Y258_HELPY
ID Y258_HELPY Reviewed; 348 AA.
AC P56136;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative zinc metalloprotease HP_0258;
DE EC=3.4.24.-;
GN OrderedLocusNames=HP_0258;
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07326.1; -; Genomic_DNA.
DR PIR; B64552; B64552.
DR RefSeq; NP_207056.1; NC_000915.1.
DR RefSeq; WP_001863029.1; NC_018939.1.
DR AlphaFoldDB; P56136; -.
DR SMR; P56136; -.
DR STRING; 85962.C694_01305; -.
DR PaxDb; P56136; -.
DR EnsemblBacteria; AAD07326; AAD07326; HP_0258.
DR KEGG; hpy:HP_0258; -.
DR PATRIC; fig|85962.47.peg.278; -.
DR eggNOG; COG0750; Bacteria.
DR OMA; QYMVGFG; -.
DR PhylomeDB; P56136; -.
DR Proteomes; UP000000429; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR TIGRFAMs; TIGR00054; TIGR00054; 2.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..348
FT /note="Putative zinc metalloprotease HP_0258"
FT /id="PRO_0000088443"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 106..175
FT /note="PDZ"
FT ACT_SITE 17
FT /evidence="ECO:0000255"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 38464 MW; 3F849E05B1A92DA0 CRC64;
MFIVAVLMLA FLIFVHELGH FTIARICGVK VEVFSIGFGK KLCFFKLFGT QFALSLIPLG
GYVKLKGMDK EENGMNETTD DSYAQKSPFQ KLWILFGGAF FNFLFAILVY FFLALGGEKV
LLPVIGDLDK NALEAGLLKG DKILSINHKK IASFREIRSV VARARGELVL EIERNHQVLE
KRLTPKIVAV ISDSNDPNEM IRYKAIGIKP DMQKMGVVSY SLFQAFEKAL SRFKEGVVLI
VDSLRRLIMG SSSVKELSGV VGIVGALSHA NSLSMLLLFG AFLSINLGIL NLLPIPALDG
AQMLGVVFKN IFHITLPTPI QNALWLAGVG FLVFIMFLGL FNDLTRLL