ID   Y242_HELPJ              Reviewed;         350 AA.
AC   Q9ZMH8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Putative zinc metalloprotease jhp_0242;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=jhp_0242;
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD05832.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE001439; AAD05832.1; ALT_INIT; Genomic_DNA.
DR   PIR; D71955; D71955.
DR   AlphaFoldDB; Q9ZMH8; -.
DR   SMR; Q9ZMH8; -.
DR   STRING; 85963.jhp_0242; -.
DR   PRIDE; Q9ZMH8; -.
DR   EnsemblBacteria; AAD05832; AAD05832; jhp_0242.
DR   KEGG; hpj:jhp_0242; -.
DR   eggNOG; COG0750; Bacteria.
DR   OMA; QYMVGFG; -.
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: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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..350
FT                   /note="Putative zinc metalloprotease jhp_0242"
FT                   /id="PRO_0000088444"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          108..177
FT                   /note="PDZ"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   350 AA;  38864 MW;  99DCA574282D6AF9 CRC64;
     MFIVAVLMLA FLIFVHELGH FIIARICGVK VEVFSIGFGK KLWFFKLFGT QFALSLIPLG
     GYVKLKGMDK EENEENKINQ ANDSYAQKSP FQKLWILFGG AFFNFLFAVL VYFFLALSGE
     KVLLPVIGGL EKNALEAGLL KGDRILSINH QKIASFREIR EIVARSQGEL ILEIERNNQI
     LEKRLTPKIV AVISESNDPN EIIKYKIIGI KPDMQKMGVV SYSVFQAFEK ALSRFKEGVV
     LIVDSLRRLI MGSASVKELS GVIGIVGALS HANSVSMLLL FGAFLSINLG ILNLLPIPAL
     DGAQMLGVVF KNIFHIALPT PIQNALWLVG VGFLVFVMFL GLFNDITRLL