COPZ_STAA8
ID COPZ_STAA8 Reviewed; 68 AA.
AC Q2FV63;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Copper chaperone CopZ;
GN Name=copZ; OrderedLocusNames=SAOUHSC_02874;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION IN COPPER TRANSPORT, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=18048940; DOI=10.1099/mic.0.2007/009860-0;
RA Sitthisak S., Knutsson L., Webb J.W., Jayaswal R.K.;
RT "Molecular characterization of the copper transport system in
RT Staphylococcus aureus.";
RL Microbiology 153:4274-4283(2007).
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 ECO:0000269|PubMed:18048940}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Highest expression during the exponential growth
CC phase. {ECO:0000269|PubMed:18048940}.
CC -!- INDUCTION: Induced by copper and, to some extent, by ferric and lead
CC ions. {ECO:0000269|PubMed:18048940}.
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DR EMBL; CP000253; ABD31872.1; -; Genomic_DNA.
DR RefSeq; WP_000076661.1; NZ_LS483365.1.
DR RefSeq; YP_501329.1; NC_007795.1.
DR PDB; 6FF2; X-ray; 1.30 A; A/B=1-68.
DR PDBsum; 6FF2; -.
DR AlphaFoldDB; Q2FV63; -.
DR SMR; Q2FV63; -.
DR STRING; 1280.SAXN108_2809; -.
DR EnsemblBacteria; ABD31872; ABD31872; SAOUHSC_02874.
DR GeneID; 3921545; -.
DR KEGG; sao:SAOUHSC_02874; -.
DR PATRIC; fig|93061.5.peg.2598; -.
DR eggNOG; COG2608; Bacteria.
DR HOGENOM; CLU_134973_10_4_9; -.
DR OMA; NHCKMTV; -.
DR PRO; PR:Q2FV63; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Copper; Cytoplasm; Metal-binding;
KW Reference proteome.
FT CHAIN 1..68
FT /note="Copper chaperone CopZ"
FT /id="PRO_0000351280"
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"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6FF2"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:6FF2"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:6FF2"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6FF2"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:6FF2"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6FF2"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:6FF2"
SQ SEQUENCE 68 AA; 7237 MW; D8DC0D1349C1BF3C CRC64;
MSQEILNVEG MSCGHCKSAV ESALNNIDGV TSADVNLENG QVSVQYDDSK VAVSQMKDAI
EDQGYDVV
