ID   COPZ_ENTHR              Reviewed;          69 AA.
AC   Q47840;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Copper chaperone copZ;
DE   AltName: Full=Activator of copYZAB;
GN   Name=copZ;
OS   Enterococcus hirae.
OC   Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus.
OX   NCBI_TaxID=1354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
RX   MEDLINE=95181419; PubMed=7876197; DOI=10.1074/jbc.270.9.4349;
RA   Odermatt A., Solioz M.;
RT   "Two trans-acting metalloregulatory proteins controlling expression of
RT   the copper-ATPases of Enterococcus hirae.";
RL   J. Biol. Chem. 270:4349-4354(1995).
RN   [2]
RP   INDUCTION BY COPPER.
RC   STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
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
RT   operon of Enterococcus hirae by copper(I) and copper(II).";
RL   Biochem. Biophys. Res. Commun. 259:443-449(1999).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
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
RT   the CopY repressor.";
RL   FEBS Lett. 445:27-30(1999).
RN   [4]
RP   REGULATION BY PROTEOLYSIS.
RC   STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
RX   PubMed=11585824; DOI=10.1074/jbc.M106218200;
RA   Lu Z.H., Solioz M.;
RT   "Copper-induced proteolysis of the CopZ copper chaperone of
RT   Enterococcus hirae.";
RL   J. Biol. Chem. 276:47822-47827(2001).
RN   [5]
RP   INTERACTION WITH COPA.
RC   STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
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
RT   of Enterococcus hirae assessed by surface plasmon resonance.";
RL   Biochem. Biophys. Res. Commun. 288:172-177(2001).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH COPY.
RC   STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
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
RT   interactions.";
RL   Biochemistry 41:5822-5829(2002).
RN   [7]
RP   STRUCTURE BY NMR OF 3-69, SUBUNIT, AND COPPER BINDING.
RC   STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
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
CC       copY Zn(2+)-bound form. This transfer results in displacement of
CC       zinc and dissociation of copY from the promoter, allowing
CC       transcription of the copYZAB operon.
CC   -!- SUBUNIT: Monomer in the absence of copper. Homodimer or
CC       homooligomer in the presence of copper ions. Interacts with the
CC       copper ATPase copA. Interacts with copY via a charge-based
CC       interaction.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- INDUCTION: By Cu(+) and Cu(2+).
CC   -!- MISCELLANEOUS: Controlled by copper-induced proteolysis.
CC   -!- SIMILARITY: Contains 1 HMA domain.
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DR   EMBL; Z46807; CAA86836.1; -; Genomic_DNA.
DR   PIR; B56085; B56085.
DR   PDB; 1CPZ; NMR; -; A=3-69.
DR   PDBsum; 1CPZ; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004008; F:copper-exporting ATPase activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006825; P:copper ion transport; IEA:InterPro.
DR   InterPro; IPR001877; ATPase1_Cu-transp.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR006122; Cu_ion_bd.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HeavyMe_transpt.
DR   PANTHER; PTHR11939; ATPase_P; 1.
DR   Pfam; PF00403; HMA; 1.
DR   PRINTS; PR00942; CUATPASEI.
DR   TIGRFAMs; TIGR00003; Cu_ion_bd; 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       Copper chaperone copZ.
FT                                /FTId=PRO_0000079248.
FT   DOMAIN        2     68       HMA.
FT   METAL        12     12       Copper.
FT   METAL        15     15       Copper.
FT   STRAND        4      8
FT   STRAND       12     14
FT   HELIX        15     24
FT   STRAND       29     35
FT   TURN         36     39
FT   STRAND       40     45
FT   TURN         47     49
FT   HELIX        52     60
FT   STRAND       66     68
SQ   SEQUENCE   69 AA;  7653 MW;  8BBCBFA4BD10C997 CRC64;
     MKQEFSVKGM SCNHCVARIE EAVGRISGVK KVKVQLKKEK AVVKFDEANV QATEICQAIN
     ELGYQAEVI
//