ID   FUR_CUPMC               Reviewed;         143 AA.
AC   O30330; Q1LJ27;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Ferric uptake regulation protein;
DE            Short=Ferric uptake regulator;
GN   Name=fur; Synonyms=aleO; OrderedLocusNames=Rmet_2976;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gilis A., Borremans B., Cornelis P., Mergeay M., van der Lelie D.;
RT   "Identification and regulation of the Alcaligenes eutrophus CH34 fur
RT   gene.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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       Regulator for biosynthesis of the siderophore alcaligin E.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AJ001224; CAA04620.1; -; Genomic_DNA.
DR   EMBL; CP000352; ABF09849.1; -; Genomic_DNA.
DR   RefSeq; WP_008648581.1; NC_007973.1.
DR   AlphaFoldDB; O30330; -.
DR   SMR; O30330; -.
DR   STRING; 266264.Rmet_2976; -.
DR   EnsemblBacteria; ABF09849; ABF09849; Rmet_2976.
DR   GeneID; 60820587; -.
DR   KEGG; rme:Rmet_2976; -.
DR   eggNOG; COG0735; Bacteria.
DR   HOGENOM; CLU_096072_3_3_4; -.
DR   OMA; HDHVILT; -.
DR   OrthoDB; 1630127at2; -.
DR   Proteomes; UP000002429; 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..143
FT                   /note="Ferric uptake regulation protein"
FT                   /id="PRO_0000095540"
FT   REGION          1..83
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          84..143
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   143 AA;  16432 MW;  D88B8E603901E49B CRC64;
     MPSPADLKNI GLKATVPRLK ILEIFQTSEQ RHLSAEDVYR ILLNEHMDIG LATVYRVLTQ
     FEQAGLLSRN NFESGKAIFE LNEGKHHDHL VCLDCGRVEE FFDADIEQRQ QSIARERGFA
     LQEHALSLYG NCTKDDCPHR PRR