FUR_CAMUP
ID FUR_CAMUP Reviewed; 156 AA.
AC Q46463;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur;
OS Campylobacter upsaliensis.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=28080;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43954 / DSM 5365 / CCUG 14913 / LMG 8850 / NCTC 11541;
RX PubMed=8996110; DOI=10.1016/s0378-1119(96)00562-8;
RA Bourke B., Al-Rashid S.T., Bingham H.L., Chan V.L.;
RT "Characterization of Campylobacter upsaliensis fur and its localization in
RT a highly conserved region of the Campylobacter genome.";
RL Gene 183:219-224(1996).
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; L77075; AAB41341.1; -; Genomic_DNA.
DR PIR; JC5752; JC5752.
DR AlphaFoldDB; Q46463; -.
DR SMR; Q46463; -.
DR STRING; 306264.CUP0207; -.
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; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..156
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095549"
FT REGION 1..96
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 97..156
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT BINDING 43
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 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 156 AA; 18109 MW; B81B307CDE80BD48 CRC64;
MLMENLEYDV LLEKFKKILR EGGLKYTKQR EVLLKTLYHS DTHYTPESLY MEIKQAEPDS
NVGIATVYRT LNLLEEAEMV TSLSLDSAGK KYELSNKPHH DHMICKVCGK IIEFENPIIE
RQQSLIANEH HFKLTGHLMQ LYGICSDCNH KTKVKI
