ID   ETFB_SYNWW              Reviewed;         252 AA.
AC   Q0AZ34;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Electron transfer flavoprotein subunit beta {ECO:0000303|PubMed:23468890};
GN   Name=etfB {ECO:0000303|PubMed:23468890};
GN   OrderedLocusNames=Swol_0696 {ECO:0000312|EMBL:ABI68020.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=19648244; DOI=10.1128/jb.01605-08;
RA   Mueller N., Schleheck D., Schink B.;
RT   "Involvement of NADH:acceptor oxidoreductase and butyryl coenzyme A
RT   dehydrogenase in reversed electron transport during syntrophic butyrate
RT   oxidation by Syntrophomonas wolfei.";
RL   J. Bacteriol. 191:6167-6177(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
RP   FUNCTION, AND PATHWAY.
RX   PubMed=23468890; DOI=10.1371/journal.pone.0056905;
RA   Schmidt A., Mueller N., Schink B., Schleheck D.;
RT   "A proteomic view at the biochemistry of syntrophic butyrate oxidation in
RT   Syntrophomonas wolfei.";
RL   PLoS ONE 8:E56905-E56905(2013).
CC   -!- FUNCTION: Part of an electron transfer flavoprotein involved in
CC       syntrophic growth of S.wolfei with butyrate. Probably receives
CC       electrons from butyryl-CoA dehydrogenases, and transfers them to the
CC       membrane-bound quinone oxidoreductase Swol_0698.
CC       {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}.
CC   -!- COFACTOR:
CC       Name=AMP; Xref=ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:P13804};
CC       Note=Binds 1 AMP per subunit. {ECO:0000250|UniProtKB:P13804};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000250|UniProtKB:P13804}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23468890}.
CC   -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at
CC       protein level) (PubMed:19648244, PubMed:23468890). Seems to be
CC       constitutively expressed (PubMed:23468890).
CC       {ECO:0000269|PubMed:19648244, ECO:0000269|PubMed:23468890}.
CC   -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {ECO:0000305}.
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DR   EMBL; CP000448; ABI68020.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0AZ34; -.
DR   SMR; Q0AZ34; -.
DR   STRING; 335541.Swol_0696; -.
DR   EnsemblBacteria; ABI68020; ABI68020; Swol_0696.
DR   KEGG; swo:Swol_0696; -.
DR   eggNOG; COG2086; Bacteria.
DR   HOGENOM; CLU_060196_1_0_9; -.
DR   OMA; YNGGMVP; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01714; ETF_beta; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR012255; ETF_b.
DR   InterPro; IPR033948; ETF_beta_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21294; PTHR21294; 1.
DR   Pfam; PF01012; ETF; 1.
DR   PIRSF; PIRSF000090; Beta-ETF; 1.
DR   SMART; SM00893; ETF; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Electron transport; Fatty acid metabolism; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..252
FT                   /note="Electron transfer flavoprotein subunit beta"
FT                   /id="PRO_0000442218"
SQ   SEQUENCE   252 AA;  26280 MW;  93D8CE68B7862732 CRC64;
     MNLKVLVCVK QTFDTEAKIE LKDGKIADAG INLIINPYDE VAVEGAIQLK EKGVAKEIVV
     VAAGSDKAMD AIRTALAMGA DRGILVQQDT AADEFARAVA LAEAIKGENP DIILAGHVAA
     DDGSSQVPTR VAEILGLPHV NVITAVEIAG GKATCTSEAD GGTQVTEVSL PAVISSQVSW
     NEPRYPSMKG IMAAKKKPVA TAAAAAAESK VKILEFSLPP AKAAGIKIED EPEVCATKLA
     EWMKNTVKVE VK