COPP_HELPY
ID COPP_HELPY Reviewed; 66 AA.
AC Q48271; O07682; Q48257;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=COP-associated protein;
DE AltName: Full=Copper ion-binding protein;
GN Name=copP; OrderedLocusNames=HP_1073;
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].
RC STRAIN=A68;
RX PubMed=8550601; DOI=10.1074/jbc.271.1.446;
RA Melchers K., Weitzenegger T., Buhmann A., Steinhilber W., Sachs G.,
RA Schaefer K.P.;
RT "Cloning and membrane topology of a P type ATPase from Helicobacter
RT pylori.";
RL J. Biol. Chem. 271:446-457(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RX PubMed=7752900; DOI=10.1111/j.1365-2958.1995.tb02224.x;
RA Ge Z., Hiratsuka K., Taylor D.E.;
RT "Nucleotide sequence and mutational analysis indicate that two Helicobacter
RT pylori genes encode a P-type ATPase and a cation-binding protein associated
RT with copper transport.";
RL Mol. Microbiol. 15:97-106(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9244252; DOI=10.1128/jb.179.15.4676-4683.1997;
RA Beier D., Spohn G., Rappuoli R., Scarlato V.;
RT "Identification and characterization of an operon of Helicobacter pylori
RT that is involved in motility and stress adaptation.";
RL J. Bacteriol. 179:4676-4683(1997).
RN [4]
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).
RN [5]
RP STRUCTURE BY NMR IN COMPLEX WITH COPPER IONS, AND DISULFIDE BOND.
RX PubMed=18214986; DOI=10.1002/prot.21957;
RA Park S.J., Jung Y.-S., Kim J.-S., Seo M.-D., Lee B.J.;
RT "Structural insight into the distinct properties of copper transport by the
RT Helicobacter pylori CopP protein.";
RL Proteins 71:1007-1019(2008).
CC -!- FUNCTION: Part of a cation-transporting system which is associated with
CC copper export out of the H.pylori cells.
CC -!- INTERACTION:
CC Q48271; P56039: rplN; NbExp=3; IntAct=EBI-7497456, EBI-7497678;
CC -!- MISCELLANEOUS: Copper (2+) binding can oxidyze the Cys residues at the
CC metal-binding site, leading to the formation of a disulfide bond.
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DR EMBL; U59625; AAB05476.1; -; Genomic_DNA.
DR EMBL; U97567; AAB66381.1; -; Genomic_DNA.
DR EMBL; L33259; AAB67321.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD08120.1; -; Genomic_DNA.
DR PIR; A64654; A64654.
DR RefSeq; NP_207864.1; NC_000915.1.
DR RefSeq; WP_000648265.1; NC_018939.1.
DR PDB; 1YG0; NMR; -; A=1-66.
DR PDBsum; 1YG0; -.
DR AlphaFoldDB; Q48271; -.
DR SMR; Q48271; -.
DR DIP; DIP-3638N; -.
DR IntAct; Q48271; 4.
DR MINT; Q48271; -.
DR STRING; 85962.C694_05545; -.
DR PaxDb; Q48271; -.
DR EnsemblBacteria; AAD08120; AAD08120; HP_1073.
DR KEGG; hpy:HP_1073; -.
DR PATRIC; fig|85962.47.peg.1152; -.
DR eggNOG; COG2608; Bacteria.
DR OMA; MKVTFQV; -.
DR EvolutionaryTrace; Q48271; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006825; P:copper ion transport; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR InterPro; IPR000428; Cu-bd.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR Pfam; PF00403; HMA; 1.
DR PRINTS; PR00944; CUEXPORT.
DR SUPFAM; SSF55008; SSF55008; 1.
DR TIGRFAMs; TIGR00003; TIGR00003; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Disulfide bond; Metal-binding; Reference proteome.
FT CHAIN 1..66
FT /note="COP-associated protein"
FT /id="PRO_0000079246"
FT DOMAIN 1..66
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 12
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 15
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DISULFID 12..15
FT /note="Alternate"
FT /evidence="ECO:0000269|PubMed:18214986"
FT VARIANT 3
FT /note="A -> V (in strain: A68, NCTC 11638 and NCTC 11639)"
FT VARIANT 13
FT /note="N -> D (in strain: NCTC 11638)"
FT VARIANT 13
FT /note="N -> S (in strain: NCTC 11639)"
FT VARIANT 34
FT /note="V -> A (in strain: A68, NCTC 11638 and NCTC 11639)"
FT VARIANT 35
FT /note="S -> N (in strain: NCTC 11639)"
FT VARIANT 66
FT /note="V -> I (in strain: A68, NCTC 11638 and NCTC 11639)"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1YG0"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1YG0"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:1YG0"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1YG0"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1YG0"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:1YG0"
SQ SEQUENCE 66 AA; 7196 MW; 353E2C3D392816F1 CRC64;
MKATFQVPSI TCNHCVDKIE KFVGEIEGVS FIDVSVEKKS VVVEFDAPAT QDLIKEALLD
AGQEVV
