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COPZ_STAES
ID   COPZ_STAES              Reviewed;          68 AA.
AC   Q8CN01;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Copper chaperone CopZ;
GN   Name=copZ; OrderedLocusNames=SE_2120;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Chaperone that serves for the intracellular sequestration and
CC       transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type
CC       ATPase A (CopA) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AE015929; AAO05762.1; -; Genomic_DNA.
DR   RefSeq; NP_765675.1; NC_004461.1.
DR   RefSeq; WP_001832344.1; NZ_WBME01000013.1.
DR   AlphaFoldDB; Q8CN01; -.
DR   SMR; Q8CN01; -.
DR   STRING; 176280.SE_2120; -.
DR   EnsemblBacteria; AAO05762; AAO05762; SE_2120.
DR   GeneID; 50017798; -.
DR   KEGG; sep:SE_2120; -.
DR   PATRIC; fig|176280.10.peg.2071; -.
DR   eggNOG; COG2608; Bacteria.
DR   HOGENOM; CLU_134973_10_4_9; -.
DR   OMA; NHCKMTV; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Chaperone; Copper; Cytoplasm; Metal-binding.
FT   CHAIN           1..68
FT                   /note="Copper chaperone CopZ"
FT                   /id="PRO_0000351284"
FT   DOMAIN          2..68
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         13
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         16
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ   SEQUENCE   68 AA;  7661 MW;  F2BE2AC6992E36AA CRC64;
     MTQKIIKVEG MSCEHCRNAV ESALAKLNGV SSAEVNLDEN HVRVEYNDSK VTFENMKEAI
     EEQGYDVK
 
 
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