YTFE_ECOLI
ID YTFE_ECOLI Reviewed; 220 AA.
AC P69506; P39313; Q2M696;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Iron-sulfur cluster repair protein YtfE;
DE AltName: Full=Regulator of cell morphogenesis and NO signaling;
DE Short=RCMNS;
GN Name=ytfE; OrderedLocusNames=b4209, JW4167;
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 INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / ATCC 23716 / DSM 498 / CIP 110067 / IMG 1711;
RX PubMed=15546870; DOI=10.1074/jbc.m411070200;
RA Justino M.C., Vicente J.B., Teixeira M., Saraiva L.M.;
RT "New genes implicated in the protection of anaerobically grown Escherichia
RT coli against nitric oxide.";
RL J. Biol. Chem. 280:2636-2643(2005).
RN [5]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND IRON-BINDING.
RC STRAIN=K12 / ATCC 23716 / DSM 498 / CIP 110067 / IMG 1711;
RX PubMed=16553864; DOI=10.1111/j.1574-6968.2006.00179.x;
RA Justino M.C., Almeida C.C., Goncalves V.L., Teixeira M., Saraiva L.M.;
RT "Escherichia coli YtfE is a di-iron protein with an important function in
RT assembly of iron-sulphur clusters.";
RL FEMS Microbiol. Lett. 257:278-284(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / ATCC 23716 / DSM 498 / CIP 110067 / IMG 1711;
RX PubMed=17289666; DOI=10.1074/jbc.m610656200;
RA Justino M.C., Almeida C.C., Teixeira M., Saraiva L.M.;
RT "Escherichia coli di-iron YtfE protein is necessary for the repair of
RT stress-damaged iron-sulfur clusters.";
RL J. Biol. Chem. 282:10352-10359(2007).
RN [7]
RP FUNCTION, SUBUNIT, AND IRON-BINDING.
RX PubMed=18357473; DOI=10.1007/s00775-008-0362-y;
RA Todorovic S., Justino M.C., Wellenreuther G., Hildebrandt P., Murgida D.H.,
RA Meyer-Klaucke W., Saraiva L.M.;
RT "Iron-sulfur repair YtfE protein from Escherichia coli: structural
RT characterization of the di-iron center.";
RL J. Biol. Inorg. Chem. 13:765-770(2008).
CC -!- FUNCTION: Di-iron-containing protein involved in the repair of iron-
CC sulfur clusters damaged by oxidative and nitrosative stress conditions.
CC {ECO:0000269|PubMed:16553864, ECO:0000269|PubMed:17289666,
CC ECO:0000269|PubMed:18357473}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18357473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by nitric oxide. Negatively regulated by Fnr and
CC Fur, but no obvious Fnr or Fur binding sites were found, suggesting
CC that this regulation could be indirect. {ECO:0000269|PubMed:15546870,
CC ECO:0000269|PubMed:16553864}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a severe growth impairment under
CC nitrosative and oxidative stress conditions. Mutation increases the
CC sensitivity of the bacterium to iron starvation, increases the
CC intracellular levels of free iron, and decreases the activity of
CC several iron-sulfur-containing proteins. {ECO:0000269|PubMed:15546870,
CC ECO:0000269|PubMed:16553864, ECO:0000269|PubMed:17289666}.
CC -!- SIMILARITY: Belongs to the RIC family. YtfE subfamily. {ECO:0000305}.
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DR EMBL; U14003; AAA97105.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77166.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78210.1; -; Genomic_DNA.
DR PIR; S56434; S56434.
DR RefSeq; NP_418630.1; NC_000913.3.
DR RefSeq; WP_000331456.1; NZ_STEB01000013.1.
DR PDB; 5FNN; X-ray; 2.09 A; A/B=1-220.
DR PDB; 5FNP; X-ray; 1.80 A; A/B=1-220.
DR PDB; 5FNY; X-ray; 2.01 A; A/B=1-220.
DR PDB; 7BE8; X-ray; 2.02 A; A/B=1-220.
DR PDB; 7BHA; X-ray; 2.19 A; A/B=2-220.
DR PDB; 7BHB; X-ray; 2.36 A; A/B=2-220.
DR PDB; 7BHC; X-ray; 1.87 A; A/B=2-220.
DR PDBsum; 5FNN; -.
DR PDBsum; 5FNP; -.
DR PDBsum; 5FNY; -.
DR PDBsum; 7BE8; -.
DR PDBsum; 7BHA; -.
DR PDBsum; 7BHB; -.
DR PDBsum; 7BHC; -.
DR AlphaFoldDB; P69506; -.
DR SMR; P69506; -.
DR BioGRID; 4263431; 77.
DR DIP; DIP-35833N; -.
DR IntAct; P69506; 1.
DR STRING; 511145.b4209; -.
DR jPOST; P69506; -.
DR PaxDb; P69506; -.
DR PRIDE; P69506; -.
DR EnsemblBacteria; AAC77166; AAC77166; b4209.
DR EnsemblBacteria; BAE78210; BAE78210; BAE78210.
DR GeneID; 66671871; -.
DR GeneID; 948724; -.
DR KEGG; ecj:JW4167; -.
DR KEGG; eco:b4209; -.
DR PATRIC; fig|1411691.4.peg.2492; -.
DR EchoBASE; EB2398; -.
DR eggNOG; COG2846; Bacteria.
DR HOGENOM; CLU_076075_2_0_6; -.
DR InParanoid; P69506; -.
DR OMA; ACTTWRV; -.
DR PhylomeDB; P69506; -.
DR BioCyc; EcoCyc:G7866-MON; -.
DR PRO; PR:P69506; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IDA:EcoCyc.
DR GO; GO:0030091; P:protein repair; IDA:EcoCyc.
DR GO; GO:0051409; P:response to nitrosative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01606; RIC_YtfE; 1.
DR InterPro; IPR023742; FeS-repair_YftE.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR019903; RIC_family.
DR PANTHER; PTHR36438; PTHR36438; 1.
DR Pfam; PF01814; Hemerythrin; 1.
DR Pfam; PF04405; ScdA_N; 1.
DR TIGRFAMs; TIGR03652; FeS_repair_RIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Iron; Metal-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..220
FT /note="Iron-sulfur cluster repair protein YtfE"
FT /id="PRO_0000213049"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:5FNP"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:5FNP"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7BHA"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 84..104
FT /evidence="ECO:0007829|PDB:5FNP"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5FNP"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:7BHB"
FT HELIX 115..135
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 150..173
FT /evidence="ECO:0007829|PDB:5FNP"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 185..210
FT /evidence="ECO:0007829|PDB:5FNP"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:5FNP"
SQ SEQUENCE 220 AA; 24883 MW; CC81A560EDA6A03B CRC64;
MAYRDQPLGE LALSIPRASA LFRKYDMDYC CGGKQTLARA AARKELDVEV IEAELAKLAE
QPIEKDWRSA PLAEIIDHII VRYHDRHREQ LPELILQATK VERVHADKPS VPKGLTKYLT
MLHEELSSHM MKEEQILFPM IKQGMGSQAM GPISVMESEH DEAGELLEVI KHTTNNVTPP
PEACTTWKAM YNGINELIDD LMDHISLENN VLFPRALAGE
