ID   HPN_HELPY               Reviewed;          60 AA.
AC   P0A0V6; Q48251;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Histidine-rich metal-binding polypeptide;
GN   Name=hpn; OrderedLocusNames=HP_1427;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19 AND 48-60.
RC   STRAIN=LEU;
RX   PubMed=7790085; DOI=10.1128/iai.63.7.2682-2688.1995;
RA   Gilbert J.V., Ramakrishna J., Sunderman F.W. Jr., Wright A., Plaut A.G.;
RT   "Protein Hpn: cloning and characterization of a histidine-rich metal-
RT   binding polypeptide in Helicobacter pylori and Helicobacter mustelae.";
RL   Infect. Immun. 63:2682-2688(1995).
RN   [2]
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   -!- FUNCTION: Strongly binds nickel and zinc. Binds other metals less
CC       strongly: cobalt > copper > cadmium > manganese. May act to increase,
CC       or at least to preserve, urease activity. Exact function is still
CC       unknown.
CC   -!- INTERACTION:
CC       P0A0V6; O25772: HP_1157; NbExp=3; IntAct=EBI-7512037, EBI-7500169;
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DR   EMBL; U26361; AAA85859.1; -; Genomic_DNA.
DR   EMBL; AE000511; AAD08471.1; -; Genomic_DNA.
DR   PIR; C64698; C64698.
DR   AlphaFoldDB; P0A0V6; -.
DR   IntAct; P0A0V6; 16.
DR   MINT; P0A0V6; -.
DR   PaxDb; P0A0V6; -.
DR   EnsemblBacteria; AAD08471; AAD08471; HP_1427.
DR   KEGG; hpy:HP_1427; -.
DR   OMA; HYHSHCH; -.
DR   PHI-base; PHI:5425; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; Nickel; Reference proteome;
KW   Repeat; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7790085"
FT   CHAIN           2..60
FT                   /note="Histidine-rich metal-binding polypeptide"
FT                   /id="PRO_0000084044"
FT   REPEAT          38..42
FT                   /note="1"
FT   REPEAT          51..55
FT                   /note="2"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..55
FT                   /note="2 X 5 AA repeats of E-E-G-C-C"
FT   COMPBIAS        8..31
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   60 AA;  7077 MW;  C3AEE3BB4FECDA71 CRC64;
     MAHHEEQHGG HHHHHHHTHH HHYHGGEHHH HHHSSHHEEG CCSTSDSHHQ EEGCCHGHHE