COPZ_ARCFU
ID COPZ_ARCFU Reviewed; 204 AA.
AC O29901;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Copper chaperone CopZ;
GN Name=copZ; OrderedLocusNames=AF_0346;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION IN COPPER DELIVERY, AND SUBUNIT.
RX PubMed=18417453; DOI=10.1073/pnas.0711446105;
RA Gonzalez-Guerrero M., Arguello J.M.;
RT "Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly
RT transfer Cu+ to transmembrane transport sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5992-5997(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 1-130, FUNCTION, COFACTOR,
RP SUBUNIT, AND MUTAGENESIS OF CYS-75; CYS-77; CYS-109; CYS-118 AND CYS-119.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=17609202; DOI=10.1074/jbc.m703311200;
RA Sazinsky M.H., LeMoine B., Orofino M., Davydov R., Bencze K.Z.,
RA Stemmler T.L., Hoffman B.M., Arguello J.M., Rosenzweig A.C.;
RT "Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper
RT chaperone from Archaeoglobus fulgidus.";
RL J. Biol. Chem. 282:25950-25959(2007).
CC -!- FUNCTION: Chaperone that serves for the intracellular sequestration and
CC transport of Cu(+). Delivers Cu(+) directly to the transmembrane
CC transport sites of copper-exporting P-type ATPase A (CopA). Probably
CC has a redox function due to the presence of a 2Fe-2S cluster and could
CC reduce Cu(2+) to Cu(+). {ECO:0000269|PubMed:17609202,
CC ECO:0000269|PubMed:18417453}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:17609202};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:17609202};
CC -!- SUBUNIT: Homodimer or homooligomer in the presence of copper ions (By
CC similarity). Monomer in the absence of copper. Interacts with CopA
CC probably in its Cu(+)-bound form. {ECO:0000250,
CC ECO:0000269|PubMed:17609202, ECO:0000269|PubMed:18417453}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; AE000782; AAB90886.1; -; Genomic_DNA.
DR PIR; B69293; B69293.
DR RefSeq; WP_010877853.1; NC_000917.1.
DR PDB; 2HU9; X-ray; 1.78 A; A/B=1-130.
DR PDBsum; 2HU9; -.
DR AlphaFoldDB; O29901; -.
DR SMR; O29901; -.
DR STRING; 224325.AF_0346; -.
DR TCDB; 3.A.3.5.7; the p-type atpase (p-atpase) superfamily.
DR DNASU; 1483560; -.
DR EnsemblBacteria; AAB90886; AAB90886; AF_0346.
DR GeneID; 24793885; -.
DR KEGG; afu:AF_0346; -.
DR eggNOG; arCOG02764; Archaea.
DR HOGENOM; CLU_1346350_0_0_2; -.
DR OrthoDB; 124617at2157; -.
DR EvolutionaryTrace; O29901; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 1.10.10.1100; -; 1.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR040890; Znf_CopZ.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF18423; zf_CopZ; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chaperone; Copper; Cytoplasm; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..204
FT /note="Copper chaperone CopZ"
FT /id="PRO_0000351288"
FT DOMAIN 138..200
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 109
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 149
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MUTAGEN 75
FT /note="C->S: Alters iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:17609202"
FT MUTAGEN 77
FT /note="C->S: Alters iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:17609202"
FT MUTAGEN 109
FT /note="C->S: Alters iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:17609202"
FT MUTAGEN 118
FT /note="C->S: No effect on iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:17609202"
FT MUTAGEN 119
FT /note="C->S: Alters iron-sulfur binding."
FT /evidence="ECO:0000269|PubMed:17609202"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:2HU9"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:2HU9"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2HU9"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2HU9"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2HU9"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2HU9"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2HU9"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2HU9"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:2HU9"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:2HU9"
SQ SEQUENCE 204 AA; 22588 MW; 776EE192AFDD8C85 CRC64;
MMRCPECSTE GWRVLPLTVG AHVKEGLWSK IKGDFYFCSL ESCEVVYFNE QTVFRKGELK
TRVGVKEREE PKPVCYCNRV TEKMLLEAAE KFGKEKAVEI TGAGKGKWCV VTNPSGRCCH
WHLERLGFPV GGEKKAAKRV EIKLDGLTCM GCVSAVKAAL EEAGANVVEI GLDRAVVEVD
EEAELQKLVE AVEGAGYSAR LEKR
