VATE_ANADF
ID VATE_ANADF Reviewed; 193 AA.
AC A7HDH2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=V-type ATP synthase subunit E;
DE AltName: Full=V-ATPase subunit E {ECO:0000255|HAMAP-Rule:MF_00311};
GN Name=atpE {ECO:0000255|HAMAP-Rule:MF_00311};
GN OrderedLocusNames=Anae109_2567;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000255|HAMAP-Rule:MF_00311}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00311}.
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DR EMBL; CP000769; ABS26768.1; -; Genomic_DNA.
DR RefSeq; WP_012097362.1; NC_009675.1.
DR AlphaFoldDB; A7HDH2; -.
DR SMR; A7HDH2; -.
DR STRING; 404589.Anae109_2567; -.
DR EnsemblBacteria; ABS26768; ABS26768; Anae109_2567.
DR KEGG; afw:Anae109_2567; -.
DR HOGENOM; CLU_1346616_0_0_7; -.
DR OrthoDB; 1966009at2; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.2320.30; -; 1.
DR HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR InterPro; IPR038495; ATPase_E_C.
DR InterPro; IPR002842; ATPase_V1_Esu.
PE 3: Inferred from homology;
KW ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW Transport.
FT CHAIN 1..193
FT /note="V-type ATP synthase subunit E"
FT /id="PRO_1000059401"
SQ SEQUENCE 193 AA; 20583 MW; C7E322FCE390B18D CRC64;
MGYPELLRVL GEEAAREARE VRAAADRECA RILSEARAAA DGARAAVLAR VREESEAHRR
ASREAIALER ERALLVERRR QLERLRLEAL ARLRGAGGPA LDAALLAELL PEAGDGPLEV
IVDPGAEAEV GRALASLDPA VAARAAVRAA PEARGGVALV AGRRVLDDTL PSRLDRAWTV
LEAEVARLLF GEG