ID   LEP_RICPR               Reviewed;         264 AA.
AC   Q9ZE32;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 124.
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=RP116;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14585.1; -; Genomic_DNA.
DR   PIR; B71721; B71721.
DR   RefSeq; NP_220508.1; NC_000963.1.
DR   RefSeq; WP_004597149.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE32; -.
DR   SMR; Q9ZE32; -.
DR   STRING; 272947.RP116; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; CAA14585; CAA14585; CAA14585.
DR   GeneID; 57569244; -.
DR   KEGG; rpr:RP116; -.
DR   PATRIC; fig|272947.5.peg.118; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   OMA; SDSRFWG; -.
DR   Proteomes; UP000002480; 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; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..264
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109516"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..264
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   264 AA;  30870 MW;  984E888280C989FE CRC64;
     MNRDNINSNK TVKQEFGSFA FVICIALVIR ILIMEPFTVP TGSMKATILE NDYIFSTKYS
     YGYSNYSLSF FDFIHLFKGR VFAREPERGD IVVFRPPNDM SVRYIKRLIG LPGDKIQLID
     DVIYINDKKI ERTEVGTYIG EDGIKYLKFK ETLPNGRTYF SYKLAPIFGV IPSDRYSNTD
     VFYVPEGQYF FLGDNRDRSN DSRVNLGFVP FENFIAKAQF IWFSTKITWW DNDIGIINLI
     LKLKPWIESV RLSRIFKNLY NVDE