COPZ_ENTHA
ID COPZ_ENTHA Reviewed; 69 AA.
AC Q47840; I6SDM0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Copper chaperone CopZ;
DE AltName: Full=Activator of copYZAB;
GN Name=copZ; OrderedLocusNames=EHR_09080;
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=7876197; DOI=10.1074/jbc.270.9.4349;
RA Odermatt A., Solioz M.;
RT "Two trans-acting metalloregulatory proteins controlling expression of the
RT copper-ATPases of Enterococcus hirae.";
RL J. Biol. Chem. 270:4349-4354(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=22933757; DOI=10.1128/jb.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
RN [3]
RP INDUCTION BY COPPER.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=10362527; DOI=10.1006/bbrc.1999.0807;
RA Wunderli-Ye H., Solioz M.;
RT "Effects of promoter mutations on the in vivo regulation of the cop operon
RT of Enterococcus hirae by copper(I) and copper(II).";
RL Biochem. Biophys. Res. Commun. 259:443-449(1999).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=10069368; DOI=10.1016/s0014-5793(99)00091-5;
RA Cobine P.A., Wickramasinghe W.A., Harrison M.D., Weber T., Solioz M.,
RA Dameron C.T.;
RT "The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the
RT CopY repressor.";
RL FEBS Lett. 445:27-30(1999).
RN [5]
RP REGULATION BY PROTEOLYSIS.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=11585824; DOI=10.1074/jbc.m106218200;
RA Lu Z.H., Solioz M.;
RT "Copper-induced proteolysis of the CopZ copper chaperone of Enterococcus
RT hirae.";
RL J. Biol. Chem. 276:47822-47827(2001).
RN [6]
RP INTERACTION WITH COPA.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=11594769; DOI=10.1006/bbrc.2001.5757;
RA Multhaup G., Strausak D., Bissig K.-D., Solioz M.;
RT "Interaction of the CopZ copper chaperone with the CopA copper ATPase of
RT Enterococcus hirae assessed by surface plasmon resonance.";
RL Biochem. Biophys. Res. Commun. 288:172-177(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH COPY.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=11980486; DOI=10.1021/bi025515c;
RA Cobine P.A., George G.N., Jones C.E., Wickramasinghe W.A., Solioz M.,
RA Dameron C.T.;
RT "Copper transfer from the Cu(I) chaperone, CopZ, to the repressor,
RT Zn(II)CopY: metal coordination environments and protein interactions.";
RL Biochemistry 41:5822-5829(2002).
RN [8]
RP STRUCTURE BY NMR OF 3-69, SUBUNIT, AND COPPER BINDING.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=10428839; DOI=10.1074/jbc.274.32.22597;
RA Wimmer R., Herrmann T., Solioz M., Wuethrich K.;
RT "NMR structure and metal interactions of the CopZ copper chaperone.";
RL J. Biol. Chem. 274:22597-22603(1999).
CC -!- FUNCTION: Acts as a copper chaperone by delivering 2 Cu(+) ions to CopY
CC Zn(2+)-bound form. This transfer results in displacement of zinc and
CC dissociation of CopY from the promoter, allowing transcription of the
CC copYZAB operon. {ECO:0000269|PubMed:10069368,
CC ECO:0000269|PubMed:11980486, ECO:0000269|PubMed:7876197}.
CC -!- SUBUNIT: Monomer in the absence of copper. Homodimer or homooligomer in
CC the presence of copper ions. Interacts with the copper ATPase CopA.
CC Interacts with CopY via a charge-based interaction.
CC {ECO:0000269|PubMed:10428839, ECO:0000269|PubMed:11594769,
CC ECO:0000269|PubMed:11980486}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By Cu(+) and Cu(2+). {ECO:0000269|PubMed:10362527}.
CC -!- MISCELLANEOUS: Controlled by copper-induced proteolysis.
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DR EMBL; Z46807; CAA86836.1; -; Genomic_DNA.
DR EMBL; CP003504; AFM70728.1; -; Genomic_DNA.
DR PIR; B56085; B56085.
DR RefSeq; WP_010718490.1; NZ_KB946231.1.
DR PDB; 1CPZ; NMR; -; A=2-69.
DR PDBsum; 1CPZ; -.
DR AlphaFoldDB; Q47840; -.
DR BMRB; Q47840; -.
DR SMR; Q47840; -.
DR STRING; 768486.EHR_09080; -.
DR EnsemblBacteria; AFM70728; AFM70728; EHR_09080.
DR GeneID; 66464646; -.
DR KEGG; ehr:EHR_09080; -.
DR eggNOG; COG2608; Bacteria.
DR HOGENOM; CLU_134973_10_4_9; -.
DR EvolutionaryTrace; Q47840; -.
DR Proteomes; UP000002895; 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 Pfam; PF00403; HMA; 1.
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.
FT CHAIN 1..69
FT /note="Copper chaperone CopZ"
FT /id="PRO_0000079248"
FT DOMAIN 1..67
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 12
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 15
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1CPZ"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1CPZ"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:1CPZ"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1CPZ"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1CPZ"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1CPZ"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1CPZ"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:1CPZ"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1CPZ"
SQ SEQUENCE 69 AA; 7653 MW; 8BBCBFA4BD10C997 CRC64;
MKQEFSVKGM SCNHCVARIE EAVGRISGVK KVKVQLKKEK AVVKFDEANV QATEICQAIN
ELGYQAEVI
