ID   LEP_STAAU               Reviewed;         191 AA.
AC   P0A070; P72365;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
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;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCUH29 / NCIMB 40771;
RX   PubMed=8824617; DOI=10.1128/jb.178.19.5712-5718.1996;
RA   Cregg K.M., Wilding E.I., Black M.T.;
RT   "Molecular cloning and expression of the spsB gene encoding an essential
RT   type I signal peptidase from Staphylococcus aureus.";
RL   J. Bacteriol. 178:5712-5718(1996).
CC   -!- FUNCTION: Essential for cell viability.
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; U65000; AAC44435.1; -; Genomic_DNA.
DR   RefSeq; WP_000711896.1; NZ_WYDB01000003.1.
DR   AlphaFoldDB; P0A070; -.
DR   SMR; P0A070; -.
DR   BindingDB; P0A070; -.
DR   ChEMBL; CHEMBL2429707; -.
DR   MEROPS; S26.016; -.
DR   OMA; IEPRWIP; -.
DR   BRENDA; 3.4.21.89; 3352.
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_0000109532"
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