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FUR_ECO57
ID   FUR_ECO57               Reviewed;         148 AA.
AC   P0A9B1; P06975;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Ferric uptake regulation protein;
DE            Short=Ferric uptake regulator;
GN   Name=fur; OrderedLocusNames=Z0831, ECs0714;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG55006.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34137.1; -; Genomic_DNA.
DR   PIR; B85568; B85568.
DR   PIR; B90718; B90718.
DR   RefSeq; NP_308741.1; NC_002695.1.
DR   RefSeq; WP_000131702.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A9B1; -.
DR   BMRB; P0A9B1; -.
DR   SMR; P0A9B1; -.
DR   STRING; 155864.EDL933_0755; -.
DR   EnsemblBacteria; AAG55006; AAG55006; Z0831.
DR   EnsemblBacteria; BAB34137; BAB34137; ECs_0714.
DR   GeneID; 66671047; -.
DR   GeneID; 917083; -.
DR   KEGG; ece:Z0831; -.
DR   KEGG; ecs:ECs_0714; -.
DR   PATRIC; fig|386585.9.peg.830; -.
DR   eggNOG; COG0735; Bacteria.
DR   HOGENOM; CLU_096072_3_3_6; -.
DR   OMA; HDHVILT; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Iron; Metal-binding; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..148
FT                   /note="Ferric uptake regulation protein"
FT                   /id="PRO_0000095551"
FT   REGION          1..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                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
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"
SQ   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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