ZUR_ECOLI
ID ZUR_ECOLI Reviewed; 171 AA.
AC P0AC51; P32692; P76784; Q2M6Q8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Zinc uptake regulation protein;
DE Short=Zinc uptake regulator;
GN Name=zur; Synonyms=yjbK; OrderedLocusNames=b4046, JW5714;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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=9680209; DOI=10.1046/j.1365-2958.1998.00883.x;
RA Patzer S.I., Hantke K.;
RT "The ZnuABC high-affinity zinc uptake system and its regulator Zur in
RT Escherichia coli.";
RL Mol. Microbiol. 28:1199-1210(1998).
CC -!- FUNCTION: Acts as a negative controlling element, employing Zn(2+) as a
CC cofactor to bind the operator of the repressed genes (znuACB).
CC -!- INTERACTION:
CC P0AC51; P0AC51: zur; NbExp=2; IntAct=EBI-16126292, EBI-16126292;
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43140.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00006; AAC43140.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77016.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78048.1; -; Genomic_DNA.
DR PIR; E65212; E65212.
DR RefSeq; NP_418470.4; NC_000913.3.
DR RefSeq; WP_001295691.1; NZ_STEB01000022.1.
DR PDB; 4MTD; X-ray; 2.50 A; A/B/C/D=1-171.
DR PDB; 4MTE; X-ray; 2.50 A; A/B/C/D=1-171.
DR PDBsum; 4MTD; -.
DR PDBsum; 4MTE; -.
DR AlphaFoldDB; P0AC51; -.
DR SMR; P0AC51; -.
DR BioGRID; 4261723; 7.
DR DIP; DIP-12953N; -.
DR STRING; 511145.b4046; -.
DR jPOST; P0AC51; -.
DR PaxDb; P0AC51; -.
DR PRIDE; P0AC51; -.
DR EnsemblBacteria; AAC77016; AAC77016; b4046.
DR EnsemblBacteria; BAE78048; BAE78048; BAE78048.
DR GeneID; 66672039; -.
DR GeneID; 948552; -.
DR KEGG; ecj:JW5714; -.
DR KEGG; eco:b4046; -.
DR PATRIC; fig|511145.12.peg.4163; -.
DR EchoBASE; EB1873; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_2_1_6; -.
DR InParanoid; P0AC51; -.
DR OMA; DHSHCVH; -.
DR PhylomeDB; P0AC51; -.
DR BioCyc; EcoCyc:EG11929-MON; -.
DR PRO; PR:P0AC51; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
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:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd07153; Fur_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.1490.190; -; 1.
DR InterPro; IPR002481; FUR.
DR InterPro; IPR043135; Fur_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR33202; PTHR33202; 1.
DR Pfam; PF01475; FUR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..171
FT /note="Zinc uptake regulation protein"
FT /id="PRO_0000095592"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:4MTD"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:4MTD"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:4MTD"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:4MTD"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:4MTD"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4MTD"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:4MTD"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4MTD"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4MTD"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4MTD"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4MTD"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4MTD"
FT STRAND 131..142
FT /evidence="ECO:0007829|PDB:4MTD"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:4MTD"
SQ SEQUENCE 171 AA; 19254 MW; 84B712B1BBF00D41 CRC64;
MEKTTTQELL AQAEKICAQR NVRLTPQRLE VLRLMSLQDG AISAYDLLDL LREAEPQAKP
PTVYRALDFL LEQGFVHKVE STNSYVLCHL FDQPTHTSAM FICDRCGAVK EECAEGVEDI
MHTLAAKMGF ALRHNVIEAH GLCAACVEVE ACRHPEQCQH DHSVQVKKKP R
