ID   LEPQ_BACNA              Reviewed;         185 AA.
AC   Q57350;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Signal peptidase I P;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=sipP; Synonyms=sipP40;
OS   Bacillus subtilis subsp. natto.
OG   Plasmid pTA1040.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=86029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAM 1232;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U32378; AAC44409.1; -; Genomic_DNA.
DR   PIR; I40552; I40552.
DR   RefSeq; NP_053777.1; NC_001764.1.
DR   AlphaFoldDB; Q57350; -.
DR   SMR; Q57350; -.
DR   MEROPS; S26.007; -.
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; Plasmid; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..185
FT                   /note="Signal peptidase I P"
FT                   /id="PRO_0000109498"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  21568 MW;  D501657FEF6C7C49 CRC64;
     MFDKEKRKKS NIIDWIKAIL IALILVFLVR TFLFEPYIVQ GESMKPTLFN SERLFVNKFV
     KYTGDFKRGD IVVLNGEEKK THYVKRLIGL PGDTIEMKND NLFVNGKRFN EEYLKENKKD
     AHDSDLNLTG DFGPIKVPKD KYFVMGDNRQ NSMDSRNGLG LFNKKDIVGV EELVFFPLDR
     IRHAK