FUR_VIBCH
ID FUR_VIBCH Reviewed; 150 AA.
AC P0C6C8; P33087; Q9KQ94;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-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=VC_2106;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Fur acts as a repressor, employing Fe(2+) as a cofactor to
CC bind the operator of the iron transport operon. {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; AE003852; AAF95252.1; -; Genomic_DNA.
DR PIR; A82118; A82118.
DR RefSeq; NP_231738.1; NC_002505.1.
DR RefSeq; WP_001282826.1; NZ_LT906614.1.
DR PDB; 2W57; X-ray; 2.60 A; A/B=1-150.
DR PDBsum; 2W57; -.
DR AlphaFoldDB; P0C6C8; -.
DR SMR; P0C6C8; -.
DR STRING; 243277.VC_2106; -.
DR DNASU; 2613362; -.
DR EnsemblBacteria; AAF95252; AAF95252; VC_2106.
DR KEGG; vch:VC_2106; -.
DR PATRIC; fig|243277.26.peg.2012; -.
DR eggNOG; COG0735; Bacteria.
DR HOGENOM; CLU_096072_3_3_6; -.
DR OMA; MKHFAIF; -.
DR BioCyc; VCHO:VC2106-MON; -.
DR EvolutionaryTrace; P0C6C8; -.
DR Proteomes; UP000000584; Chromosome 1.
DR CollecTF; EXPREG_000008b0; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:1900705; P:negative regulation of siderophore biosynthetic process; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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 3D-structure; Cytoplasm; DNA-binding; Iron; Metal-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc.
FT CHAIN 1..150
FT /note="Ferric uptake regulation protein"
FT /id="PRO_0000095585"
FT REGION 1..84
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 85..143
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 90
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 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:2W57"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:2W57"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2W57"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2W57"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2W57"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:2W57"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2W57"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2W57"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2W57"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2W57"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2W57"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2W57"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:2W57"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:2W57"
SQ SEQUENCE 150 AA; 16912 MW; E03CDE8990F465FE CRC64;
MSDNNQALKD AGLKVTLPRL KILEVLQQPE CQHISAEELY KKLIDLGEEI GLATVYRVLN
QFDDAGIVTR HHFEGGKSVF ELSTQHHHDH LVCLDCGEVI EFSDDVIEQR QKEIAAKYNV
QLTNHSLYLY GKCGSDGSCK DNPNAHKPKK
