ETFB_METME
ID ETFB_METME Reviewed; 264 AA.
AC P53570;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Electron transfer flavoprotein subunit beta;
DE Short=Beta-ETF;
DE AltName: Full=Electron transfer flavoprotein small subunit;
DE Short=ETFSS;
GN Name=etfB;
OS Methylophilus methylotrophus (Bacterium W3A1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=17;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, MASS
RP SPECTROMETRY, FUNCTION, AND SUBUNIT.
RX PubMed=7798207; DOI=10.1016/s0021-9258(18)31609-0;
RA Chen D., Swenson R.P.;
RT "Cloning, sequence analysis, and expression of the genes encoding the two
RT subunits of the methylotrophic bacterium W3A1 electron transfer
RT flavoprotein.";
RL J. Biol. Chem. 269:32120-32130(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH AMP AND TMADH, AND
RP SUBUNIT.
RX PubMed=12567183; DOI=10.1038/nsb894;
RA Leys D., Basran J., Talfournier F., Sutcliffe M.J., Scrutton N.S.;
RT "Extensive conformational sampling in a ternary electron transfer
RT complex.";
RL Nat. Struct. Biol. 10:219-225(2003).
CC -!- FUNCTION: Heterodimeric electron transfer flavoprotein that accepts
CC electrons from trimethylamine dehydrogenase (PubMed:7798207). It
CC transfers the electrons to the main respiratory chain via ETF-
CC ubiquinone oxidoreductase (ETF dehydrogenase) (Probable). EtfB binds an
CC AMP molecule that probably has a purely structural role
CC (PubMed:7798207). {ECO:0000269|PubMed:7798207, ECO:0000305}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:12567183, ECO:0000269|PubMed:7798207}.
CC -!- MASS SPECTROMETRY: Mass=28970; Mass_error=29; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:7798207};
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {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; U17242; AAA64952.1; -; Genomic_DNA.
DR PIR; A55487; A55487.
DR PDB; 1O94; X-ray; 2.00 A; C/E=1-264.
DR PDB; 1O95; X-ray; 3.70 A; C/E=1-264.
DR PDB; 1O96; X-ray; 3.10 A; A/C/E/Q=1-264.
DR PDB; 1O97; X-ray; 1.60 A; C=1-264.
DR PDB; 3CLR; X-ray; 1.90 A; C=1-264.
DR PDB; 3CLS; X-ray; 1.65 A; C=1-264.
DR PDB; 3CLT; X-ray; 2.00 A; C=1-264.
DR PDB; 3CLU; X-ray; 1.80 A; C=1-264.
DR PDBsum; 1O94; -.
DR PDBsum; 1O95; -.
DR PDBsum; 1O96; -.
DR PDBsum; 1O97; -.
DR PDBsum; 3CLR; -.
DR PDBsum; 3CLS; -.
DR PDBsum; 3CLT; -.
DR PDBsum; 3CLU; -.
DR AlphaFoldDB; P53570; -.
DR SMR; P53570; -.
DR MINT; P53570; -.
DR STRING; 1122236.KB905144_gene2341; -.
DR EvolutionaryTrace; P53570; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
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.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport;
KW Nucleotide-binding; Transport.
FT CHAIN 1..264
FT /note="Electron transfer flavoprotein subunit beta"
FT /id="PRO_0000167880"
FT BINDING 6
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O94, ECO:0007744|PDB:1O95,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 36..39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O94, ECO:0007744|PDB:1O95,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007744|PDB:1O94, ECO:0007744|PDB:1O95,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 119..122
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O94, ECO:0007744|PDB:1O95,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 127..130
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O94, ECO:0007744|PDB:1O95,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 37..52
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1O94"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1O97"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:1O94"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1O96"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:1O97"
SQ SEQUENCE 264 AA; 28899 MW; 67BC04544CECABE1 CRC64;
MKILVAVKQT AALEEDFEIR EDGMDVDEDF MMYDLNEWDD FSLEEAMKIK ESSDTDVEVV
VVSVGPDRVD ESLRKCLAKG ADRAVRVWDD AAEGSDAIVV GRILTEVIKK EAPDMVFAGV
QSSDQAYAST GISVASYLNW PHAAVVADLQ YKPGDNKAVI RRELEGGMLQ EVEINCPAVL
TIQLGINKPR YASLRGIKQA ATKPIEEVSL ADIGLSANDV GAAQSMSRVR RMYIPEKGRA
TMIEGTISEQ AAKIIQIINE FKGA
