ID   VATD_ENTFA              Reviewed;         211 AA.
AC   Q834X7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=V-type ATP synthase subunit D {ECO:0000255|HAMAP-Rule:MF_00271};
DE   AltName: Full=V-ATPase subunit D {ECO:0000255|HAMAP-Rule:MF_00271};
GN   Name=atpD {ECO:0000255|HAMAP-Rule:MF_00271}; OrderedLocusNames=EF_1500;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00271}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00271}.
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DR   EMBL; AE016830; AAO81291.1; -; Genomic_DNA.
DR   RefSeq; NP_815221.1; NC_004668.1.
DR   RefSeq; WP_002357673.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q834X7; -.
DR   SMR; Q834X7; -.
DR   STRING; 226185.EF_1500; -.
DR   DNASU; 1200403; -.
DR   EnsemblBacteria; AAO81291; AAO81291; EF_1500.
DR   KEGG; efa:EF1500; -.
DR   PATRIC; fig|226185.45.peg.2000; -.
DR   eggNOG; COG1394; Bacteria.
DR   HOGENOM; CLU_069688_2_1_9; -.
DR   OMA; SKNIMGV; -.
DR   Proteomes; UP000001415; Chromosome.
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   HAMAP; MF_00271; ATP_synth_D_arch; 1.
DR   InterPro; IPR002699; V_ATPase_D.
DR   PANTHER; PTHR11671; PTHR11671; 1.
DR   Pfam; PF01813; ATP-synt_D; 1.
DR   TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..211
FT                   /note="V-type ATP synthase subunit D"
FT                   /id="PRO_1000059157"
SQ   SEQUENCE   211 AA;  24397 MW;  5B214C81D799CFDE CRC64;
     MARLNVNPTR MELSRLKKQL TTATRGHKLL KDKQDELMRR FIALVKENNE LRIQVEQEVT
     DALSNFVLAN ATLNEAFIEE LVAIPAEKVE LEIIEQNILS VPVPKMIFDY DESVQEAPLD
     YGYVNSNSEL DQAFAKISSI LPKLLALANV EKTCQLLSKE IEKTRRRVNA LEYMTIPQLE
     ETIYYIQMKL EENERGEITR LIKIKSMNKE N