ID   LEP_STAAS               Reviewed;         191 AA.
AC   Q6GAW1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Signal peptidase IB;
DE            Short=SPase IB;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase IB;
GN   Name=spsB; OrderedLocusNames=SAS0835;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Essential for cell viability. {ECO:0000250}.
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; BX571857; CAG42610.1; -; Genomic_DNA.
DR   RefSeq; WP_000711896.1; NC_002953.3.
DR   AlphaFoldDB; Q6GAW1; -.
DR   SMR; Q6GAW1; -.
DR   MEROPS; S26.016; -.
DR   KEGG; sas:SAS0835; -.
DR   HOGENOM; CLU_028723_5_0_9; -.
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..191
FT                   /note="Signal peptidase IB"
FT                   /id="PRO_0000109530"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   191 AA;  21692 MW;  1C6BF5BB423706C0 CRC64;
     MKKELLEWII SIAVAFVILF IVGKFIVTPY TIKGESMDPT LKDGERVAVN IIGYKTGGLE
     KGNVVVFHAN KNDDYVKRVI GVPGDKVEYK NDTLYVNGKK QDEPYLNYNL KHKQGDYITG
     TFQVKDLPNA NPKSNVIPKG KYLVLGDNRE VSKDSRAFGL IDEDQIVGKV SFRFWPFSEF
     KHNFNPENTK N