ID   FUR_NEIMC               Reviewed;         144 AA.
AC   P0A0S9; Q57298;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Ferric uptake regulation protein;
DE            Short=Ferric uptake regulator;
GN   Name=fur;
OS   Neisseria meningitidis serogroup C.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=135720;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FAM20 / Serogroup C;
RX   PubMed=8196544; DOI=10.1111/j.1365-2958.1994.tb00350.x;
RA   Thomas C.E., Sparling P.F.;
RT   "Identification and cloning of a fur homologue from Neisseria
RT   meningitidis.";
RL   Mol. Microbiol. 11:725-737(1994).
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.
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; L19777; AAA21816.1; -; Genomic_DNA.
DR   PIR; S54164; S54164.
DR   AlphaFoldDB; P0A0S9; -.
DR   SMR; P0A0S9; -.
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_0000095566"
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;  16384 MW;  B36153D6DB7C8502 CRC64;
     MEKFSNIAQL KDSGLKVTGP RLKILDLFET HAEEHLSAED VYRILLEEGV EIGVATIYRV
     LTQFEQAGIL QRHHFETGKA VYELDKGDHH DHIVCVKCGE VTEFHNPEIE ALQDKIAEEN
     GYRIVDHALY MYGVCSDCQA KGKR