FUR_CAMJE
ID FUR_CAMJE Reviewed; 157 AA.
AC P0C631; O68606; P48796; Q0PBB0; Q46112;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; OrderedLocusNames=Cj0400;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=7590316; DOI=10.1016/0378-1119(95)00477-n;
RA Chan V.L., Louie H., Bingham H.L.;
RT "Cloning and transcription regulation of the ferric uptake regulatory gene
RT of Campylobacter jejuni TGH9011.";
RL Gene 164:25-31(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=9765558; DOI=10.1128/jb.180.20.5291-5298.1998;
RA van Vliet A.H.M., Wooldridge K.G., Ketley J.M.;
RT "Iron-responsive gene regulation in a campylobacter jejuni fur mutant.";
RL J. Bacteriol. 180:5291-5298(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 -!- INTERACTION:
CC P0C631; P0C631: fur; NbExp=2; IntAct=EBI-1327904, EBI-1327904;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000305}.
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DR EMBL; Z35165; CAA84528.1; -; Genomic_DNA.
DR EMBL; AF052056; AAC64259.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL34550.1; -; Genomic_DNA.
DR PIR; F81383; F81383.
DR RefSeq; WP_002854230.1; NC_002163.1.
DR RefSeq; YP_002343837.1; NC_002163.1.
DR PDB; 4ETS; X-ray; 2.10 A; A/B=1-157.
DR PDBsum; 4ETS; -.
DR AlphaFoldDB; P0C631; -.
DR SMR; P0C631; -.
DR DIP; DIP-60047N; -.
DR IntAct; P0C631; 16.
DR STRING; 192222.Cj0400; -.
DR PaxDb; P0C631; -.
DR PRIDE; P0C631; -.
DR EnsemblBacteria; CAL34550; CAL34550; Cj0400.
DR GeneID; 904724; -.
DR KEGG; cje:Cj0400; -.
DR PATRIC; fig|192222.6.peg.391; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_3_1_7; -.
DR OMA; YLYGVCT; -.
DR Proteomes; UP000000799; 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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Iron; Metal-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..157
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095548"
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 42
FT /note="T -> I (in Ref. 1; CAA84528)"
FT /evidence="ECO:0000305"
FT HELIX 6..22
FT /evidence="ECO:0007829|PDB:4ETS"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:4ETS"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:4ETS"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4ETS"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:4ETS"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4ETS"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4ETS"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4ETS"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4ETS"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4ETS"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:4ETS"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:4ETS"
SQ SEQUENCE 157 AA; 18054 MW; 1DCFA9A59281F1EF CRC64;
MLIENVEYDV LLERFKKILR QGGLKYTKQR EVLLKTLYHS DTHYTPESLY MEIKQAEPDL
NVGIATVYRT LNLLEEAEMV TSISFGSAGK KYELANKPHH DHMICKNCGK IIEFENPIIE
RQQALIAKEH GFKLTGHLMQ LYGVCGDCNN QKAKVKI
