SDHE_FRATT
ID SDHE_FRATT Reviewed; 95 AA.
AC Q5NFS4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=FAD assembly factor SdhE;
GN Name=sdhE; OrderedLocusNames=FTT_1151c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
CC -!- FUNCTION: An FAD assembly protein, which accelerates covalent
CC attachment of the cofactor into other proteins. Plays an essential role
CC in the assembly of succinate dehydrogenase (SDH, respiratory complex
CC II), an enzyme complex that is a component of both the tricarboxylic
CC acid cycle and the electron transport chain, and which couples the
CC oxidation of succinate to fumarate with the reduction of ubiquinone
CC (coenzyme Q) to ubiquinol. Required for flavinylation (covalent
CC attachment of FAD) of the flavoprotein subunit SdhA of SDH and other
CC flavinylated proteins as well. {ECO:0000250|UniProtKB:G4V4G2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:G4V4G2}.
CC -!- SIMILARITY: Belongs to the SdhE FAD assembly factor family.
CC {ECO:0000305}.
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; AJ749949; CAG45784.1; -; Genomic_DNA.
DR RefSeq; WP_003018632.1; NZ_CP010290.1.
DR RefSeq; YP_170118.1; NC_006570.2.
DR AlphaFoldDB; Q5NFS4; -.
DR SMR; Q5NFS4; -.
DR STRING; 177416.FTT_1151c; -.
DR DNASU; 3191681; -.
DR EnsemblBacteria; CAG45784; CAG45784; FTT_1151c.
DR GeneID; 60806432; -.
DR KEGG; ftu:FTT_1151c; -.
DR eggNOG; COG2938; Bacteria.
DR OMA; FEHEYDT; -.
DR Proteomes; UP000001174; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..95
FT /note="FAD assembly factor SdhE"
FT /id="PRO_0000214398"
SQ SEQUENCE 95 AA; 11321 MW; 70E74452CA6CA4FA CRC64;
MLIKNNDLIF SSVDKIKYSA RRGMLELDII LAPYLNNCYM HEDLANKKLF VEFLTSEDSD
MFDWLFKGVT PPQRYQQLID KIIKEKKKFN QTKLK