FUR_HELPY
ID FUR_HELPY Reviewed; 150 AA.
AC O25671; O32689;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ferric uptake regulation protein;
DE Short=Ferric uptake regulator;
GN Name=fur; OrderedLocusNames=HP_1027;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9503612; DOI=10.1111/j.1574-6968.1998.tb12860.x;
RA Bereswill S., Lichte F., Vey T., Fassbinder F., Kist M.;
RT "Cloning and characterization of the fur gene from Helicobacter pylori.";
RL FEMS Microbiol. Lett. 159:193-200(1998).
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; AE000511; AAD08073.1; -; Genomic_DNA.
DR EMBL; Y14394; CAA74751.1; -; Genomic_DNA.
DR PIR; C64648; C64648.
DR RefSeq; NP_207817.1; NC_000915.1.
DR RefSeq; WP_000824996.1; NC_018939.1.
DR PDB; 2XIG; X-ray; 1.85 A; A/B/C/D=1-150.
DR PDBsum; 2XIG; -.
DR AlphaFoldDB; O25671; -.
DR SMR; O25671; -.
DR STRING; 85962.C694_05315; -.
DR PaxDb; O25671; -.
DR DNASU; 899562; -.
DR EnsemblBacteria; AAD08073; AAD08073; HP_1027.
DR KEGG; hpy:HP_1027; -.
DR PATRIC; fig|85962.47.peg.1106; -.
DR eggNOG; COG0735; Bacteria.
DR OMA; YLYGVCT; -.
DR PhylomeDB; O25671; -.
DR EvolutionaryTrace; O25671; -.
DR Proteomes; UP000000429; Chromosome.
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_0000095555"
FT REGION 1..93
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 94..150
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 124
FT /note="V -> I (in Ref. 2; CAA74751)"
FT /evidence="ECO:0000305"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:2XIG"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:2XIG"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2XIG"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2XIG"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2XIG"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2XIG"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:2XIG"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2XIG"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2XIG"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2XIG"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2XIG"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2XIG"
FT STRAND 130..141
FT /evidence="ECO:0007829|PDB:2XIG"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2XIG"
SQ SEQUENCE 150 AA; 17681 MW; 9227BB71A6BD5100 CRC64;
MKRLETLESI LERLRMSIKK NGLKNSKQRE EVVSVLYRSG THLSPEEITH SIRQKDKNTS
ISSVYRILNF LEKENFICVL ETSKSGRRYE IAAKEHHDHI ICLHCGKIIE FADPEIENRQ
NEVVKKYQAK LISHDMKMFV WCKECQESEC
