ID   VATA_BETVU              Reviewed;         623 AA.
AC   Q39442;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=V-type proton ATPase catalytic subunit A;
DE            Short=V-ATPase subunit A;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase 69 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit alpha;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kirsch M.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar
CC       ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a
CC       variety of intracellular compartments in eukaryotic cells.
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   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC       attached to an integral membrane V0 proton pore complex (main
CC       component: the proteolipid protein).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; X98767; CAA67305.1; -; mRNA.
DR   RefSeq; NP_001290002.1; NM_001303073.1.
DR   AlphaFoldDB; Q39442; -.
DR   SMR; Q39442; -.
DR   PRIDE; Q39442; -.
DR   GeneID; 104906090; -.
DR   KEGG; bvg:104906090; -.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
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; IPR005725; ATPase_V1-cplx_asu.
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   TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN           1..623
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144575"
FT   BINDING         252..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   623 AA;  68548 MW;  DB1056924EDE93C3 CRC64;
     MPAVYGDRMT TFEDSEKESE YGYIRKVSGP VVVADGMNGA AMYELVRVGH DNLIGEIIRL
     EGDSATIQVY EETGGLTVND PVLRTHKPLS VELGPGILGN IFDGIQRPLK TIAKRSGDVY
     IPRGVSVPPL DKDTQWDFQP KKLGVGDLLT GGDLYAIVDE NSLMQHHVVL PPDAMGKITY
     IAPAGNYTIQ DTVLELEFQG VVKKFTMLQT WPVRTPRPVA SKLAADTPLL TGQRVLDALF
     PSVLGGTCAI LGAFGCGKTV ISQALSKYSN SDAVVYVGCG ERGNEMAEVL MDFPQLTMTL
     PDGREESVMK RTTLVANTSN MPVAAREASI YTGITIAEYF RDMGYNVSMM ADSGSRWAEA
     LREISGRLAE MPADSGYPAY LAARLASFYE AAGKVKCLGG PERNGSVTIV GAVSPPGGDF
     SDPVTSATLS IVQVFWGLDK KLAQRKHFPS VNWLISYSKY SGALESFYEK FDSEFIDIRT
     KAREVLQRED DLNEIVQLVG KDALAETDKI TLDTAKLLRE DYLAQNAFTA YDKFCPFYKS
     VWMMRNIIHF YNLANQAVER GAGSDGQKIT YSLIKLRLGD LFYRLVSQKF EDPAEGEDAL
     VAKFKKLNED LTAAFRNLED ETR