ZNTR_ECOLI
ID ZNTR_ECOLI Reviewed; 141 AA.
AC P0ACS5; P36676; Q2M6V7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=HTH-type transcriptional regulator ZntR;
DE AltName: Full=Zn(II)-responsive regulator of zntA;
GN Name=zntR; Synonyms=yhdM; OrderedLocusNames=b3292, JW3254;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8063098; DOI=10.1016/0378-1119(94)90847-8;
RA Christie G.E., White T.J., Goodwin T.S.;
RT "A merR homologue at 74 minutes on the Escherichia coli genome.";
RL Gene 146:131-132(1994).
RN [2]
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 [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=10048032; DOI=10.1046/j.1365-2958.1999.01229.x;
RA Brocklehurst K.R., Hobman J.L., Lawley B., Blank L., Marshall S.J.,
RA Brown N.L., Morby A.P.;
RT "ZntR is a Zn(II)-responsive MerR-like transcriptional regulator of zntA in
RT Escherichia coli.";
RL Mol. Microbiol. 31:893-902(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 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: Zinc-responsive transcriptional regulator of zntA.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P0ACS5; P75959: nagK; NbExp=2; IntAct=EBI-562184, EBI-556240;
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DR EMBL; L29458; AAA24773.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58089.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76317.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77999.1; -; Genomic_DNA.
DR PIR; I67892; I67892.
DR RefSeq; NP_417751.1; NC_000913.3.
DR RefSeq; WP_000285607.1; NZ_STEB01000038.1.
DR PDB; 1Q08; X-ray; 1.90 A; A/B=43-141.
DR PDB; 1Q09; X-ray; 2.50 A; A=43-141.
DR PDB; 1Q0A; X-ray; 2.00 A; A/B=43-141.
DR PDBsum; 1Q08; -.
DR PDBsum; 1Q09; -.
DR PDBsum; 1Q0A; -.
DR AlphaFoldDB; P0ACS5; -.
DR SMR; P0ACS5; -.
DR BioGRID; 4263395; 8.
DR DIP; DIP-48253N; -.
DR IntAct; P0ACS5; 5.
DR STRING; 511145.b3292; -.
DR jPOST; P0ACS5; -.
DR PaxDb; P0ACS5; -.
DR PRIDE; P0ACS5; -.
DR EnsemblBacteria; AAC76317; AAC76317; b3292.
DR EnsemblBacteria; BAE77999; BAE77999; BAE77999.
DR GeneID; 66672814; -.
DR GeneID; 947786; -.
DR KEGG; ecj:JW3254; -.
DR KEGG; eco:b3292; -.
DR PATRIC; fig|1411691.4.peg.3439; -.
DR EchoBASE; EB1912; -.
DR eggNOG; COG0789; Bacteria.
DR HOGENOM; CLU_060077_2_0_6; -.
DR InParanoid; P0ACS5; -.
DR OMA; FIKCMRN; -.
DR PhylomeDB; P0ACS5; -.
DR BioCyc; EcoCyc:EG11969-MON; -.
DR EvolutionaryTrace; P0ACS5; -.
DR PRO; PR:P0ACS5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR011788; ZntR.
DR Pfam; PF13411; MerR_1; 1.
DR PRINTS; PR00040; HTHMERR.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR02043; ZntR; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..141
FT /note="HTH-type transcriptional regulator ZntR"
FT /id="PRO_0000098160"
FT DOMAIN 1..70
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 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1Q08"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:1Q08"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1Q08"
FT HELIX 79..113
FT /evidence="ECO:0007829|PDB:1Q08"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1Q08"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1Q08"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1Q08"
SQ SEQUENCE 141 AA; 16179 MW; EB451201C8BDCE20 CRC64;
MYRIGELAKM AEVTPDTIRY YEKQQMMEHE VRTEGGFRLY TESDLQRLKF IRHARQLGFS
LESIRELLSI RIDPEHHTCQ ESKGIVQERL QEVEARIAEL QSMQRSLQRL NDACCGTAHS
SVYCSILEAL EQGASGVKSG C
