COPZ_STAAN
ID COPZ_STAAN Reviewed; 68 AA.
AC Q7A3E5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Copper chaperone CopZ;
GN Name=copZ; OrderedLocusNames=SA2345;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB43649.1; -; Genomic_DNA.
DR PIR; G90060; G90060.
DR RefSeq; WP_000076661.1; NC_002745.2.
DR AlphaFoldDB; Q7A3E5; -.
DR SMR; Q7A3E5; -.
DR EnsemblBacteria; BAB43649; BAB43649; BAB43649.
DR KEGG; sau:SA2345; -.
DR HOGENOM; CLU_134973_10_4_9; -.
DR OMA; NHCKMTV; -.
DR Proteomes; UP000000751; 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 Chaperone; Copper; Cytoplasm; Metal-binding.
FT CHAIN 1..68
FT /note="Copper chaperone CopZ"
FT /id="PRO_0000351279"
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