ID   COPP_HELFC              Reviewed;          66 AA.
AC   O32620; E7A9G7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=COP-associated protein;
DE   AltName: Full=Copper ion-binding protein;
GN   Name=copP; OrderedLocusNames=Hfelis_12600;
OS   Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=936155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RX   PubMed=9440521; DOI=10.1128/jb.180.2.317-329.1998;
RA   Bayle D., Waengler S., Weitzenegger T., Steinhilber W., Volz J.,
RA   Przybylski M., Schaefer K.P., Sachs G., Melchers K.;
RT   "Properties of the P-type ATPases encoded by the copAP operons of
RT   Helicobacter pylori and Helicobacter felis.";
RL   J. Bacteriol. 180:317-329(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49179 / NCTC 12436 / CS1;
RA   Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M.,
RA   Muller A.;
RT   "Comparative whole genome analysis of the carcinogenic bacterial pathogen
RT   Helicobacter felis.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a cation-transporting system which is associated with
CC       copper export out of the H.pylori cells.
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DR   EMBL; AJ001932; CAA05105.1; -; Genomic_DNA.
DR   EMBL; FQ670179; CBY83344.1; -; Genomic_DNA.
DR   PIR; T47270; T47270.
DR   RefSeq; WP_013469708.1; NC_014810.2.
DR   AlphaFoldDB; O32620; -.
DR   SMR; O32620; -.
DR   STRING; 936155.HFELIS_12600; -.
DR   EnsemblBacteria; CBY83344; CBY83344; HFELIS_12600.
DR   GeneID; 36134465; -.
DR   KEGG; hfe:HFELIS_12600; -.
DR   eggNOG; COG2608; Bacteria.
DR   HOGENOM; CLU_134973_6_2_7; -.
DR   OMA; MKVTFQV; -.
DR   OrthoDB; 2061355at2; -.
DR   Proteomes; UP000007934; 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   4: Predicted;
KW   Copper; Metal-binding.
FT   CHAIN           1..66
FT                   /note="COP-associated protein"
FT                   /id="PRO_0000079244"
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"
SQ   SEQUENCE   66 AA;  7116 MW;  0F1FDEC94F07AA72 CRC64;
     MKIDIPVKGM TCQHCVDKIE KFVGELEGVS YIGVDLDKQS VQVEFSAPAS AEAIEEAILD
     AGYELG