ID   LEP2_BACAM              Reviewed;         193 AA.
AC   P41025;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Signal peptidase I;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=sipS2; Synonyms=sip;
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23844 / P;
RX   PubMed=7578273; DOI=10.1016/0167-4889(95)00101-w;
RA   Hoang V., Hofemeister J.;
RT   "Bacillus amyloliquefaciens possesses a second type I signal peptidase with
RT   extensive sequence similarity to other Bacillus SPases.";
RL   Biochim. Biophys. Acta 1269:64-68(1995).
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; Z33640; CAA83921.1; -; Genomic_DNA.
DR   PIR; S59966; S45022.
DR   RefSeq; WP_003154568.1; NZ_WOYD01000001.1.
DR   AlphaFoldDB; P41025; -.
DR   SMR; P41025; -.
DR   STRING; 692420.BAMF_1515; -.
DR   MEROPS; S26.004; -.
DR   GeneID; 66326573; -.
DR   eggNOG; COG0681; Bacteria.
DR   OMA; ACDAYIK; -.
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..193
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109494"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  21860 MW;  399D7EB879A0C7C4 CRC64;
     MTEEQKPTSE KSVKRKSNTY WEWGKAIIIA VALALLIRHF LFEPYLVEGS SMYPTLHDGE
     RLFVNKSVNY IGEIERGDIV IINGDTSKVH YVKRLIGKPG ETVEMKNDTL YINGKKIAEP
     YLASNKKEAK KLGVNLTGDF GPVKVPKGKY FVMGDNRLNS MDSRNGLGLI AENRIVGTSK
     FVFFPFHDMR QTK