ID   LEP_RICAH               Reviewed;         266 AA.
AC   A8GM78;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=A1C_00865;
OS   Rickettsia akari (strain Hartford).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=293614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hartford;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia akari.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000847; ABV74503.1; -; Genomic_DNA.
DR   RefSeq; WP_012013373.1; NC_009881.1.
DR   AlphaFoldDB; A8GM78; -.
DR   SMR; A8GM78; -.
DR   STRING; 293614.A1C_00865; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; ABV74503; ABV74503; A1C_00865.
DR   KEGG; rak:A1C_00865; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   OMA; SDSRFWG; -.
DR   Proteomes; UP000006830; 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_0000316271"
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;  31328 MW;  8EA822E12B01BF70 CRC64;
     MQTDNTKSNT NKTAKQEWWS CAFVICIALL IRILIMEPFT VPTGSMKATI LENDYIFSTK
     YSYGYSNYSL SFFDFIPLFK GRIFAREPER GDIVVFRPPN DMNVRYIKRL IGLPGDKIQL
     IDDVIYINDK KIERTEVGTY TSEDGIKYLK FKETLPNGRT YFSYKLAPIF SVIYNDRYGN
     TDVFYVPEGK YFFLGDNRDQ SNDSRVNLGF VPFENFIAKA QFIWFSTKIN WWDNDIGVMN
     LVLRLKPWIE SVRLNRIFRN LYNTDE