirement for Arg in the P1 position and a
CC         slightly less stringent preference for this residue in the P1'
CC         position, which can also contain Lys, Gly or Val.; EC=3.4.23.49;
CC   -!- ACTIVITY REGULATION: Inhibited by zinc.
CC   -!- SUBUNIT: Homopentamer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: Was originally classified as a serine protease, but it
CC       seems that OmpT could have a novel catalytic mechanism involving an
CC       Asp/His dyad and a pair of Asp.
CC   -!- MISCELLANEOUS: Encoded by the cryptic lambdoid prophage DLP12.
CC   -!- SIMILARITY: Belongs to the peptidase A26 family. {ECO:0000305}.
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DR   EMBL; X06903; CAA30008.1; -; Genomic_DNA.
DR   EMBL; M23630; AAA24430.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40761.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73666.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35199.2; -; Genomic_DNA.
DR   PIR; A31387; A31387.
DR   RefSeq; NP_415097.1; NC_000913.3.
DR   RefSeq; WP_001201845.1; NZ_LN832404.1.
DR   PDB; 1I78; X-ray; 2.60 A; A/B=21-317.
DR   PDBsum; 1I78; -.
DR   AlphaFoldDB; P09169; -.
DR   SMR; P09169; -.
DR   BioGRID; 4263520; 171.
DR   STRING; 511145.b0565; -.
DR   MEROPS; A26.001; -.
DR   MoonProt; P09169; -.
DR   TCDB; 9.B.50.1.1; the outer membrane beta-barrel endoprotease, omptin (omptin) family.
DR   jPOST; P09169; -.
DR   PaxDb; 511145-b0565; -.
DR   EnsemblBacteria; AAC73666; AAC73666; b0565.
DR   GeneID; 945185; -.
DR   KEGG; ecj:JW0554; -.
DR   KEGG; eco:b0565; -.
DR   PATRIC; fig|1411691.4.peg.1709; -.
DR   EchoBASE; EB0667; -.
DR   eggNOG; COG4571; Bacteria.
DR   HOGENOM; CLU_063041_1_0_6; -.
DR   InParanoid; P09169; -.
DR   OMA; HENFEFG; -.
DR   OrthoDB; 2112810at2; -.
DR   PhylomeDB; P09169; -.
DR   BioCyc; EcoCyc:EG10673-MONOMER; -.
DR   BioCyc; MetaCyc:EG10673-MONOMER; -.
DR   BRENDA; 3.4.23.49; 2026.
DR   EvolutionaryTrace; P09169; -.
DR   PRO; PR:P09169; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004175; F:endopeptidase activity; IMP:EcoliWiki.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IMP:EcoliWiki.
DR   GO; GO:0006508; P:proteolysis; IMP:EcoliWiki.
DR   Gene3D; 2.40.128.90; OMPT-like; 1.
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; OMPT-like; 1.
DR   PROSITE; PS00834; OMPTIN_1; 1.
DR   PROSITE; PS00835; OMPTIN_2; 1.
DR   SWISS-2DPAGE; P09169; -.
PE   1: Evidence at protein level;
KW   3D-structure; Aspartyl protease; Cell outer membrane;
KW   Direct protein sequencing; Hydrolase; Membrane; Protease;
KW   Reference proteome; Signal; Transmembrane; Transmembrane beta strand.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:10651827,
FT                   ECO:0000269|PubMed:3056908, ECO:0000269|PubMed:3278297,
FT                   ECO:0000269|PubMed:9629924"
FT   CHAIN           21..317
FT                   /note="Protease 7"
FT                   /id="PRO_0000025815"
FT   TOPO_DOM        21..31
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..41
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..69
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..78
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..83
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..92
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..130
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..140
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..145
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..156
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..197
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..209
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..211
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..221
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..261
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..264
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..274
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..316
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000305|PubMed:11576541"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000305|PubMed:11576541"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000305|PubMed:11576541"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000305|PubMed:11576541"
FT   MUTAGEN         103
FT                   /note="D->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11576541"
FT   MUTAGEN         105
FT                   /note="D->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11576541"
FT   MUTAGEN         230
FT                   /note="D->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11576541"
FT   MUTAGEN         236..237
FT                   /note="GK->KG: 70% of wild-type enzymatic activity."
FT   MUTAGEN         237
FT                   /note="K->T: 40% of wild-type enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:10651827"
FT   MUTAGEN         238
FT                   /note="R->L: Loss of activity."
FT   STRAND          32..51
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   TURN            52..56
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          57..78
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          81..95
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          97..105
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          116..142
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          144..164
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          167..170
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          188..209
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          212..233
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          239..262
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          265..287
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   TURN            288..291
FT                   /evidence="ECO:0007829|PDB:1I78"
FT   STRAND          292..316
FT                   /evidence="ECO:0007829|PDB:1I78"
SQ   SEQUENCE   317 AA;  35562 MW;  CA112FE7F6336F61 CRC64;
     MRAKLLGIVL TTPIAISSFA STETLSFTPD NINADISLGT LSGKTKERVY LAEEGGRKVS
     QLDWKFNNAA IIKGAINWDL MPQISIGAAG WTTLGSRGGN MVDQDWMDSS NPGTWTDESR
     HPDTQLNYAN EFDLNIKGWL LNEPNYRLGL MAGYQESRYS FTARGGSYIY SSEEGFRDDI
     GSFPNGERAI GYKQRFKMPY IGLTGSYRYE DFELGGTFKY SGWVESSDND EHYDPGKRIT
     YRSKVKDQNY YSVAVNAGYY VTPNAKVYVE GAWNRVTNKK GNTSLYDHNN NTSDYSKNGA
     GIENYNFITT AGLKYTF
//