SDHE_ECOLI
ID SDHE_ECOLI Reviewed; 88 AA.
AC P64559; Q2M9U4; Q46825;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=FAD assembly factor SdhE {ECO:0000303|PubMed:22474332};
DE AltName: Full=Antitoxin CptB {ECO:0000303|PubMed:22239607};
GN Name=sdhE {ECO:0000303|PubMed:22474332};
GN Synonyms=cptB {ECO:0000303|PubMed:22239607}, ygfY;
GN OrderedLocusNames=b2897, JW2865;
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=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 [2]
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 [3]
RP PRELIMINARY (INCORRECT) FUNCTION AS AN ANTITOXIN.
RC STRAIN=B / BL21-DE3, and K12 / BW25113;
RX PubMed=22239607; DOI=10.1111/j.1574-6968.2012.02496.x;
RA Masuda H., Tan Q., Awano N., Yamaguchi Y., Inouye M.;
RT "A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits
RT polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia
RT coli.";
RL FEMS Microbiol. Lett. 328:174-181(2012).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=22474332; DOI=10.1074/jbc.m111.293803;
RA McNeil M.B., Clulow J.S., Wilf N.M., Salmond G.P., Fineran P.C.;
RT "SdhE is a conserved protein required for flavinylation of succinate
RT dehydrogenase in bacteria.";
RL J. Biol. Chem. 287:18418-18428(2012).
RN [5]
RP NOT A TOXIN-ANTITOXIN SYSTEM.
RC STRAIN=K12 / BW25113;
RX PubMed=23657679; DOI=10.1099/mic.0.068510-0;
RA McNeil M.B., Iglesias-Cans M.C., Clulow J.S., Fineran P.C.;
RT "YgfX (CptA) is a multimeric membrane protein that interacts with the
RT succinate dehydrogenase assembly factor SdhE (YgfY).";
RL Microbiology 159:1352-1365(2013).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=24374335; DOI=10.1016/j.febslet.2013.12.019;
RA McNeil M.B., Hampton H.G., Hards K.J., Watson B.N., Cook G.M.,
RA Fineran P.C.;
RT "The succinate dehydrogenase assembly factor, SdhE, is required for the
RT flavinylation and activation of fumarate reductase in bacteria.";
RL FEBS Lett. 588:414-421(2014).
RN [7]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-14 AND
RP GLU-19.
RC STRAIN=K12 / RP437;
RX PubMed=26644464; DOI=10.1074/jbc.m115.690396;
RA Maklashina E., Rajagukguk S., Starbird C.A., McDonald W.H., Koganitsky A.,
RA Eisenbach M., Iverson T.M., Cecchini G.;
RT "Binding of the covalent flavin assembly factor to the flavoprotein subunit
RT of complex II.";
RL J. Biol. Chem. 291:2904-2916(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), AND SUBUNIT.
RX PubMed=15593094; DOI=10.1002/prot.20337;
RA Lim K., Doseeva V., Demirkan E.S., Pullalarevu S., Krajewski W., Galkin A.,
RA Howard A., Herzberg O.;
RT "Crystal structure of the YgfY from Escherichia coli, a protein that may be
RT involved in transcriptional regulation.";
RL Proteins 58:759-763(2005).
CC -!- FUNCTION: An FAD assembly protein, which accelerates covalent
CC attachment of the cofactor into other proteins (PubMed:22474332,
CC PubMed:26644464, PubMed:24374335). Plays an essential role in the
CC assembly of succinate dehydrogenase (SDH, respiratory complex II), an
CC enzyme complex that is a component of both the tricarboxylic acid cycle
CC and the electron transport chain, and which couples the oxidation of
CC succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to
CC ubiquinol. Required for flavinylation (covalent attachment of FAD) of
CC the flavoprotein subunit SdhA of SDH (PubMed:24374335, PubMed:26644464,
CC PubMed:22474332). Required for flavinylation of the flavoprotein
CC subunit FdrA of fumarate reductase (FDR) (PubMed:26644464). Binds 2
CC different sites on the flavoprotein target FrdA (and presumably also
CC SdhA), possibly positioning FAD and protein to facilitate the covalent
CC bond formation; covalent attachment of FAD is not required for SDH or
CC FDR complex enzyme formation (PubMed:26644464). Overexpression of this
CC protein and YgfX (formerly cptA) restores production of prodigiosin
CC antibiotic (Pig) in Serratia strains with deletions of sdhE-ygfX
CC (PubMed:22474332). {ECO:0000269|PubMed:23657679,
CC ECO:0000269|PubMed:24374335, ECO:0000269|PubMed:26644464,
CC ECO:0000305|PubMed:22474332}.
CC -!- SUBUNIT: Monomer (PubMed:15593094). Can be cross-linked to FrdA and
CC SdhA (PubMed:26644464). {ECO:0000269|PubMed:15593094,
CC ECO:0000269|PubMed:26644464}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:G4V4G2}.
CC -!- DISRUPTION PHENOTYPE: No aerobic growth on succinate, 80% reduction of
CC succinate dehydrogenase (SDH) activity (PubMed:22474332). Significantly
CC decreased anaerobic growth on glycerol fumarate medium, 70% reduction
CC in fumarate reductase activity (PubMed:24374335). Low covalent
CC attachment of FAD to FdrA or SdhA (PubMed:26644464).
CC {ECO:0000269|PubMed:22474332, ECO:0000269|PubMed:24374335,
CC ECO:0000269|PubMed:26644464}.
CC -!- SIMILARITY: Belongs to the SdhE FAD assembly factor family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the antitoxin component of a type
CC II toxin-antitoxin (TA) system (PubMed:22239607). When coexpressed with
CC cognate toxin CptA (now ygfX), the antitoxin neutralizes toxicity of
CC CptA (PubMed:22239607). Has been suggested to be a transcriptional
CC regulator (PubMed:22239607). The putative toxin, CptA (ygfX) has since
CC been shown not to be toxic in E.coli or Serratia species
CC (PubMed:23657679). {ECO:0000269|PubMed:22239607,
CC ECO:0000269|PubMed:23657679}.
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DR EMBL; U28375; AAA83078.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75935.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76962.1; -; Genomic_DNA.
DR PIR; A65074; A65074.
DR RefSeq; NP_417373.1; NC_000913.3.
DR RefSeq; WP_000354046.1; NZ_STEB01000001.1.
DR PDB; 1X6I; X-ray; 1.20 A; A/B=1-88.
DR PDB; 1X6J; X-ray; 2.00 A; A=1-88.
DR PDB; 6B58; X-ray; 2.61 A; B/D=6-84.
DR PDBsum; 1X6I; -.
DR PDBsum; 1X6J; -.
DR PDBsum; 6B58; -.
DR AlphaFoldDB; P64559; -.
DR SMR; P64559; -.
DR BioGRID; 4262342; 18.
DR BioGRID; 851704; 2.
DR IntAct; P64559; 6.
DR STRING; 511145.b2897; -.
DR jPOST; P64559; -.
DR PaxDb; P64559; -.
DR PRIDE; P64559; -.
DR EnsemblBacteria; AAC75935; AAC75935; b2897.
DR EnsemblBacteria; BAE76962; BAE76962; BAE76962.
DR GeneID; 67415218; -.
DR GeneID; 947382; -.
DR KEGG; ecj:JW2865; -.
DR KEGG; eco:b2897; -.
DR PATRIC; fig|511145.12.peg.2991; -.
DR EchoBASE; EB2885; -.
DR eggNOG; COG2938; Bacteria.
DR HOGENOM; CLU_103054_2_2_6; -.
DR InParanoid; P64559; -.
DR OMA; FEHEYDT; -.
DR PhylomeDB; P64559; -.
DR BioCyc; EcoCyc:G7510-MON; -.
DR EvolutionaryTrace; P64559; -.
DR PRO; PR:P64559; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017013; P:protein flavinylation; IDA:EcoCyc.
DR GO; GO:0034552; P:respiratory chain complex II assembly; IDA:UniProtKB.
DR GO; GO:0006105; P:succinate metabolic process; IMP:EcoCyc.
DR Gene3D; 1.10.150.250; -; 1.
DR InterPro; IPR005631; SDH.
DR InterPro; IPR036714; SDH_sf.
DR Pfam; PF03937; Sdh5; 1.
DR SUPFAM; SSF109910; SSF109910; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..88
FT /note="FAD assembly factor SdhE"
FT /id="PRO_0000214394"
FT MUTAGEN 14
FT /note="R->A: Flavinylates both FrdA and SdhA."
FT /evidence="ECO:0000269|PubMed:26644464"
FT MUTAGEN 19
FT /note="E->A: Flavinylates FrdA but not SdhA."
FT /evidence="ECO:0000269|PubMed:26644464"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:1X6I"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:1X6I"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1X6I"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:1X6I"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1X6I"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1X6I"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:1X6I"
SQ SEQUENCE 88 AA; 10547 MW; B7047D93220989DE CRC64;
MDINNKARIH WACRRGMREL DISIMPFFEH EYDSLSDDEK RIFIRLLECD DPDLFNWLMN
HGKPADAELE MMVRLIQTRN RERGPVAI
