ID   LEP_BUCAP               Reviewed;         312 AA.
AC   Q8K9R0;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Signal peptidase I;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=lepB; OrderedLocusNames=BUsg_250;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
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DR   EMBL; AE013218; AAM67809.1; -; Genomic_DNA.
DR   RefSeq; NP_660598.1; -.
DR   HSSP; P00803; 1KN9.
DR   MEROPS; S26.001; -.
DR   GeneID; 1005452; -.
DR   GenomeReviews; AE013218_GR; BUsg_250.
DR   KEGG; bas:BUsg250; -.
DR   HOGENOM; Q8K9R0; -.
DR   OMA; Q8K9R0; VAVFKYP.
DR   BioCyc; BAPH198804:BUSG250-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   InterPro; IPR019533; Peptidase_S26_cons-reg.
DR   Gene3D; G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   Pfam; PF10502; Peptidase_S26; 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    312       Signal peptidase I.
FT                                /FTId=PRO_0000109504.
FT   TRANSMEM      7     27       Potential.
FT   TOPO_DOM     28     63       Cytoplasmic (Potential).
FT   TRANSMEM     64     84       Potential.
FT   TOPO_DOM     85    312       Extracellular (Potential).
FT   ACT_SITE     88     88       By similarity.
FT   ACT_SITE    142    142       By similarity.
SQ   SEQUENCE   312 AA;  37103 MW;  63602053A16A0D8B CRC64;
     MRNILTIFLL TSTFFTGILW IIDHILLIKN YFYNKKKTKN NNTILINKVI LENKKCFFRS
     LSSLFPTFFI VFIIRSFIYE PFQIPSGSMM PTLLIGDFIL VKKFSYGIKE PITNKTIIKM
     NLPQRGDIVV FKHPKNNIDY IKRVVGLPGD KIQYDINRKK IKICINYTNQ KNCENKLFIT
     YSKPKLSNFF QKIYLLKSRT NEEEKVYNSI YFKKVEEKIN NLKHNILILD GINSKINDYY
     QQKGMPKLIW IVPKNKYFMM GDNRDNSLDS RYWGFVPEEN LLGKATKIWM SFEKKENEWP
     TGIRIKRIGN IY
//