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   16-JUN-2009, entry version 49.
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.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=785;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION IN E.COLI.
RC   STRAIN=Ethiopian AZ322;
RX   MEDLINE=22749750; PubMed=12867468;
RX   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.,
RA   Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C.,
RA   Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G.,
RA   Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with
RT   sequences of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Complements E.coli mutants temperature-sensitive for
CC       lepB function.
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II
CC       membrane protein (Potential).
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
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DR   EMBL; AF503336; AAM22228.1; -; Genomic_DNA.
DR   EMBL; AE017197; AAU03508.1; -; Genomic_DNA.
DR   RefSeq; YP_066990.1; -.
DR   HSSP; P00803; 1B12.
DR   MEROPS; S26.001; -.
DR   GeneID; 2958484; -.
DR   GenomeReviews; AE017197_GR; RT0020.
DR   KEGG; rty:RT0020; -.
DR   HOGENOM; Q8L2J7; -.
DR   OMA; Q8L2J7; KPWIESV.
DR   BioCyc; RTYP257363:RT0020-MON; -.
DR   BRENDA; 3.4.21.89; 281221.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR019759; Peptidase_S24_S26_cons-reg.
DR   InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn.
DR   Gene3D; G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00727; LEADERPTASE.
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; Complete proteome; Hydrolase;
KW   Membrane; Transmembrane.
FT   CHAIN         1    264       Signal peptidase I.
FT                                /FTId=PRO_0000316278.
FT   TOPO_DOM      1     18       Cytoplasmic (Potential).
FT   TRANSMEM     19     39       Potential.
FT   TOPO_DOM     40    264       Periplasmic (Potential).
FT   ACT_SITE     43     43       By similarity.
FT   ACT_SITE    106    106       By similarity.
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
//