ID   CUER_ECOL6              Reviewed;         135 AA.
AC   Q8FK74;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=HTH-type transcriptional regulator CueR;
DE   AltName: Full=Copper efflux regulator;
DE   AltName: Full=Copper export regulator;
GN   Name=cueR; OrderedLocusNames=c0607;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: It contains a N-terminal DNA binding region and a C-terminal
CC       metal binding region. {ECO:0000250}.
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DR   EMBL; AE014075; AAN79085.1; -; Genomic_DNA.
DR   RefSeq; WP_001026743.1; NC_004431.1.
DR   AlphaFoldDB; Q8FK74; -.
DR   SMR; Q8FK74; -.
DR   STRING; 199310.c0607; -.
DR   EnsemblBacteria; AAN79085; AAN79085; c0607.
DR   KEGG; ecc:c0607; -.
DR   eggNOG; COG0789; Bacteria.
DR   HOGENOM; CLU_060077_2_0_6; -.
DR   OMA; FNDPERH; -.
DR   BioCyc; ECOL199310:C0607-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
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   3: Inferred from homology;
KW   Activator; Copper; Cytoplasm; DNA-binding; Metal-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..135
FT                   /note="HTH-type transcriptional regulator CueR"
FT                   /id="PRO_0000098112"
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                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15206 MW;  ADA0DAEA2C2B0862 CRC64;
     MNISDVAKIT GLTSKAIRFY EEKGLVTPPM RSENGYRTYT QQHLNELTLL RQARQVGFNL
     EESGELVNLF NDPQRHSADV KRRTLEKVAE IEQHIEELQS MRNQLLALAN ACPGDDSADC
     PIIENLSGCC HHRAG