ID   LEP_RICTY               Reviewed;         264 AA.
AC   Q8L2J7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=RT0020;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION IN E.COLI.
RC   STRAIN=Ethiopian AZ322;
RX   PubMed=12867468; DOI=10.1128/jb.185.15.4578-4584.2003;
RA   Rahman M.S., Simser J.A., Macaluso K.R., Azad A.F.;
RT   "Molecular and functional analysis of the lepB gene, encoding a type I
RT   signal peptidase from Rickettsia rickettsii and Rickettsia typhi.";
RL   J. Bacteriol. 185:4578-4584(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Complements E.coli mutants temperature-sensitive for LepB
CC       function.
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; AF503336; AAM22228.1; -; Genomic_DNA.
DR   EMBL; AE017197; AAU03508.1; -; Genomic_DNA.
DR   RefSeq; WP_011190495.1; NC_006142.1.
DR   AlphaFoldDB; Q8L2J7; -.
DR   SMR; Q8L2J7; -.
DR   STRING; 257363.RT0020; -.
DR   MEROPS; S26.001; -.
DR   EnsemblBacteria; AAU03508; AAU03508; RT0020.
DR   KEGG; rty:RT0020; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   OMA; SDSRFWG; -.
DR   OrthoDB; 1741894at2; -.
DR   Proteomes; UP000000604; 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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..264
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000316278"
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="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   264 AA;  30849 MW;  E35E28BD4585A002 CRC64;
     MNRDNTKTNK TVKQEFASFT FVICIALVIR ILIMEPFTVP TGSMKATILE NDYIFSTKYS
     YGYSNYSLSF FDFIPLFKGR VFAREPERGD IVVFRPPNDM SVRYIKRLIG LPGDKIQLID
     DVIYINDKKI ERTEVGTYIG EDGIKYLKFK ETLPNGRTYF SYKLAPIFGI ISNDRYSNTG
     VFYVPEGQYF FLGDNRDRSN DSRVNLGFVP FENFIGKAQF IWFSTKITWW DNDIGIINLI
     LKLKPWIESV RLSRIFKNLY NVDE