ID   COPZ_STAAM              Reviewed;          68 AA.
AC   Q99R79;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Copper chaperone CopZ;
GN   Name=copZ; OrderedLocusNames=SAV2558;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB58720.1; -; Genomic_DNA.
DR   RefSeq; WP_000076661.1; NC_002758.2.
DR   AlphaFoldDB; Q99R79; -.
DR   SMR; Q99R79; -.
DR   PaxDb; Q99R79; -.
DR   EnsemblBacteria; BAB58720; BAB58720; SAV2558.
DR   KEGG; sav:SAV2558; -.
DR   HOGENOM; CLU_134973_10_4_9; -.
DR   OMA; NHCKMTV; -.
DR   PhylomeDB; Q99R79; -.
DR   BioCyc; SAUR158878:SAV_RS13955-MON; -.
DR   Proteomes; UP000002481; Chromosome.
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_0000351277"
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