ID   SPPA_SALTI              Reviewed;         618 AA.
AC   Q8Z6F3; Q7CA98;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Protease 4;
DE            EC=3.4.21.-;
DE   AltName: Full=Endopeptidase IV;
DE   AltName: Full=Protease IV;
DE   AltName: Full=Signal peptide peptidase;
GN   Name=sppA; OrderedLocusNames=STY1819, t1174;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Digests cleaved signal peptides in vitro, its in vivo
CC       function is unknown. This activity is necessary to maintain proper
CC       secretion of mature proteins across the membrane (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD02059.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68831.1; -; Genomic_DNA.
DR   RefSeq; NP_456217.1; NC_003198.1.
DR   RefSeq; WP_001259874.1; NZ_WSUR01000034.1.
DR   AlphaFoldDB; Q8Z6F3; -.
DR   SMR; Q8Z6F3; -.
DR   STRING; 220341.16502896; -.
DR   EnsemblBacteria; AAO68831; AAO68831; t1174.
DR   KEGG; stt:t1174; -.
DR   KEGG; sty:STY1819; -.
DR   PATRIC; fig|220341.7.peg.1832; -.
DR   eggNOG; COG0616; Bacteria.
DR   HOGENOM; CLU_008856_1_1_6; -.
DR   OMA; DPKGQYL; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd07019; S49_SppA_1; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR004634; Pept_S49_pIV.
DR   InterPro; IPR004635; Pept_S49_SppA.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR033854; S49_SppA_1.
DR   Pfam; PF01343; Peptidase_S49; 2.
DR   PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   TIGRFAMs; TIGR00705; SppA_67K; 1.
DR   TIGRFAMs; TIGR00706; SppA_dom; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW   Serine protease; Transmembrane; Transmembrane helix.
FT   CHAIN           1..618
FT                   /note="Protease 4"
FT                   /id="PRO_0000394511"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..618
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        209
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   618 AA;  67189 MW;  9BD2A76ACF967464 CRC64;
     MRTLWRFIAG FFKWTWRVLN FVREMVLNLF FIFLVLVGVG IWMQIGNGSN SEQTARGALL
     LDISGVIVDK PSTNHRLGAL GRQLFGASSD RLQENSLFDI VNAIRQAKDD RNITGIVLDL
     KNFTGADQPS MRYIGKALRE FRDSGKPVFA VGENYSQGQY YLASFANKIW LSPQGQVDLH
     GFATNGLYYK TLLDKLKVST HVFRVGTYKS AVEPFIRDDM SPAAREADSR WIGELWQNYL
     HTVSANRQIS PQQLFPGAQA IIDGLTSVGG DTAKYALDHK LVDALASSAD VEKALTKQFG
     WSKTENNYRA ISYYDYSLKT PADTGGTIAV IFANGAIMDG EETPGNVGGD TTASQIRDAR
     LDPKVKAIVL RVNSPGGSVN ASEVIRAELA AARAAGKPVV VSMGGMAASG GYWISTPANY
     IVASPSTLTG SIGIFGVINT VENSLSSIGV HSDGVSTSPL ADISMTKALS PEVQQMMQLS
     IEYGYKRFIT LVADARKRTP EQIDKIAQGH VWTGEDAKAN GLVDSLGDFD DAVAKAAELA
     KLKQWHLDYY QDEPTVLDMV MDSMTGSVRA MLPEAIQAML PAPLVSAANT VKAEGDKLAA
     FNDPQNRYAF CLTCANVR