ID   VATA_ENTFA              Reviewed;         593 AA.
AC   Q834X9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=V-type ATP synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=EF_1498;
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. The V-type alpha chain is a catalytic subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00309};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO81289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016830; AAO81289.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_815219.1; NC_004668.1.
DR   RefSeq; WP_002371187.1; NC_004668.1.
DR   AlphaFoldDB; Q834X9; -.
DR   SMR; Q834X9; -.
DR   STRING; 226185.EF_1498; -.
DR   PRIDE; Q834X9; -.
DR   EnsemblBacteria; AAO81289; AAO81289; EF_1498.
DR   GeneID; 60893805; -.
DR   KEGG; efa:EF1498; -.
DR   PATRIC; fig|226185.45.peg.2002; -.
DR   eggNOG; COG1155; Bacteria.
DR   HOGENOM; CLU_008162_3_1_9; -.
DR   OMA; RIVKTFW; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
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:UniProtKB-EC.
DR   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022878; V-ATPase_asu.
DR   PANTHER; PTHR43607; PTHR43607; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..593
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000322466"
FT   BINDING         232..239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   593 AA;  65069 MW;  9C36A89A84C4442C CRC64;
     MQIGKIVKVS GPLILAENMS DASIQDICHV GDLGVIGEII EMRGDVASIQ VYEETTGIGP
     GEPVISTGEP LSVELAPGLI AEMFDGIQRP LDTFQEVTHS NFLGRGVKID ALDREKKWTF
     EPTVAVGEEV SAGDIVGVVQ ETPIIQHKIM VPFGVSGTIA EIKAGDFAID ETVYSVETAK
     GTESFSMMQK WPVRRGRPIL EKLSPKVPMV TGQRVIDTFF PITKGGAAAV PGPFGAGKTV
     VQHQIAKWAD VDLVVYVGCG ERGNEMTDVL NEFPELIDPT TGESLMNRTI LIANTSNMPV
     AAREASIYTG ITIAEYFRDM GYSVAIMADS TSRWAEALRE MSGRLEEMPG DEGYPAYLGS
     RLAEYYERAG QVIALGKDHR EGSITAISAV SPSGGDISEP VTQNTLRVVK VFWGLDSQLA
     QKRHFPSINW LQSYSLYSTE VGQYLDLELQ GNWAAMVAEG MRILQEESQL EEIVRLVGID
     SLSDKDRLTL ETAKSLREDY LQQNAFDDVD TFTSRTKQAK MLQLILTFGE EGQKALSLGT
     YFSELMAGTV EIRDRIARSK YLPEEELEKL DRLQAEIKTT IKEIIAEGGM TND