ID   LEP_RICCN               Reviewed;         266 AA.
AC   Q92JB1;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 120.
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=RC0156;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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}.
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DR   EMBL; AE006914; AAL02694.1; -; Genomic_DNA.
DR   PIR; D97719; D97719.
DR   RefSeq; WP_010976832.1; NC_003103.1.
DR   AlphaFoldDB; Q92JB1; -.
DR   SMR; Q92JB1; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; AAL02694; AAL02694; RC0156.
DR   KEGG; rco:RC0156; -.
DR   PATRIC; fig|272944.4.peg.185; -.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   OMA; SDSRFWG; -.
DR   Proteomes; UP000000816; Chromosome.
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; 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; 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..266
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109515"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  31140 MW;  7C3926FECAB482FA CRC64;
     MQTDNTKSNT NKTAKQEWGS FAFVICIALL IRILIMEPFN VPTGSMKATI LENDYIFSTK
     YSYGYSNYSL SFFDFIPLFK GRIFAREPDR GDIVVFRPPN DMSVRYIKRL IGLPGDKIQL
     IDDVIYINDK KIERTEVGTY ISEEGIKYLK FKETLPNGRT YFSYKLAPIY GVIYNDRYSN
     TDVFYVPEGQ YFFLGDNRDQ SNDSRVNLGF VPFENFIAKA QFIWFSTKIT WWDNDIGVIN
     LVLKLKPWIE SVRLNRIFRN LYNTDA