ID LEP_RICFE Reviewed; 266 AA. AC Q4UKA7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 35. 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=RF_1177; OS Rickettsia felis (Rickettsia azadi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=42862; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000053; AAY62028.1; -; Genomic_DNA. DR RefSeq; YP_247193.1; -. DR MEROPS; S26.001; -. DR GeneID; 3401475; -. DR GenomeReviews; CP000053_GR; RF_1177. DR KEGG; rfe:RF_1177; -. DR NMPDR; fig|315456.3.peg.1177; -. DR HOGENOM; Q4UKA7; -. DR OMA; Q4UKA7; KPWIESV. DR BioCyc; RFEL315456:RF_1177-MON; -. DR BRENDA; 3.4.21.89; 297363. 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 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Transmembrane. FT CHAIN 1 266 Signal peptidase I. FT /FTId=PRO_0000316275. FT TOPO_DOM 1 20 Cytoplasmic (Potential). FT TRANSMEM 21 41 Potential. FT TOPO_DOM 42 266 Periplasmic (Potential). FT ACT_SITE 45 45 By similarity. FT ACT_SITE 108 108 By similarity. SQ SEQUENCE 266 AA; 31119 MW; D7CE673D20F67D45 CRC64; MQTDNTKSNT NKTAKQEWGS FAFVICIALL IRILIMEPFT VPTGSMKATI LENDYIFSTK YSYGYSNYSL SFFDFIPLFK GRIFAREPER GDIVVFRPPN DMNVRYIKRL IGLPGDKIQL IDDVIYINDK KIERTEVGTY ISEEGIKYLK FKETLPNGRT YFSYKLAPIF GVIYNDRYGN TDVFYVPEGK YFFLGDNRDQ SNDSRVNLGF VPFENFIAKA QFIWLSTKIT WWDNDIGVIN LVLKLKPWIE SVRLNRIFRN LYSTDE //