OMPT_ECOLI
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 03-AUG-2022, entry version 173.
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; Proteobacteria; 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 TCDB; 9.B.50.1.1; the outer membrane beta-barrel endoprotease, omptin (omptin) family.
DR SWISS-2DPAGE; P09169; -.
DR jPOST; P09169; -.
DR PaxDb; P09169; -.
DR PRIDE; P09169; -.
DR EnsemblBacteria; AAC73666; AAC73666; b0565.
DR EnsemblBacteria; BAA35199; BAA35199; BAA35199.
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 OMA; HENFEFG; -.
DR PhylomeDB; P09169; -.
DR BioCyc; EcoCyc:EG10673-MON; -.
DR BioCyc; MetaCyc:EG10673-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031230; C:intrinsic component of cell outer membrane; IDA:EcoliWiki.
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 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 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
