FUR_NEIMA
ID FUR_NEIMA Reviewed; 144 AA.
AC P0A0S7; A1INS7; Q57298;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; OrderedLocusNames=NMA0064;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(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 Regulates the expression of the fbp protein (By similarity).
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; AL157959; CAM07384.1; -; Genomic_DNA.
DR PIR; G81226; G81226.
DR RefSeq; WP_002218609.1; NC_003116.1.
DR AlphaFoldDB; P0A0S7; -.
DR SMR; P0A0S7; -.
DR PRIDE; P0A0S7; -.
DR EnsemblBacteria; CAM07384; CAM07384; NMA0064.
DR GeneID; 61282203; -.
DR KEGG; nma:NMA0064; -.
DR HOGENOM; CLU_096072_3_3_4; -.
DR OMA; HDHVILT; -.
DR BioCyc; NMEN122587:NMA_RS00325-MON; -.
DR Proteomes; UP000000626; 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; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..144
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095564"
FT REGION 1..86
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 87..144
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 144 AA; 16411 MW; B37489E92856AC02 CRC64;
MEKFNNIAQL KDSGLKVTGP RLKILDLFET HAEEHLSAED VYRILLEEGV EIGVATIYRV
LTQFEQAGIL QRHHFETGKA VYELDKGDHH DHIVCVKCGE VTEFHNPEIE ALQDKIAEEN
GYRIVDHALY MYGVCSDCQA KGKR