ID   FUR_STAEP               Reviewed;         138 AA.
AC   P0C0P3; P54204;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-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   Staphylococcus epidermidis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BN 280;
RX   PubMed=8764488; DOI=10.1111/j.1574-6968.1996.tb08345.x;
RA   Heidrich C., Hantke K., Bierbaum G., Sahl H.-G.;
RT   "Identification and analysis of a gene encoding a Fur-like protein of
RT   Staphylococcus epidermidis.";
RL   FEMS Microbiol. Lett. 140:253-259(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; X97011; CAA65733.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C0P3; -.
DR   SMR; P0C0P3; -.
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..138
FT                   /note="Ferric uptake regulation protein"
FT                   /id="PRO_0000095579"
FT   REGION          1..85
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          86..138
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  16174 MW;  4199D479823169DF CRC64;
     MNTNDAIKIL KDNGLKYTDK RKDMLDIFVE EDKYLNAKHI QQKMDKDYPG ISFDTVYRNL
     HLFKDLGIIE STELEGEMKF RIACTNHHHH HFICENCGDT KVIDFCPIEQ IKQYLPNVTI
     HTHKLEVYGV CESCQKNA