FUR_BORPE
ID FUR_BORPE Reviewed; 139 AA.
AC P0A3E3; Q45337; Q45369; Q45765;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; OrderedLocusNames=BP2507;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UT25;
RX PubMed=7798143; DOI=10.1128/jb.177.1.268-270.1995;
RA Brickman T.J., Armstrong S.K.;
RT "Bordetella pertussis fur gene restores iron repressibility of siderophore
RT and protein expression to deregulated Bordetella bronchiseptica mutants.";
RL J. Bacteriol. 177:268-270(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=80;
RX PubMed=7765895; DOI=10.1007/bf00293637;
RA Beall B.W., Sanden G.N.;
RT "Cloning and initial characterization of the Bordetella pertussis fur
RT gene.";
RL Curr. Microbiol. 30:223-226(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RA Pradel E., Farmer K., Locht C.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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 {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; U11699; AAC43292.1; -; Genomic_DNA.
DR EMBL; L31851; AAC36930.1; -; Genomic_DNA.
DR EMBL; Z48227; CAA88257.1; -; Genomic_DNA.
DR EMBL; BX640418; CAE42779.1; -; Genomic_DNA.
DR PIR; I40326; I40326.
DR RefSeq; NP_881134.1; NC_002929.2.
DR RefSeq; WP_003814098.1; NZ_CP039022.1.
DR AlphaFoldDB; P0A3E3; -.
DR SMR; P0A3E3; -.
DR STRING; 257313.BP2507; -.
DR GeneID; 56477573; -.
DR GeneID; 66437512; -.
DR KEGG; bpe:BP2507; -.
DR PATRIC; fig|257313.5.peg.2705; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_3_3_4; -.
DR OMA; HDHVILT; -.
DR Proteomes; UP000002676; 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..139
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095543"
FT REGION 1..83
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 84..139
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 139 AA; 15728 MW; 048C2F3384C75051 CRC64;
MSDQSELKNM GLKATFPRLK ILDIFRKSDL RHLSAEDVYR ALIAENVEIG LATVYRVLTQ
FEQAGILTRS QFDTGKAVFE LNDGDHHDHL ICTNCGTVFE FSDPDIEKRQ YKVAKDNGFV
LESHAMVLYG ICGNCQKGR