ID   COPZ_STAAS              Reviewed;          68 AA.
AC   Q6G6B6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Copper chaperone CopZ;
GN   Name=copZ; OrderedLocusNames=SAS2444;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG44260.1; -; Genomic_DNA.
DR   RefSeq; WP_000076661.1; NC_002953.3.
DR   AlphaFoldDB; Q6G6B6; -.
DR   SMR; Q6G6B6; -.
DR   KEGG; sas:SAS2444; -.
DR   HOGENOM; CLU_134973_10_4_9; -.
DR   OMA; NHCKMTV; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   CDD; cd00371; HMA; 1.
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   InterPro; IPR001802; MerP/CopZ.
DR   Pfam; PF00403; HMA; 1.
DR   PRINTS; PR00946; HGSCAVENGER.
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_0000351275"
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;  7237 MW;  D8DC0D1349C1BF3C CRC64;
     MSQEILNVEG MSCGHCKSAV ESALNNIDGV TSADVNLENG QVSVQYDDSK VAVSQMKDAI
     EDQGYDVV