ID   PGTE_SALTY              Reviewed;         312 AA.
AC   P06185; Q9KI72;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Outer membrane protease E;
DE            Short=E protein;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=pgtE; Synonyms=prtA; OrderedLocusNames=STM2395;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3023201; DOI=10.1016/0378-1119(86)90131-9;
RA   Yu G.-Q., Hong J.-S.;
RT   "Identification and nucleotide sequence of the activator gene of the
RT   externally induced phosphoglycerate transport system of Salmonella
RT   typhimurium.";
RL   Gene 45:51-57(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10869088; DOI=10.1128/jb.182.14.4077-4086.2000;
RA   Guina T., Yi E.C., Wang H., Hackett M., Miller S.I.;
RT   "A PhoP-regulated outer membrane protease of Salmonella enterica serovar
RT   typhimurium promotes resistance to alpha-helical antimicrobial peptides.";
RL   J. Bacteriol. 182:4077-4086(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [4]
RP   SIMILARITY TO OMPT, AND FUNCTION.
RX   PubMed=2651422; DOI=10.1128/jb.171.5.2903-2905.1989;
RA   Grodberg J., Dunn J.J.;
RT   "Comparison of Escherichia coli K-12 outer membrane protease OmpT and
RT   Salmonella typhimurium E protein.";
RL   J. Bacteriol. 171:2903-2905(1989).
CC   -!- FUNCTION: Protease that can cleave T7 RNA polymerase. Specific for
CC       paired basic residues. {ECO:0000269|PubMed:2651422}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA27185.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M13923; AAA27185.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AF239770; AAF85951.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21295.1; -; Genomic_DNA.
DR   PIR; B28255; B28255.
DR   RefSeq; NP_461336.1; NC_003197.2.
DR   RefSeq; WP_000716007.1; NC_003197.2.
DR   AlphaFoldDB; P06185; -.
DR   SMR; P06185; -.
DR   STRING; 99287.STM2395; -.
DR   MEROPS; A26.004; -.
DR   TCDB; 9.B.50.1.3; the outer membrane beta-barrel endoprotease, omptin (omptin) family.
DR   PaxDb; P06185; -.
DR   EnsemblBacteria; AAL21295; AAL21295; STM2395.
DR   GeneID; 1253917; -.
DR   KEGG; stm:STM2395; -.
DR   PATRIC; fig|99287.12.peg.2533; -.
DR   HOGENOM; CLU_063041_1_0_6; -.
DR   OMA; YNYDNGA; -.
DR   PhylomeDB; P06185; -.
DR   BioCyc; SENT99287:STM2395-MON; -.
DR   BRENDA; 3.4.23.49; 5542.
DR   Proteomes; UP000001014; 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..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..312
FT                   /note="Outer membrane protease E"
FT                   /id="PRO_0000025818"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000250"
FT   CONFLICT        296
FT                   /note="G -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   312 AA;  35055 MW;  5A6841732AF2E8C4 CRC64;
     MKKHAIAVMM IAVFSESVYA ESALFIPDVS PDSVTTSLSV GVLNGKSREL VYDTDTGRKL
     SQLDWKIKNV ATLQGDLSWE PYSFMTLDAR GWTSLASGSG HMVDHDWMSS EQPGWTDRSI
     HPDTSVNYAN EYDLNVKGWL LQGDNYKAGV TAGYQETRFS WTARGGSYIY DNGRYIGNFP
     HGVRGIGYSQ RFEMPYIGLA GDYRINDFEC NVLFKYSDWV NAHDNDEHYM RKLTFREKTE
     NSRYYGASID AGYYITSNAK IFAEFAYSKY EEGKGGTQII DKTSGDTAYF GGDAAGIANN
     NYTVTAGLQY RF