FUR_CAMJ8
ID FUR_CAMJ8 Reviewed; 157 AA.
AC A8FKI7; O68606; P48796; Q0PBB0; Q46112;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; OrderedLocusNames=C8J_0375;
OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS 11828).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=407148;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8083178; DOI=10.1128/jb.176.18.5852-5856.1994;
RA Wooldridge K.G., Williams P.H., Ketley J.M.;
RT "Iron-responsive genetic regulation in Campylobacter jejuni: cloning and
RT characterization of a fur homolog.";
RL J. Bacteriol. 176:5852-5856(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81116 / NCTC 11828;
RX PubMed=17873037; DOI=10.1128/jb.01404-07;
RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA van Vliet A.H.M.;
RT "The complete genome sequence of Campylobacter jejuni strain 81116
RT (NCTC11828).";
RL J. Bacteriol. 189:8402-8403(2007).
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; X78965; CAA55559.1; -; Genomic_DNA.
DR EMBL; CP000814; ABV51974.1; -; Genomic_DNA.
DR PIR; I40766; S44239.
DR RefSeq; WP_002854230.1; NC_009839.1.
DR AlphaFoldDB; A8FKI7; -.
DR SMR; A8FKI7; -.
DR KEGG; cju:C8J_0375; -.
DR HOGENOM; CLU_096072_3_1_7; -.
DR OMA; YLYGVCT; -.
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..157
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000315383"
FT REGION 1..96
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 97..157
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"
FT CONFLICT 68..70
FT /note="YRT -> IVL (in Ref. 1; CAA55559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 18054 MW; 1DCFA9A59281F1EF CRC64;
MLIENVEYDV LLERFKKILR QGGLKYTKQR EVLLKTLYHS DTHYTPESLY MEIKQAEPDL
NVGIATVYRT LNLLEEAEMV TSISFGSAGK KYELANKPHH DHMICKNCGK IIEFENPIIE
RQQALIAKEH GFKLTGHLMQ LYGVCGDCNN QKAKVKI