ID   VATA_PLAFA              Reviewed;         611 AA.
AC   Q03498;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 125.
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;
GN   Name=vapA;
OS   Plasmodium falciparum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8479458; DOI=10.1016/0166-6851(93)90056-4;
RA   Karcz S.R., Herrmann V.R., Cowman A.F.;
RT   "Cloning and characterization of a vacuolar ATPase A subunit homologue from
RT   Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 58:333-344(1993).
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; L08200; AAA29782.1; -; Genomic_DNA.
DR   PIR; A48582; A48582.
DR   RefSeq; XP_001349847.1; XM_001349811.1.
DR   AlphaFoldDB; Q03498; -.
DR   SMR; Q03498; -.
DR   EnsemblProtists; CAD52254; CAD52254; PF3D7_1311900.
DR   GeneID; 814043; -.
DR   KEGG; pfa:PF3D7_1311900; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1311900; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000415100; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_130016300; -.
DR   VEuPathDB; PlasmoDB:PfCD01_130017400; -.
DR   VEuPathDB; PlasmoDB:PfDd2_130017700; -.
DR   VEuPathDB; PlasmoDB:PfGA01_130017900; -.
DR   VEuPathDB; PlasmoDB:PfGB4_130017800; -.
DR   VEuPathDB; PlasmoDB:PfGN01_130018600; -.
DR   VEuPathDB; PlasmoDB:PfHB3_130018200; -.
DR   VEuPathDB; PlasmoDB:PfIT_130017100; -.
DR   VEuPathDB; PlasmoDB:PfKE01_130017500; -.
DR   VEuPathDB; PlasmoDB:PfKH01_130016100; -.
DR   VEuPathDB; PlasmoDB:PfKH02_130014800; -.
DR   VEuPathDB; PlasmoDB:PfML01_130015100; -.
DR   VEuPathDB; PlasmoDB:PfNF135_130016900; -.
DR   VEuPathDB; PlasmoDB:PfNF166_130017500; -.
DR   VEuPathDB; PlasmoDB:PfNF54_130017200; -.
DR   VEuPathDB; PlasmoDB:PfSD01_130018600; -.
DR   VEuPathDB; PlasmoDB:PfSN01_130014900; -.
DR   VEuPathDB; PlasmoDB:PfTG01_130017600; -.
DR   OMA; RIVKTFW; -.
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   3: Inferred from homology;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN           1..611
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144570"
FT   BINDING         244..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   611 AA;  68576 MW;  C3642BB0D895330F CRC64;
     MTKVAVEKEE PGVVYKVAGS LVIAENMSGT RMYELAKVGW NKLVGEIIRL EGNYAYIQVY
     EDTSGLSVGD PVIKTGNALS VELGPGILDN IYDGIQRPLE RIANVCGDVY IYKGIDMTSL
     DHDKQWQFYA DKKLKLNDIV TGGDIFGFVD ENKLFKEHKI MAPPNAKGRL TYIAPDGSYT
     LKDKIFELEY QGKKYTYGLS HLWPVRDPRP VLEKVTGDTL LLTGQRVLDS LFPTVQGGTC
     AIPGAFGCGK TCVSQALSKY SNSEVIIYVG CGERGNEMAE ILSDFPELTT KVDNEDVGIM
     QRTCLVANTS NMPVAAREAS IYTGITLCEY FRDMGYNATM MADSTSRWAE ALREISGRLA
     EMPADSGYPA YLGARLASFY ERAGKVKCIG SPSRIGSITI VGAVSPPGGD FSDPVTTATM
     SIVQAFWGLD KKLAQRKHFP SVNWSTSFSK YVRQLEQYFD NFDQDFLSLR QKISDILQQE
     SDLNDIVQLV GKDSLSEDQK VVMEVAKIIR EDFLQQNAFS DYDYMCPLQK TVGMMRIICH
     FYAQCLRTLQ EYDSRERKIG WGSIYNTLRP TINKITHMKF ENPKNSDEYF KKYFKALEEE
     ITVGLRNLME K