SDHE_SERS3
ID SDHE_SERS3 Reviewed; 88 AA.
AC G4V4G2;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=FAD assembly factor SdhE {ECO:0000303|PubMed:22474332};
DE AltName: Full=Antitoxin CptB {ECO:0000250|UniProtKB:P64559};
DE AltName: Full=DUF339 protein {ECO:0000303|PubMed:22474332};
GN Name=sdhE {ECO:0000303|PubMed:22474332}; Synonyms=cptB, ygfY;
GN ORFNames=Ser39006_01161;
OS Serratia sp. (strain ATCC 39006).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia; unclassified Serratia.
OX NCBI_TaxID=104623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, FAD-BINDING, PATHWAY, SUBUNIT,
RP SUBCELLULAR LOCATION, INDUCTION, MASS SPECTROMETRY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-16.
RC STRAIN=ATCC 39006 / SC 11482;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=24336377; DOI=10.1128/genomea.01039-13;
RA Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., Cossyleon D.,
RA McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., Stanton J.A.,
RA Brugger K., Brown S.D., Salmond G.P.;
RT "Draft genome sequence of Serratia sp. strain ATCC 39006, a model bacterium
RT for analysis of the biosynthesis and regulation of prodigiosin, a
RT carbapenem, and gas vesicles.";
RL Genome Announc. 1:E01039-E01039(2013).
RN [3]
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 39006 / SC 11482;
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 [4]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-15; GLY-16;
RP GLU-19; ASP-21; PHE-27 AND ASP-51.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=24070374; DOI=10.1021/bi401006a;
RA McNeil M.B., Fineran P.C.;
RT "The conserved RGxxE motif of the bacterial FAD assembly factor SdhE is
RT required for succinate dehydrogenase flavinylation and activity.";
RL Biochemistry 52:7628-7640(2013).
RN [5]
RP FUNCTION, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-15; GLY-16; GLU-19; ASP-21; PHE-27 AND ASP-51.
RC STRAIN=ATCC 39006 / SC 11482;
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 [6]
RP FUNCTION.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=26399411; DOI=10.1007/s00253-015-6972-8;
RA Kiefler I., Bringer S., Bott M.;
RT "SdhE-dependent formation of a functional Acetobacter pasteurianus
RT succinate dehydrogenase in Gluconobacter oxydans--a first step toward a
RT complete tricarboxylic acid cycle.";
RL Appl. Microbiol. Biotechnol. 99:9147-9160(2015).
CC -!- FUNCTION: An FAD assembly protein, which accelerates covalent
CC attachment of the cofactor into other proteins (PubMed:24070374,
CC PubMed:24374335). Plays an essential role in the assembly of succinate
CC dehydrogenase (SDH, respiratory complex II), an enzyme complex that is
CC a component of both the tricarboxylic acid cycle and the electron
CC transport chain, and which couples the oxidation of succinate to
CC fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol.
CC Required for flavinylation (covalent attachment of FAD) of the
CC flavoprotein subunit SdhA of SDH (PubMed:22474332). Required for
CC flavinylation of the flavoprotein subunit FdrA of fumarate reductase
CC (FDR) (PubMed:24374335). Flavinylation of SDH and FDR occurs in a
CC similar but not identical manner, as site-specific mutations display
CC subtle differences between them (PubMed:24070374, PubMed:24374335).
CC Flavinylates SdhA in vivo in the absence of the other SDH subunits;
CC SdhE mutants that do not flavinylate also interfere with wild-type
CC activity in a possible dominant-negative fashion (PubMed:24070374).
CC Weakly binds to FAD and facilitates its binding to SdhA
CC (PubMed:22474332). Required for production of prodigiosin antibiotic
CC (Pig); overproduction of SdhE in a deletion mutant leads to decreased
CC synthesis of Pig compared to wild-type (PubMed:22474332). Capable of
CC flavinylating A.pasteurianus SdhA when the SDH operon and this gene are
CC expressed in G.oxydans; flavinylation of SdhA is detected only in the
CC presence of sdhE (PubMed:26399411). {ECO:0000269|PubMed:22474332,
CC ECO:0000269|PubMed:24070374, ECO:0000269|PubMed:24374335,
CC ECO:0000269|PubMed:26399411}.
CC -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC {ECO:0000269|PubMed:22474332}.
CC -!- SUBUNIT: Monomer (By similarity). Makes weak or transient interactions
CC with SdhA (PubMed:22474332, PubMed:24070374). Interacts with YgfX
CC (PubMed:23657679). Interacts with FrdA (PubMed:24374335).
CC {ECO:0000250|UniProtKB:P64559, ECO:0000269|PubMed:22474332,
CC ECO:0000269|PubMed:23657679, ECO:0000269|PubMed:24070374,
CC ECO:0000269|PubMed:24374335}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22474332}.
CC -!- INDUCTION: Transcribed under both aerobic (with succinate or glucose)
CC and anaerobic (with glycerol with or without fumarate) conditions
CC (PubMed:24374335). Part of the sdhE-ygfX operon (PubMed:22474332).
CC {ECO:0000269|PubMed:22474332, ECO:0000269|PubMed:24374335}.
CC -!- MASS SPECTROMETRY: Mass=11884.7; Method=MALDI; Note=Includes the mass
CC of an N-terminal His tag.; Evidence={ECO:0000269|PubMed:22474332};
CC -!- MASS SPECTROMETRY: Mass=12679.4; Method=MALDI; Note=Includes the mass
CC of an N-terminal His tag plus FAD.;
CC Evidence={ECO:0000269|PubMed:22474332};
CC -!- DISRUPTION PHENOTYPE: Pleiotropic effects (PubMed:22474332). Under
CC aerobic conditions no growth on succinate, 90% reduction of succinate
CC dehydrogenase (SDH) activity, no incorporation of FAD into SDH, however
CC the SHD enzyme complex forms stably, more SdhA is incorporated into the
CC membrane (PubMed:22474332, PubMed:24070374). Decreased aerobic growth
CC rate in rich medium (LB) (PubMed:22474332, PubMed:23657679). Partial
CC growth defect during anaerobic growth on glycerol fumarate medium;
CC greatly decreased incorporation of FAD into FDR (PubMed:24374335).
CC During aerobic growth 50% decreased synthesis of prodigiosin
CC antibiotic, decreased transcription of flavoprotein desaturase PigA
CC (PubMed:22474332). During aerobic growth decreased production of
CC cellulase and pectin lyase, reduced swimming motility, reduced
CC virulence in potato infection assays, reduced N-acyl homoserine lacton
CC production, abolition of beta-lactam antibiotic synthesis
CC (PubMed:22474332). {ECO:0000269|PubMed:22474332,
CC ECO:0000269|PubMed:23657679, ECO:0000269|PubMed:24070374,
CC ECO:0000269|PubMed:24374335}.
CC -!- SIMILARITY: Belongs to the SdhE FAD assembly factor family.
CC {ECO:0000305}.
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DR EMBL; HE580156; CCD22035.1; -; Genomic_DNA.
DR EMBL; CP025084; ESN63753.1; -; Genomic_DNA.
DR RefSeq; WP_021014431.1; NZ_CP025085.1.
DR AlphaFoldDB; G4V4G2; -.
DR SMR; G4V4G2; -.
DR IntAct; G4V4G2; 1.
DR MINT; G4V4G2; -.
DR STRING; 104623.Ser39006_01161; -.
DR eggNOG; COG2938; Bacteria.
DR OrthoDB; 2055100at2; -.
DR UniPathway; UPA01072; -.
DR Proteomes; UP000017700; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034552; P:respiratory chain complex II assembly; IDA:UniProtKB.
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 Antibiotic biosynthesis; Chaperone; Cytoplasm; FAD; Flavoprotein;
KW Reference proteome.
FT CHAIN 1..88
FT /note="FAD assembly factor SdhE"
FT /id="PRO_0000438885"
FT MUTAGEN 15
FT /note="R->A: Partially restores aerobic growth of deletion
FT on succinate, less growth in LB, slightly decreased SDH
FT activity, protein expressed at low levels. Wild-type
FT flavinylation of SdhA in vivo, protein still interacts with
FT SdhA. Does not restore anaerobic growth in E.coli to an
FT sdhE deletion, FrdA from Serratia is flavinated to near
FT wild-type levels."
FT /evidence="ECO:0000269|PubMed:24070374,
FT ECO:0000269|PubMed:24374335"
FT MUTAGEN 16
FT /note="G->A: No change from wild-type."
FT /evidence="ECO:0000269|PubMed:24070374,
FT ECO:0000269|PubMed:24374335"
FT MUTAGEN 16
FT /note="G->R: Binds decreased amounts of FAD. Does not
FT restore aerobic growth of deletion on succinate, less
FT growth in LB, does not restore SDH activity. No
FT flavinylation of SdhA in vivo; protein has wild-type
FT secondary structure and still interacts with SdhA. Impairs
FT growth and SDH activity on succinate in the presence of
FT wild-type SdhE. Does not restore anaerobic growth in E.coli
FT to an sdhE deletion, does not flavinate FrdA from Serratia
FT but still interacts with FrdA."
FT /evidence="ECO:0000269|PubMed:22474332,
FT ECO:0000269|PubMed:24070374, ECO:0000269|PubMed:24374335"
FT MUTAGEN 19
FT /note="E->A: Does not restore aerobic growth of deletion on
FT succinate, less growth in LB, does not restore SDH
FT activity. Greatly reduced flavinylation of SdhA in vivo;
FT protein has wild-type secondary structure and still
FT interacts with SdhA. Greatly impairs growth and SDH
FT activity on succinate in the presence of wild-type SdhE.
FT Fully restores anaerobic growth in E.coli to an sdhE
FT deletion, FrdA from Serratia is flavinated to near wild-
FT type levels."
FT /evidence="ECO:0000269|PubMed:24070374,
FT ECO:0000269|PubMed:24374335"
FT MUTAGEN 19
FT /note="E->D: Restores aerobic growth of deletion on
FT succinate, does not impair growth on succinate in the
FT presence of wild-type SdhE."
FT /evidence="ECO:0000269|PubMed:24070374"
FT MUTAGEN 21
FT /note="D->A: No change from wild-type."
FT /evidence="ECO:0000269|PubMed:24070374,
FT ECO:0000269|PubMed:24374335"
FT MUTAGEN 27
FT /note="F->A: No change from wild-type."
FT /evidence="ECO:0000269|PubMed:24070374,
FT ECO:0000269|PubMed:24374335"
FT MUTAGEN 51
FT /note="D->A: No change from wild-type."
FT /evidence="ECO:0000269|PubMed:24070374,
FT ECO:0000269|PubMed:24374335"
SQ SEQUENCE 88 AA; 10487 MW; 77CC2E0E8DC3C23C CRC64;
MDIDNKPRIH WACRRGMREL DISIMPFFEH DYDTLSDDDK RNFIRLLQCD DPDLFNWLMN
HGEPTDQGLK HMVSLIQTRN KNRGPVAM
