OMPT_ECO57
ID OMPT_ECO57 Reviewed; 317 AA.
AC P58603;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=Z1931, ECs1663;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A26 family. {ECO:0000305}.
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DR EMBL; AE005174; AAG56020.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35086.1; -; Genomic_DNA.
DR PIR; G90836; G90836.
DR PIR; H85694; H85694.
DR RefSeq; NP_309690.1; NC_002695.1.
DR RefSeq; WP_001201843.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58603; -.
DR SMR; P58603; -.
DR STRING; 155864.EDL933_1860; -.
DR MEROPS; A26.001; -.
DR PRIDE; P58603; -.
DR EnsemblBacteria; AAG56020; AAG56020; Z1931.
DR EnsemblBacteria; BAB35086; BAB35086; ECs_1663.
DR GeneID; 913212; -.
DR KEGG; ece:Z1931; -.
DR KEGG; ecs:ECs_1663; -.
DR PATRIC; fig|386585.9.peg.1760; -.
DR eggNOG; COG4571; Bacteria.
DR HOGENOM; CLU_063041_1_0_6; -.
DR OMA; HENFEFG; -.
DR BRENDA; 3.4.23.49; 2026.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 3: Inferred from homology;
KW Aspartyl protease; Cell outer membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..317
FT /note="Protease 7"
FT /id="PRO_0000025816"
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"
FT ACT_SITE 105
FT /evidence="ECO:0000305"
FT ACT_SITE 230
FT /evidence="ECO:0000305"
FT ACT_SITE 232
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35593 MW; D13F5786049B4E41 CRC64;
MRAKLLGIVL TTPIAISSFA STETLSFTPD NINADISLGT LSGKTKERVY LAEEGGRKVS
QLDWKFNNAA IIKGAINWDL MPQISIGAAG WTTLGSRGGN MVDQDWMDSS NPGTWTDESR
HPDTQLNYAN EFDLNIKGWL LNEPNYRLGL MAGYQESRYS FTARGGSYIY SSEEGFRDDI
GSFPNGERAI GYKQRFKMPY IGLTGSYRYE DFELGGTFKY SGWVEASDND EHYDPGKRIT
YRSKVKDQNY YSVSVNAGYY VTPNAKVYVE GTWNRVTNKK GNTSLYDHND NTSDYSKNGA
GIENYNFITT AGLKYTF
