FUR_BACSU
ID FUR_BACSU Reviewed; 149 AA.
AC P54574;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; Synonyms=yqkL; OrderedLocusNames=BSU23520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 103 AND 111.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9701813; DOI=10.1046/j.1365-2958.1998.00921.x;
RA Bsat N., Herbig A., Casillas-Martinez L., Setlow P., Helmann J.D.;
RT "Bacillus subtilis contains multiple Fur homologues: identification of the
RT iron uptake (Fur) and peroxide regulon (PerR) repressors.";
RL Mol. Microbiol. 29:189-198(1998).
CC -!- FUNCTION: Iron uptake repressor. Acts on the transcription of ferri-
CC siderophore uptake genes.
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; D84432; BAA12648.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14284.2; -; Genomic_DNA.
DR PIR; E69967; E69967.
DR RefSeq; NP_390233.2; NC_000964.3.
DR RefSeq; WP_003223972.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54574; -.
DR SMR; P54574; -.
DR STRING; 224308.BSU23520; -.
DR PaxDb; P54574; -.
DR PRIDE; P54574; -.
DR EnsemblBacteria; CAB14284; CAB14284; BSU_23520.
DR GeneID; 64304133; -.
DR GeneID; 938727; -.
DR KEGG; bsu:BSU23520; -.
DR PATRIC; fig|224308.179.peg.2564; -.
DR eggNOG; COG0735; Bacteria.
DR InParanoid; P54574; -.
DR OMA; HDHVILT; -.
DR PhylomeDB; P54574; -.
DR BioCyc; BSUB:BSU23520-MON; -.
DR PRO; PR:P54574; -.
DR Proteomes; UP000001570; Chromosome.
DR CollecTF; EXPREG_00000b40; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CollecTF.
DR GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IBA:GO_Central.
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 Cytoplasm; DNA-binding; Iron; Metal-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..149
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095589"
FT REGION 6..91
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 92..147
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 97
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 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 103
FT /note="C -> F (in Ref. 1; BAA12648)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="E -> G (in Ref. 1; BAA12648)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 17428 MW; F6ACD6F0F397744D CRC64;
MENRIDRIKK QLHSSSYKLT PQREATVRVL LENEEDHLSA EDVYLLVKEK SPEIGLATVY
RTLELLTELK VVDKINFGDG VSRYDLRKEG AAHFHHHLVC MECGAVDEIE EDLLEDVEEI
IERDWKFKIK DHRLTFHGIC HRCNGKETE
