FHUF_ECOLI
ID FHUF_ECOLI Reviewed; 262 AA.
AC P39405; Q2M5U9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ferric iron reductase protein FhuF;
GN Name=fhuF; Synonyms=yjjS; OrderedLocusNames=b4367, JW4331;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9990318; DOI=10.1046/j.1432-1327.1998.2581001.x;
RA Muller K., Matzanke B.F., Schunemann V., Trautwein A.X., Hantke K.;
RT "FhuF, an iron-regulated protein of Escherichia coli with a new type of
RT 2Fe-2S center.";
RL Eur. J. Biochem. 258:1001-1008(1998).
RN [5]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
CC -!- FUNCTION: Involved in the reduction of ferric iron in cytoplasmic
CC ferrioxamine B.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein.
CC -!- INDUCTION: Induced 2.4-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14003; AAA97266.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77323.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78357.1; -; Genomic_DNA.
DR PIR; S56594; S56594.
DR RefSeq; NP_418787.1; NC_000913.3.
DR RefSeq; WP_000331618.1; NZ_LN832404.1.
DR AlphaFoldDB; P39405; -.
DR SASBDB; P39405; -.
DR SMR; P39405; -.
DR BioGRID; 4262784; 6.
DR BioGRID; 853168; 14.
DR DIP; DIP-9607N; -.
DR IntAct; P39405; 18.
DR STRING; 511145.b4367; -.
DR jPOST; P39405; -.
DR PaxDb; P39405; -.
DR PRIDE; P39405; -.
DR EnsemblBacteria; AAC77323; AAC77323; b4367.
DR EnsemblBacteria; BAE78357; BAE78357; BAE78357.
DR GeneID; 948891; -.
DR KEGG; ecj:JW4331; -.
DR KEGG; eco:b4367; -.
DR PATRIC; fig|1411691.4.peg.2319; -.
DR EchoBASE; EB2480; -.
DR eggNOG; COG4114; Bacteria.
DR HOGENOM; CLU_088228_0_0_6; -.
DR OMA; HLDVVWL; -.
DR PhylomeDB; P39405; -.
DR BioCyc; EcoCyc:G7949-MON; -.
DR PRO; PR:P39405; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IDA:EcoCyc.
DR GO; GO:0033215; P:reductive iron assimilation; IDA:EcoCyc.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:EcoCyc.
DR InterPro; IPR008090; Fe_iron_reduct.
DR InterPro; IPR024726; FhuF_C.
DR InterPro; IPR022770; FhuF_domain.
DR Pfam; PF06276; FhuF; 1.
DR Pfam; PF11575; FhuF_C; 1.
DR PRINTS; PR01714; 2FE2SRDCTASE.
DR TIGRFAMs; TIGR03951; Fe_III_red_FhuF; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cell membrane; Cytoplasm; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome.
FT CHAIN 1..262
FT /note="Ferric iron reductase protein FhuF"
FT /id="PRO_0000087235"
FT BINDING 244
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9990318"
FT BINDING 245
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9990318"
FT BINDING 256
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9990318"
FT BINDING 259
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9990318"
SQ SEQUENCE 262 AA; 30113 MW; 7708E776B1BE7783 CRC64;
MAYRSAPLYE DVIWRTHLQP QDPTLAQAVR ATIAKHREHL LEFIRLDEPA PLNAMTLAQW
SSPNVLSSLL AVYSDHIYRN QPMMIRENKP LISLWAQWYI GLMVPPLMLA LLTQEKALDV
SPEHFHAEFH ETGRVACFWV DVCEDKNATP HSPQHRMETL ISQALVPVVQ ALEATGEING
KLIWSNTGYL INWYLTEMKQ LLGEATVESL RHALFFEKTL TNGEDNPLWR TVVLRDGLLV
RRTCCQRYRL PDVQQCGDCT LK