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Database: UniProt
Entry: P0A067
LinkDB: P0A067
Original site: P0A067 
ID   LEP_STAAM               Reviewed;         191 AA.
AC   P0A067; P72365;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   09-JUL-2014, entry version 70.
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=SAV0965;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB57127.1; -; Genomic_DNA.
DR   RefSeq; NP_371489.1; NC_002758.2.
DR   ProteinModelPortal; P0A067; -.
DR   SMR; P0A067; 25-179.
DR   STRING; 158878.SAV0965; -.
DR   DNASU; 1120940; -.
DR   EnsemblBacteria; BAB57127; BAB57127; SAV0965.
DR   GeneID; 1120940; -.
DR   KEGG; sav:SAV0965; -.
DR   PATRIC; 19562621; VBIStaAur52173_0991.
DR   eggNOG; COG0681; -.
DR   HOGENOM; HOG000003673; -.
DR   KO; K03100; -.
DR   OMA; PLAETHI; -.
DR   OrthoDB; EOG622PW8; -.
DR   PhylomeDB; P0A067; -.
DR   BioCyc; SAUR158878:GJJ5-983-MONOMER; -.
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:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   Gene3D; 2.10.109.10; -; 2.
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; IPR028360; Peptidase_S24/S26_b-rbn.
DR   InterPro; IPR019759; Peptidase_S24_S26.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   PANTHER; PTHR12383; PTHR12383; 1.
DR   Pfam; PF00717; Peptidase_S24; 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; Complete proteome; Hydrolase; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    191       Signal peptidase IB.
FT                                /FTId=PRO_0000109527.
FT   TOPO_DOM      1      7       Cytoplasmic (Potential).
FT   TRANSMEM      8     28       Helical; (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
//
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