ID   LEP_RICM5               Reviewed;         266 AA.
AC   A8F0M1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 84.
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=RMA_0163;
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5;
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria: evidence
RT   from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(2007).
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 inner membrane {ECO:0000305}; Single-pass
CC       type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV84457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000683; ABV84457.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041404492.1; NC_009900.1.
DR   AlphaFoldDB; A8F0M1; -.
DR   SMR; A8F0M1; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; ABV84457; ABV84457; RMA_0163.
DR   KEGG; rms:RMA_0163; -.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   OMA; SDSRFWG; -.
DR   Proteomes; UP000001311; 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 inner membrane; Cell membrane; Hydrolase; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..266
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000316276"
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="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  31190 MW;  CE46F86BB5907FF1 CRC64;
     MQTDNTKSNT NKTAKQEWGS FVFVICIALL IRILIMEPFT VPTGSMKATI LENDYIFSTK
     YSYGYSNYSL SFFDFIPLFK GRIFAREPER GDIVVFRPPH DMSVRYIKRL IGLPGDKIQL
     IDDVIYINDK KIERTEVGTY ISEEGIKYLK FKETLPNGRT YFSYKLAPIY GVIYNDRYGN
     TDVFYVPEGK YFFLGDNRDQ SNDSRVNLGF VPFENFIAKA QFIWFSTKIT WWDNDIGVIN
     LVLKLKPWIE SVRLNRIFRN LYNTDV