ID   LEP_STRPN               Reviewed;         204 AA.
AC   O07344;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 140.
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=SP_0402;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=533;
RX   PubMed=9272867; DOI=10.1016/s0378-1119(97)00198-4;
RA   Zhang Y.-B., Greenberg B., Lacks S.A.;
RT   "Analysis of a Streptococcus pneumoniae gene encoding signal peptidase I
RT   and overproduction of the enzyme.";
RL   Gene 194:249-255(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(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; U90721; AAB69116.1; -; Genomic_DNA.
DR   EMBL; AE005672; AAK74565.1; -; Genomic_DNA.
DR   PIR; D95046; D95046.
DR   PIR; D97917; D97917.
DR   RefSeq; WP_001820908.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; O07344; -.
DR   SMR; O07344; -.
DR   STRING; 170187.SP_0402; -.
DR   MEROPS; S26.015; -.
DR   DNASU; 930336; -.
DR   EnsemblBacteria; AAK74565; AAK74565; SP_0402.
DR   KEGG; spn:SP_0402; -.
DR   eggNOG; COG0681; Bacteria.
DR   OMA; IEPRWIP; -.
DR   PhylomeDB; O07344; -.
DR   BioCyc; SPNE170187:G1FZB-418-MON; -.
DR   Proteomes; UP000000585; 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   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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..204
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109533"
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"
FT   CONFLICT        3
FT                   /note="S -> L (in Ref. 1; AAB69116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="L -> F (in Ref. 1; AAB69116)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  23438 MW;  2B3CDCF1A070C4B9 CRC64;
     MNSFKNFLKE WGLFLLILSL LALSRIFFWS NVRVEGHSMD PTLADGEILF VVKHLPIDRF
     DIVVAHEEDG NKDIVKRVIG MPGDTIRYEN DKLYINDKET DEPYLADYIK RFKDDKLQST
     YSGKGFEGNK GTFFRSIAQK AQAFTVDVNY NTNFSFTVPE GEYLLLGDDR LVSSDSRHVG
     TFKAKDITGE AKFRLWPITR IGTF