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Database: UniProt
Entry: P42668
LinkDB: P42668
Original site: P42668 
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   01-OCT-2014, entry version 86.
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 / NCTC 6346 / IMET 11025;
RA   Hoang V., Birger A., Hofemeister J.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type II 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   ProteinModelPortal; P42668; -.
DR   MEROPS; S26.004; -.
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:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   Gene3D; 2.10.109.10; -; 2.
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; IPR028360; Peptidase_S24/S26_b-rbn.
DR   InterPro; IPR019759; Peptidase_S24_S26.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   PANTHER; PTHR12383; PTHR12383; 1.
DR   Pfam; PF00717; Peptidase_S24; 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       Signal peptidase I.
FT                                /FTId=PRO_0000109496.
FT   TOPO_DOM      1     19       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     20     40       Helical. {ECO:0000255}.
FT   TOPO_DOM     41    186       Extracellular. {ECO:0000255}.
FT   ACT_SITE     44     44       {ECO:0000250}.
FT   ACT_SITE     86     86       {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
//
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