ID   COPZ_STAHJ              Reviewed;          68 AA.
AC   Q4L971;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Copper chaperone CopZ;
GN   Name=copZ; OrderedLocusNames=SH0495;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE03804.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP006716; BAE03804.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029376679.1; NC_007168.1.
DR   AlphaFoldDB; Q4L971; -.
DR   SMR; Q4L971; -.
DR   STRING; 279808.SH0495; -.
DR   EnsemblBacteria; BAE03804; BAE03804; SH0495.
DR   GeneID; 58063309; -.
DR   KEGG; sha:SH0495; -.
DR   eggNOG; COG2608; Bacteria.
DR   HOGENOM; CLU_134973_10_4_9; -.
DR   OrthoDB; 2061355at2; -.
DR   Proteomes; UP000000543; 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_0000351286"
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;  7615 MW;  8055786F51C54DED CRC64;
     MINKVINVEG MSCDHCRNAV ESALAKLNGV TSAEVDLDKN QVRVDYDENR VSVEQMKEAI
     EDQGYDVK