ID   LEP_BACCL               Reviewed;         182 AA.
AC   P41027;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=sipC;
OS   Bacillus caldolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8801417; DOI=10.1111/j.1365-2958.1995.mmi_17040621.x;
RA   Meijer W.J.J., de Jong A., Bea G., Wisman A., Tjalsma H., Venema G.,
RA   Bron S., van Dijl J.M.;
RT   "The endogenous Bacillus subtilis (natto) plasmids pTA1015 and pTA1040
RT   contain signal peptidase-encoding genes: identification of a new structural
RT   module on cryptic plasmids.";
RL   Mol. Microbiol. 17:621-631(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; Z27457; CAA81813.1; -; Genomic_DNA.
DR   EMBL; L26257; AAA22759.1; -; Genomic_DNA.
DR   PIR; I40175; I40175.
DR   RefSeq; WP_011230183.1; NZ_CP025074.1.
DR   AlphaFoldDB; P41027; -.
DR   SMR; P41027; -.
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..182
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109495"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   182 AA;  21263 MW;  908E40A6B9A1E7F9 CRC64;
     MTKQKEKRGR RWPWFVAVCV VATLRLFVFS NYVVEGKSMM PTLESGNLLI VNKLSYDIGP
     IRRFDIIVFH ANKKEDYVKR VIGLPGDRIA YKNDILYVNG KKVDEPYLRP YKQKLLDGRL
     TGDFTLEEVT GKTRVPPGCI FVLGDNRLSS WDSRHFGFVK INQIVGKVDF RYWPFKQFAF
     QF