ID LEP_RICB8 Reviewed; 289 AA.
AC A8GYE1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=A1I_01370;
OS Rickettsia bellii (strain OSU 85-389).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=391896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU 85-389;
RA Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT "Complete genome sequencing of Rickettsia bellii.";
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}.
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DR EMBL; CP000849; ABV78666.1; -; Genomic_DNA.
DR AlphaFoldDB; A8GYE1; -.
DR SMR; A8GYE1; -.
DR MEROPS; S26.001; -.
DR KEGG; rbo:A1I_01370; -.
DR HOGENOM; CLU_028723_1_2_5; -.
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 Gene3D; 2.10.109.10; Umud Fragment, subunit A; 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 NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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..289
FT /note="Signal peptidase I"
FT /id="PRO_0000316272"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..289
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 68
FT /evidence="ECO:0000250"
FT ACT_SITE 131
FT /evidence="ECO:0000250"
SQ SEQUENCE 289 AA; 33889 MW; F8A30C279F34650F CRC64;
MKKLTSTTTT LWDNKLFINN LKNFMQTNTE SNNNKTTAQE WKSFILVVVI ALMIRILIIE
SFVVPTGSMK ATILENDRIF GTKYSYGYSN YSLSFFDFIH LFKGRIFART PERGDIIIFR
PPHEMNTRYI KRLIGLPGDK VQLIDDVIYI NDEKIERVES GIYVSEEGRK YLKFKETLPN
GKTYFSYKLA PVLGIMFNDK YGNTDAFYVP EGEYFFLGDN RDQSNDSRID LGFVPFENFI
AKAQFIWFST KITWWDSDIG VINLILKLKP WAESIRFNRI FRNLYSIED
//
