ID   HAP_HELPX               Reviewed;         256 AA.
AC   Q48259;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Zinc metalloprotease;
DE            EC=3.4.24.-;
DE   Flags: Fragment;
GN   Name=hap;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX   PubMed=7984089; DOI=10.1111/j.1365-2958.1994.tb00410.x;
RA   Smith A.W., Chahal B., French G.L.;
RT   "The human gastric pathogen Helicobacter pylori has a gene encoding an
RT   enzyme first classified as a mucinase in Vibrio cholerae.";
RL   Mol. Microbiol. 13:153-160(1994).
CC   -!- FUNCTION: May play a role in ulcer formation. Proteolytic digestion of
CC       gastric mucus has been suggested as an important mechanism by which its
CC       pathogenicity is at least partly exerted.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; Z27239; CAA81753.1; -; Genomic_DNA.
DR   PIR; S54406; S54406.
DR   AlphaFoldDB; Q48259; -.
DR   SMR; Q48259; -.
DR   MEROPS; M04.003; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   Pfam; PF04151; PPC; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
PE   3: Inferred from homology;
KW   Calcium; Hydrolase; Metalloprotease; Protease; Secreted; Zinc.
FT   CHAIN           <1..256
FT                   /note="Zinc metalloprotease"
FT                   /id="PRO_0000078175"
FT   ACT_SITE        74
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   NON_TER         1
SQ   SEQUENCE   256 AA;  27276 MW;  F3552513B7BA5456 CRC64;
     NSGLVYRDMS GGINEAFSDI AGEAAEYFMR GNVDWIVGAD IFKSSGGLRY FDQPSRDGRS
     IDHASQYYSG IDVHSSGVFN RAFYLLANKS GWNVRKGFEV FAVANQLYWT PNSTFDQGGC
     GVVKAAQDLN YNTADVVAAF NTVGVNASCG TTPPPVGKVL EKGKPITGLS GSRGGEDFYT
     FTVTNSGSVV VSISGGTGDA DLYVKAGSKP TTSSWDCRPY RSGNAEQCSI SAVVGTTYHV
     MLRGYSNYSG VTLRLD