ID   LEP_HELPJ               Reviewed;         290 AA.
AC   Q9ZLQ5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 132.
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=jhp_0523;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD06104.1; -; Genomic_DNA.
DR   PIR; D71921; D71921.
DR   RefSeq; WP_000670646.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZLQ5; -.
DR   STRING; 85963.jhp_0523; -.
DR   EnsemblBacteria; AAD06104; AAD06104; jhp_0523.
DR   KEGG; hpj:jhp_0523; -.
DR   PATRIC; fig|85963.30.peg.471; -.
DR   eggNOG; COG0681; Bacteria.
DR   OMA; SDSRFWG; -.
DR   Proteomes; UP000000804; 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; 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; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..290
FT                   /note="Signal peptidase I"
FT                   /id="PRO_0000109509"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   290 AA;  33726 MW;  0276F02BCB189D3D CRC64;
     MKFLRSVYAF CSSWVGTIII VLLVIFFIAQ AFIIPSRSMV GTLYEGDMLF VKKFSYGIPI
     PKIPWIELPV MPDFKNNGHL IEGDRPKRGE VVVFIPPHEK KSYYVKRNFA IGGDEVLFTN
     EGFYLHPFES GNDKDYISKH YPNALTKEFM GKIFVLNPYK SKHPGIHYQK DNETFHLMEQ
     LATQGAEANI SMQLIQMEGE KVFYKKINHD EFFMIGDNRD NSSDSRFWGS VAYKNIVGSP
     WFVYFSLSLK NSLEVDAENN PKKRYLVRWE RMFKSVEGLE KIIKKEKATH