ID   LEP_STAAW               Reviewed;         191 AA.
AC   P0A069; P72365;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=MW0847;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Essential for cell viability (By similarity).
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
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DR   EMBL; BA000033; BAB94712.1; -; Genomic_DNA.
DR   RefSeq; NP_645664.1; -.
DR   HSSP; P00803; 1B12.
DR   MEROPS; S26.016; -.
DR   GeneID; 1002959; -.
DR   GenomeReviews; BA000033_GR; MW0847.
DR   KEGG; sam:MW0847; -.
DR   HOGENOM; P0A069; -.
DR   OMA; P0A069; LAETHIT.
DR   BioCyc; SAUR196620:MW0847-MON; -.
DR   GO; GO:0016021; C:integral to 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   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR019759; Peptidase_S24_S26_cons-reg.
DR   InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn.
DR   Gene3D; G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00727; LEADERPTASE.
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; Complete proteome; Hydrolase; Membrane; Protease;
KW   Transmembrane.
FT   CHAIN         1    191       Signal peptidase IB.
FT                                /FTId=PRO_0000109531.
FT   TOPO_DOM      1      7       Cytoplasmic (Potential).
FT   TRANSMEM      8     28       Potential.
FT   TOPO_DOM     29    191       Extracellular (Potential).
FT   ACT_SITE     36     36       By similarity.
FT   ACT_SITE     77     77       By similarity.
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
//