ID   VATA_PLAF7              Reviewed;         611 AA.
AC   Q76NM6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
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; ORFNames=PF13_0065;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA   Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA   Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
RN   [3]
RP   SYNTHESIS OF 446-478, AND POSSIBLE CANDIDATE MALARIA EPITOPE.
RX   PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA   Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA   Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA   Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT   "Rapid identification of malaria vaccine candidates based on alpha-helical
RT   coiled coil protein motif.";
RL   PLoS ONE 2:E645-E645(2007).
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   -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC       determined by epitope response in sera.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; AL844509; CAD52254.1; -; Genomic_DNA.
DR   RefSeq; XP_001349847.1; XM_001349811.1.
DR   AlphaFoldDB; Q76NM6; -.
DR   SMR; Q76NM6; -.
DR   STRING; 5833.PF13_0065; -.
DR   DrugBank; DB11638; Artenimol.
DR   PRIDE; Q76NM6; -.
DR   EnsemblProtists; CAD52254; CAD52254; PF3D7_1311900.
DR   GeneID; 814043; -.
DR   KEGG; pfa:PF3D7_1311900; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1311900; -.
DR   HOGENOM; CLU_008162_3_1_1; -.
DR   InParanoid; Q76NM6; -.
DR   OMA; RIVKTFW; -.
DR   PhylomeDB; Q76NM6; -.
DR   Reactome; R-PFA-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-PFA-77387; Insulin receptor recycling.
DR   Reactome; R-PFA-917977; Transferrin endocytosis and recycling.
DR   Proteomes; UP000001450; Chromosome 13.
DR   GO; GO:0020020; C:food vacuole; IDA:GeneDB.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:GeneDB.
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; IBA:GO_Central.
DR   GO; GO:1902600; P:proton transmembrane transport; ISS:GeneDB.
DR   GO; GO:0007035; P:vacuolar acidification; ISS:GeneDB.
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   1: Evidence at protein level;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Merozoite;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..611
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144569"
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