ID   LEP_BACLI               Reviewed;         186 AA.
AC   P42668;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 119.
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=sip;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9789 / DSM 8785 / NBRC 12195 / NCIMB 6346 / NCTC 6346 / IMET
RC   11025 / NRS 243;
RA   Hoang V., Birger A., Hofemeister J.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
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; X75604; CAA53272.1; -; Genomic_DNA.
DR   RefSeq; WP_003181363.1; NZ_UAQA01000001.1.
DR   AlphaFoldDB; P42668; -.
DR   SMR; P42668; -.
DR   MEROPS; S26.004; -.
DR   GeneID; 66216329; -.
DR   PATRIC; fig|1402.62.peg.3752; -.
DR   OMA; IEPRWIP; -.
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   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   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.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..186
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109496"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   186 AA;  21145 MW;  F8F82EB84F8BF5B8 CRC64;
     MTEEKSTNKK NSLFEWVKAI IIAVVLALLI RAFLFEPYLV EGTSMDPTLH DGERLFVYKT
     VRYVGEFKRG DIVIIDGDEK NVHYVKRLIG LPGDTVQMKD DTLYINGKKV SEPYLSENRK
     EAEAVGVKLT GDFGPVKVPE GKYFVMGDNR QRSMDSRNGL GLIDKKRVAG TSQFVFFPFN
     EIRKTD