LEP_HELPY
ID LEP_HELPY Reviewed; 290 AA.
AC O25300;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
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=HP_0576;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07643.1; -; Genomic_DNA.
DR PIR; H64591; H64591.
DR RefSeq; NP_207371.1; NC_000915.1.
DR RefSeq; WP_000670710.1; NC_018939.1.
DR AlphaFoldDB; O25300; -.
DR SMR; O25300; -.
DR IntAct; O25300; 2.
DR STRING; 85962.C694_02970; -.
DR PaxDb; O25300; -.
DR EnsemblBacteria; AAD07643; AAD07643; HP_0576.
DR KEGG; hpy:HP_0576; -.
DR PATRIC; fig|85962.47.peg.621; -.
DR eggNOG; COG0681; Bacteria.
DR OMA; SDSRFWG; -.
DR PhylomeDB; O25300; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..290
FT /note="Signal peptidase I"
FT /id="PRO_0000109508"
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; 33710 MW; F3DF2DFCE8465310 CRC64;
MKFLRSVYAF CSSWVGTIVI VLLVIFFIAQ AFIIPSRSMV GTLYEGDMLF VKKFSYGIPI
PKIPWIELPV MPDFKNNGHL IEGDRPKRGE VVVFIPPHEK KSYYVKRNFA IGGDEVLFTN
EGFYLHPFES DTDKNYIAKH YPNAMTKEFM GKIFVLNPYK NEHPGIHYQK DNETFHLMEQ
LATQGAEANI SMQLIQMEGE KVFYKKINDD EFFMIGDNRD NSSDSRFWGS VAYKNIVGSP
WFVYFSLSLK NSLEMDAENN PKKRYLVRWE RMFKSVGGLE KIIKKENATH