ID   LEP_SALTI               Reviewed;         324 AA.
AC   P0A1W3; P23697;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Signal peptidase I;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=lepB; OrderedLocusNames=STY2828, t0275;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD02784.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68000.1; -; Genomic_DNA.
DR   RefSeq; NP_457111.1; NC_003198.1.
DR   RefSeq; WP_000002559.1; NZ_WSUR01000007.1.
DR   AlphaFoldDB; P0A1W3; -.
DR   SMR; P0A1W3; -.
DR   STRING; 220341.16503794; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; AAO68000; AAO68000; t0275.
DR   KEGG; stt:t0275; -.
DR   KEGG; sty:STY2828; -.
DR   PATRIC; fig|220341.7.peg.2876; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_1_6; -.
DR   OMA; SDSRFWG; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.170.230.10; -; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   InterPro; IPR019766; Sign_pep_all-beta_subdom.
DR   PANTHER; PTHR43390; PTHR43390; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 2.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..324
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109517"
FT   TOPO_DOM        1..3
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..324
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35778 MW;  40607CDA15779575 CRC64;
     MANMFALILV IATLVTGILW CVDKFVFAPK RRARQAAAQT ASGDALDNAT LNKVAPKPGW
     LETGASVFPV LAIVLIVRSF LYEPFQIPSG SMMPTLLIGD FILVEKFAYG IKDPIYQKTL
     IETGHPKRGD IVVFKYPEDP KLDYIKRAVG LPGDKITYDP VAKEVTIQPG CSSGQACENA
     LPVTYSNVEP SDFVQTFARR NGGEATSGFF EVPLNETKEN GIRLTERKET LGDVTHRILM
     VPIAQDQLGM YYQQPGQPLA TWVVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGKAVAI
     WMSFDKQEGE WPTGVRLSRI GGIH