ID   LEP_RICCK               Reviewed;         265 AA.
AC   A8EXI2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=A1E_00585;
OS   Rickettsia canadensis (strain McKiel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=293613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=McKiel;
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 canadensis.";
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}.
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; CP000409; ABV73065.1; -; Genomic_DNA.
DR   RefSeq; WP_012148266.1; NC_009879.1.
DR   AlphaFoldDB; A8EXI2; -.
DR   SMR; A8EXI2; -.
DR   STRING; 293613.A1E_00585; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; ABV73065; ABV73065; A1E_00585.
DR   KEGG; rcm:A1E_00585; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   OMA; SDSRFWG; -.
DR   OrthoDB; 1741894at2; -.
DR   Proteomes; UP000007056; 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..265
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000316274"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..265
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  31038 MW;  EBC074D99D4DFC28 CRC64;
     MQIDTKTNTN KTTAQEWKSF AFVVCIALLI RILIMEPFTV PTGSMKATIL ENDYIFSTKY
     SYGYSNYSLS FFDFIPLFKG RIFACEPERG DIVVFRPPND MSVRYIKRLI GLPGDKIQLI
     DDIIYINDKK IERTEVGTYI SEEGRKYLKF KETLPNGRTY FSYKLAPIFG VISDDRYGNT
     DVFYVPEGKY FFLGDNRDQS NDSRVNLGFV PFENFIAKAQ FIWFSTKITW WDNDIGVINL
     ILKLKPWIES VRLNRIFRNL YNTDE