FUR_ECOLI
ID FUR_ECOLI Reviewed; 148 AA.
AC P0A9A9; P06975;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; OrderedLocusNames=b0683, JW0669;
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=2993806; DOI=10.1007/bf00383321;
RA Schaeffer S., Hantke K., Braun V.;
RT "Nucleotide sequence of the iron regulatory gene fur.";
RL Mol. Gen. Genet. 200:110-113(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 PROTEIN SEQUENCE OF 2-8.
RC STRAIN=K12;
RX PubMed=17895580; DOI=10.1266/ggs.82.291;
RA Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
RT "A role of RnlA in the RNase LS activity from Escherichia coli.";
RL Genes Genet. Syst. 82:291-299(2007).
RN [6]
RP FUNCTION.
RX PubMed=2823881; DOI=10.1021/bi00391a039;
RA Bagg A., Neilands J.B.;
RT "Ferric uptake regulation protein acts as a repressor, employing iron (II)
RT as a cofactor to bind the operator of an iron transport operon in
RT Escherichia coli.";
RL Biochemistry 26:5471-5477(1987).
RN [7]
RP STRUCTURAL DYNAMICS.
RX PubMed=1868094; DOI=10.1021/bi00247a016;
RA Coy M., Neilands J.B.;
RT "Structural dynamics and functional domains of the fur protein.";
RL Biochemistry 30:8201-8210(1991).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP ZINC-BINDING SITES.
RX PubMed=10387106; DOI=10.1021/bi9902283;
RA Gonzalez de Peredo A., Saint-Pierre C., Adrait A., Jacquamet L.,
RA Latour J.M., Michaud-Soret I., Forest E.;
RT "Identification of the two zinc-bound cysteines in the ferric uptake
RT regulation protein from Escherichia coli: chemical modification and mass
RT spectrometry analysis.";
RL Biochemistry 38:8582-8589(1999).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=2015825; DOI=10.1111/j.1432-1033.1991.tb15880.x;
RA Saito T., Williams R.J.;
RT "The binding of the ferric uptake regulation protein to a DNA fragment.";
RL Eur. J. Biochem. 197:43-47(1991).
CC -!- FUNCTION: Acts as a global negative controlling element, employing
CC Fe(2+) as a cofactor to bind the operator of the repressed genes.
CC Regulates the expression of several outer-membrane proteins including
CC the iron transport operon. {ECO:0000269|PubMed:2823881}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Activated by cadmium, cobalt, copper, and manganese
CC ions, but not zinc ions.
CC -!- SIMILARITY: Belongs to the Fur family. {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; X02589; CAA26429.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73777.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35331.1; -; Genomic_DNA.
DR PIR; S07308; S07308.
DR RefSeq; NP_415209.1; NC_000913.3.
DR RefSeq; WP_000131702.1; NZ_STEB01000044.1.
DR PDB; 2FU4; X-ray; 1.80 A; A/B=1-83.
DR PDBsum; 2FU4; -.
DR AlphaFoldDB; P0A9A9; -.
DR BMRB; P0A9A9; -.
DR SMR; P0A9A9; -.
DR BioGRID; 4262110; 43.
DR BioGRID; 849672; 1.
DR DIP; DIP-31858N; -.
DR IntAct; P0A9A9; 50.
DR STRING; 511145.b0683; -.
DR SWISS-2DPAGE; P0A9A9; -.
DR jPOST; P0A9A9; -.
DR PaxDb; P0A9A9; -.
DR PRIDE; P0A9A9; -.
DR EnsemblBacteria; AAC73777; AAC73777; b0683.
DR EnsemblBacteria; BAA35331; BAA35331; BAA35331.
DR GeneID; 66671047; -.
DR GeneID; 945295; -.
DR KEGG; ecj:JW0669; -.
DR KEGG; eco:b0683; -.
DR PATRIC; fig|1411691.4.peg.1593; -.
DR EchoBASE; EB0354; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_3_3_6; -.
DR InParanoid; P0A9A9; -.
DR OMA; HDHVILT; -.
DR PhylomeDB; P0A9A9; -.
DR BioCyc; EcoCyc:PD00260; -.
DR EvolutionaryTrace; P0A9A9; -.
DR PHI-base; PHI:4887; -.
DR PRO; PR:P0A9A9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_000007c0; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; 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; IMP:CollecTF.
DR GO; GO:0043565; F:sequence-specific DNA binding; IPI:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:1900705; P:negative regulation of siderophore biosynthetic process; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CollecTF.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
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; Cytoplasm; Direct protein sequencing; DNA-binding; Iron;
KW Metal-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17895580"
FT CHAIN 2..148
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095550"
FT REGION 2..84
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 85..148
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:2FU4"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:2FU4"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2FU4"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2FU4"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2FU4"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:2FU4"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2FU4"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2FU4"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2FU4"
SQ SEQUENCE 148 AA; 16795 MW; B868360513489DD3 CRC64;
MTDNNTALKK AGLKVTLPRL KILEVLQEPD NHHVSAEDLY KRLIDMGEEI GLATVYRVLN
QFDDAGIVTR HNFEGGKSVF ELTQQHHHDH LICLDCGKVI EFSDDSIEAR QREIAAKHGI
RLTNHSLYLY GHCAEGDCRE DEHAHEGK
