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 01-MAY-2013, entry version 65.
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; ITGSFET; -.
DR ProtClustDB; CLSK885033; -.
DR BioCyc; SAUR158878:GJJ5-983-MONOMER; -.
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:UniProtKB-KW.
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; IPR019759; Peptidase_S24_S26.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn.
DR PANTHER; PTHR12383; PTHR12383; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; Pept_S24_S26_C; 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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