CUER_ECOLI
ID CUER_ECOLI Reviewed; 135 AA.
AC P0A9G4; P77565; Q2MBU0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=HTH-type transcriptional regulator CueR;
DE AltName: Full=Copper efflux regulator;
DE AltName: Full=Copper export regulator;
GN Name=cueR {ECO:0000303|PubMed:10915804};
GN Synonyms=copR {ECO:0000303|PubMed:11167016}, ybbI;
GN OrderedLocusNames=b0487, JW0476;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=11136469; DOI=10.1046/j.1365-2958.2001.02264.x;
RA Stoyanov J.V., Hobman J.L., Brown N.L.;
RT "CueR (YbbI) of Escherichia coli is a MerR family regulator controlling
RT expression of the copper exporter CopA.";
RL Mol. Microbiol. 39:502-512(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=11167016; DOI=10.1016/s0378-1119(00)00509-6;
RA Petersen C., Moeller L.B.;
RT "Control of copper homeostasis in Escherichia coli by a P-type ATPase,
RT CopA, and a MerR-like transcriptional activator, CopR.";
RL Gene 261:289-298(2000).
RN [6]
RP FUNCTION.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=10915804; DOI=10.1074/jbc.m006508200;
RA Outten F.W., Outten C.E., Hale J.A., O'Halloran T.V.;
RT "Transcriptional activation of an Escherichia coli copper efflux regulon by
RT the chromosomal merR homologue, cueR.";
RL J. Biol. Chem. 275:31024-31029(2000).
RN [7]
RP ROLE IN COPPER HOMEOSTASIS.
RC STRAIN=K12;
RX PubMed=11399769; DOI=10.1074/jbc.m104122200;
RA Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.;
RT "The independent cue and cus systems confer copper tolerance during aerobic
RT and anaerobic growth in Escherichia coli.";
RL J. Biol. Chem. 276:30670-30677(2001).
RN [8]
RP CHARACTERIZATION OF THE METAL-BINDING CENTER, AND MUTAGENESIS OF CYS-112;
RP CYS-120; CYS-129 AND CYS-130.
RX PubMed=14518983; DOI=10.1021/ja036070y;
RA Chen K., Yuldasheva S., Penner-Hahn J.E., O'Halloran T.V.;
RT "An atypical linear Cu(I)-S2 center constitutes the high-affinity metal-
RT sensing site in the CueR metalloregulatory protein.";
RL J. Am. Chem. Soc. 125:12088-12089(2003).
RN [9]
RP INDUCTION, AND MUTAGENESIS OF CYS-112; CYS-120; CYS-129 AND CYS-130.
RX PubMed=12446701; DOI=10.1074/jbc.c200580200;
RA Stoyanov J.V., Brown N.L.;
RT "The Escherichia coli copper-responsive copA promoter is activated by
RT gold.";
RL J. Biol. Chem. 278:1407-1410(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).
RX PubMed=12958362; DOI=10.1126/science.1085950;
RA Changela A., Chen K., Xue Y., Holschen J., Outten C.E., O'Halloran T.V.,
RA Mondragon A.;
RT "Molecular basis of metal-ion selectivity and zeptomolar sensitivity by
RT CueR.";
RL Science 301:1383-1387(2003).
CC -!- FUNCTION: Regulates the transcription of the copA and cueO genes. It
CC detects cytoplasmic copper stress and activates transcription in
CC response to increasing copper concentrations.
CC {ECO:0000269|PubMed:10915804, ECO:0000269|PubMed:11167016,
CC ECO:0000269|PubMed:11399769}.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P0A9G4; P0A9G4: cueR; NbExp=3; IntAct=EBI-1117686, EBI-1117686;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: It contains an N-terminal DNA binding region and a C-terminal
CC metal binding region.
CC -!- DISRUPTION PHENOTYPE: Loss of Cu-induction of copA, forms smaller than
CC wild-type colonies when grown on 2 mM CuSO(4) (PubMed:11167016).
CC {ECO:0000269|PubMed:11167016}.
CC -!- MISCELLANEOUS: CueR tightly binds Cu(1+) via a linear S-Cu-S center.
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DR EMBL; AF318185; AAK06655.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40241.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73589.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76266.1; -; Genomic_DNA.
DR PIR; F64779; F64779.
DR RefSeq; NP_415020.1; NC_000913.3.
DR RefSeq; WP_001026747.1; NZ_STEB01000007.1.
DR PDB; 1Q05; X-ray; 2.20 A; A/B=1-135.
DR PDB; 1Q06; X-ray; 2.07 A; A/B=1-135.
DR PDB; 1Q07; X-ray; 2.50 A; A/B=1-135.
DR PDB; 4WLS; X-ray; 2.10 A; A/B=1-128.
DR PDB; 4WLW; X-ray; 2.80 A; A=1-135.
DR PDB; 6LDI; EM; 3.69 A; G/H=1-135.
DR PDB; 6XH7; EM; 3.90 A; G/H=1-135.
DR PDB; 6XH8; EM; 4.10 A; G/H=1-135.
DR PDB; 7C17; EM; 4.22 A; G/H=1-135.
DR PDBsum; 1Q05; -.
DR PDBsum; 1Q06; -.
DR PDBsum; 1Q07; -.
DR PDBsum; 4WLS; -.
DR PDBsum; 4WLW; -.
DR PDBsum; 6LDI; -.
DR PDBsum; 6XH7; -.
DR PDBsum; 6XH8; -.
DR PDBsum; 7C17; -.
DR AlphaFoldDB; P0A9G4; -.
DR SMR; P0A9G4; -.
DR BioGRID; 4259848; 11.
DR DIP; DIP-51206N; -.
DR IntAct; P0A9G4; 4.
DR STRING; 511145.b0487; -.
DR jPOST; P0A9G4; -.
DR PaxDb; P0A9G4; -.
DR PRIDE; P0A9G4; -.
DR EnsemblBacteria; AAC73589; AAC73589; b0487.
DR EnsemblBacteria; BAE76266; BAE76266; BAE76266.
DR GeneID; 66671211; -.
DR GeneID; 945332; -.
DR KEGG; ecj:JW0476; -.
DR KEGG; eco:b0487; -.
DR PATRIC; fig|1411691.4.peg.1789; -.
DR EchoBASE; EB3044; -.
DR eggNOG; COG0789; Bacteria.
DR HOGENOM; CLU_060077_2_0_6; -.
DR InParanoid; P0A9G4; -.
DR OMA; FNDPERH; -.
DR PhylomeDB; P0A9G4; -.
DR BioCyc; EcoCyc:G6263-MON; -.
DR EvolutionaryTrace; P0A9G4; -.
DR PRO; PR:P0A9G4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IPI:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd01108; HTH_CueR; 1.
DR InterPro; IPR011789; CueR.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR Pfam; PF13411; MerR_1; 1.
DR PRINTS; PR00040; HTHMERR.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR02044; CueR; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Copper; Cytoplasm; DNA-binding; Metal-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..135
FT /note="HTH-type transcriptional regulator CueR"
FT /id="PRO_0000098111"
FT DOMAIN 1..69
FT /note="HTH merR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT DNA_BIND 4..23
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT BINDING 112
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT BINDING 120
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT MUTAGEN 112
FT /note="C->S: Loss of sensitivity to copper."
FT /evidence="ECO:0000269|PubMed:12446701,
FT ECO:0000269|PubMed:14518983"
FT MUTAGEN 120
FT /note="C->S: Loss of sensitivity to copper."
FT /evidence="ECO:0000269|PubMed:12446701,
FT ECO:0000269|PubMed:14518983"
FT MUTAGEN 129
FT /note="C->S: No effect on response to copper."
FT /evidence="ECO:0000269|PubMed:12446701,
FT ECO:0000269|PubMed:14518983"
FT MUTAGEN 130
FT /note="C->S: No effect on response to copper."
FT /evidence="ECO:0000269|PubMed:12446701,
FT ECO:0000269|PubMed:14518983"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:1Q06"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:1Q06"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:1Q06"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1Q06"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:4WLS"
FT HELIX 77..110
FT /evidence="ECO:0007829|PDB:1Q06"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1Q06"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:1Q06"
SQ SEQUENCE 135 AA; 15235 MW; A3AE39F9E3140862 CRC64;
MNISDVAKIT GLTSKAIRFY EEKGLVTPPM RSENGYRTYT QQHLNELTLL RQARQVGFNL
EESGELVNLF NDPQRHSADV KRRTLEKVAE IERHIEELQS MRDQLLALAN ACPGDDSADC
PIIENLSGCC HHRAG
