ID   LEP_STRR6               Reviewed;         204 AA.
AC   P59662;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 1.
DT   25-MAY-2022, entry version 113.
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; Synonyms=spi; OrderedLocusNames=spr0364;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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 membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR   EMBL; AE007317; AAK99168.1; -; Genomic_DNA.
DR   RefSeq; NP_357958.1; NC_003098.1.
DR   RefSeq; WP_001048155.1; NC_003098.1.
DR   AlphaFoldDB; P59662; -.
DR   SMR; P59662; -.
DR   STRING; 171101.spr0364; -.
DR   MEROPS; S26.015; -.
DR   EnsemblBacteria; AAK99168; AAK99168; spr0364.
DR   GeneID; 60233331; -.
DR   GeneID; 66805594; -.
DR   KEGG; spr:spr0364; -.
DR   PATRIC; fig|171101.6.peg.405; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_5_0_9; -.
DR   OMA; IEPRWIP; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
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   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; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..204
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109534"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23498 MW;  3D56798C79C2C3CA CRC64;
     MNLFKNFLKE WGLFLLILSL LALSRIFFWS NVRVEGHSMD PTLADGEILF VVKHLPIDRF
     DIVVAHEEDG NKDIVKRVIG MPGDTIRYEN DKLYINDKET DEPYLADYIK RFKDDKLQST
     YSGKGFEGNK GTFFRSIAQK AQAFTVDVNY NTNFSFTVPE GEYLLLGDDR LVSSDSRHVG
     TFKAKDITGE AKFRFWPITR IGTF