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Ferric uptake regulation protein (Ferric uptake regulator)

 FUR_ECOLI               Reviewed;         148 AA.
P0A9A9; P06975;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
28-MAR-2018, entry version 114.
RecName: Full=Ferric uptake regulation protein;
Short=Ferric uptake regulator;
Name=fur; OrderedLocusNames=b0683, JW0669;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2993806; DOI=10.1007/BF00383321;
Schaeffer S., Hantke K., Braun V.;
"Nucleotide sequence of the iron regulatory gene fur.";
Mol. Gen. Genet. 200:110-113(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-8.
STRAIN=K12;
PubMed=17895580; DOI=10.1266/ggs.82.291;
Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
"A role of RnlA in the RNase LS activity from Escherichia coli.";
Genes Genet. Syst. 82:291-299(2007).
[6]
FUNCTION.
PubMed=2823881; DOI=10.1021/bi00391a039;
Bagg A., Neilands J.B.;
"Ferric uptake regulation protein acts as a repressor, employing iron
(II) as a cofactor to bind the operator of an iron transport operon in
Escherichia coli.";
Biochemistry 26:5471-5477(1987).
[7]
STRUCTURAL DYNAMICS.
PubMed=1868094; DOI=10.1021/bi00247a016;
Coy M., Neilands J.B.;
"Structural dynamics and functional domains of the fur protein.";
Biochemistry 30:8201-8210(1991).
[8]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[9]
ZINC-BINDING SITES.
PubMed=10387106; DOI=10.1021/bi9902283;
Gonzalez de Peredo A., Saint-Pierre C., Adrait A., Jacquamet L.,
Latour J.M., Michaud-Soret I., Forest E.;
"Identification of the two zinc-bound cysteines in the ferric uptake
regulation protein from Escherichia coli: chemical modification and
mass spectrometry analysis.";
Biochemistry 38:8582-8589(1999).
[10]
STRUCTURE BY NMR.
PubMed=2015825; DOI=10.1111/j.1432-1033.1991.tb15880.x;
Saito T., Williams R.J.;
"The binding of the ferric uptake regulation protein to a DNA
fragment.";
Eur. J. Biochem. 197:43-47(1991).
-!- FUNCTION: Acts as a global negative controlling element, employing
Fe(2+) as a cofactor to bind the operator of the repressed genes.
Regulates the expression of several outer-membrane proteins
including the iron transport operon. {ECO:0000269|PubMed:2823881}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: Activated by cadmium, cobalt, copper, and manganese
ions, but not zinc ions.
-!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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EMBL; X02589; CAA26429.1; -; Genomic_DNA.
EMBL; U00096; AAC73777.1; -; Genomic_DNA.
EMBL; AP009048; BAA35331.1; -; Genomic_DNA.
PIR; S07308; S07308.
RefSeq; NP_415209.1; NC_000913.3.
RefSeq; WP_000131702.1; NZ_LN832404.1.
PDB; 2FU4; X-ray; 1.80 A; A/B=1-83.
PDBsum; 2FU4; -.
ProteinModelPortal; P0A9A9; -.
SMR; P0A9A9; -.
BioGrid; 4262110; 43.
BioGrid; 849672; 1.
DIP; DIP-31858N; -.
IntAct; P0A9A9; 50.
STRING; 316385.ECDH10B_0748; -.
SWISS-2DPAGE; P0A9A9; -.
EPD; P0A9A9; -.
PaxDb; P0A9A9; -.
PRIDE; P0A9A9; -.
EnsemblBacteria; AAC73777; AAC73777; b0683.
EnsemblBacteria; BAA35331; BAA35331; BAA35331.
GeneID; 945295; -.
KEGG; ecj:JW0669; -.
KEGG; eco:b0683; -.
PATRIC; fig|1411691.4.peg.1593; -.
EchoBASE; EB0354; -.
EcoGene; EG10359; fur.
eggNOG; ENOG41090R7; Bacteria.
eggNOG; COG0735; LUCA.
HOGENOM; HOG000014144; -.
InParanoid; P0A9A9; -.
KO; K03711; -.
OMA; NEGQHHD; -.
PhylomeDB; P0A9A9; -.
BioCyc; EcoCyc:PD00260; -.
EvolutionaryTrace; P0A9A9; -.
PRO; PR:P0A9A9; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
CollecTF; EXPREG_000007c0; -.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
GO; GO:0001216; F:bacterial-type RNA polymerase transcriptional activator activity, sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0001217; F:bacterial-type RNA polymerase transcriptional repressor activity, sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CollecTF.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd07153; Fur_like; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR002481; FUR.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR33202; PTHR33202; 1.
Pfam; PF01475; FUR; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
DNA-binding; Iron; Metal-binding; Reference proteome; Repressor;
Transcription; Transcription regulation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:17895580}.
CHAIN 2 148 Ferric uptake regulation protein.
/FTId=PRO_0000095550.
REGION 2 84 DNA-binding. {ECO:0000250}.
REGION 85 148 Dimerization. {ECO:0000250}.
COMPBIAS 86 90 His-rich.
METAL 33 33 Zinc. {ECO:0000250}.
METAL 81 81 Zinc. {ECO:0000250}.
METAL 87 87 Iron. {ECO:0000250}.
METAL 89 89 Iron. {ECO:0000250}.
METAL 90 90 Zinc. {ECO:0000250}.
METAL 93 93 Zinc.
METAL 96 96 Zinc.
METAL 101 101 Zinc. {ECO:0000250}.
METAL 108 108 Iron. {ECO:0000250}.
METAL 125 125 Iron. {ECO:0000250}.
HELIX 4 10 {ECO:0000244|PDB:2FU4}.
HELIX 17 26 {ECO:0000244|PDB:2FU4}.
HELIX 29 31 {ECO:0000244|PDB:2FU4}.
STRAND 32 34 {ECO:0000244|PDB:2FU4}.
HELIX 36 45 {ECO:0000244|PDB:2FU4}.
HELIX 52 64 {ECO:0000244|PDB:2FU4}.
STRAND 67 72 {ECO:0000244|PDB:2FU4}.
HELIX 74 76 {ECO:0000244|PDB:2FU4}.
STRAND 78 82 {ECO:0000244|PDB:2FU4}.
SEQUENCE 148 AA; 16795 MW; B868360513489DD3 CRC64;
MTDNNTALKK AGLKVTLPRL KILEVLQEPD NHHVSAEDLY KRLIDMGEEI GLATVYRVLN
QFDDAGIVTR HNFEGGKSVF ELTQQHHHDH LICLDCGKVI EFSDDSIEAR QREIAAKHGI
RLTNHSLYLY GHCAEGDCRE DEHAHEGK


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