COPY_ENTHA
ID COPY_ENTHA Reviewed; 145 AA.
AC Q47839; I6SZ22;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Transcriptional repressor CopY;
DE AltName: Full=CopAB ATPases metal-fist type repressor;
GN Name=copY; OrderedLocusNames=EHR_09075;
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 AS A REPRESSOR.
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 FUNCTION AS A REPRESSOR, DNA-BINDING, AND SUBUNIT.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=9083014; DOI=10.1074/jbc.272.14.8932;
RA Strausak D., Solioz M.;
RT "CopY is a copper-inducible repressor of the Enterococcus hirae copper
RT ATPases.";
RL J. Biol. Chem. 272:8932-8936(1997).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH COPZ.
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 [6]
RP FUNCTION, AND INTERACTION WITH COPZ.
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).
CC -!- FUNCTION: Acts as a copper responsive repressor. Binds to DNA in
CC complex with Zn(2+), repressing the transcription of the copYZAB
CC operon. Exchange of the bound zinc by two copper ions delivered by CopZ
CC Cu(1+)-bound form causes release of CopY from the promoter, leading to
CC the transcription of the operon. {ECO:0000269|PubMed:10069368,
CC ECO:0000269|PubMed:11980486, ECO:0000269|PubMed:7876197,
CC ECO:0000269|PubMed:9083014}.
CC -!- SUBUNIT: Homodimer. Interacts with CopZ Cu(1+)-bound form via a charge-
CC based interaction. {ECO:0000269|PubMed:10069368,
CC ECO:0000269|PubMed:11980486, ECO:0000269|PubMed:9083014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By copper. {ECO:0000269|PubMed:10362527}.
CC -!- SIMILARITY: Belongs to the BlaI transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; Z46807; CAA86835.1; -; Genomic_DNA.
DR EMBL; CP003504; AFM70727.1; -; Genomic_DNA.
DR PIR; A56085; A56085.
DR RefSeq; WP_010737926.1; NZ_KB946231.1.
DR AlphaFoldDB; Q47839; -.
DR SMR; Q47839; -.
DR STRING; 768486.EHR_09075; -.
DR EnsemblBacteria; AFM70727; AFM70727; EHR_09075.
DR KEGG; ehr:EHR_09075; -.
DR eggNOG; COG3682; Bacteria.
DR HOGENOM; CLU_119090_2_1_9; -.
DR OrthoDB; 2027769at2; -.
DR Proteomes; UP000002895; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005650; BlaI_family.
DR InterPro; IPR014071; Cu_transp_CopY/TcrY.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34134; PTHR34134; 1.
DR Pfam; PF03965; Penicillinase_R; 1.
DR PIRSF; PIRSF019455; CopR_AtkY; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR TIGRFAMs; TIGR02698; CopY_TcrY; 1.
PE 1: Evidence at protein level;
KW Copper; Cytoplasm; DNA-binding; Metal-binding; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..145
FT /note="Transcriptional repressor CopY"
FT /id="PRO_0000062795"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
SQ SEQUENCE 145 AA; 16577 MW; BC825992EE968868 CRC64;
MEEKRVLIKI SDSEWEVMRV IWTLGQANAQ QITQILADSM DWKVATVKTL LGRLVKKEAL
WTEQEGKKFI YHPAVSEMEN VRSATENLFS HICAKRVGAT IADLVEEATL TQEDIQQIMK
QLNKKEPVET IECNCIPGQC ECKKQ
