ID   VATA_CYACA              Reviewed;         587 AA.
AC   P48414;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
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   Cyanidium caldarium (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7619836; DOI=10.1016/0005-2728(95)00060-v;
RA   Ziegler K., Hauska G., Nelson N.;
RT   "Cyanidium caldarium genes encoding subunits A and B of V-ATPase.";
RL   Biochim. Biophys. Acta 1230:202-206(1995).
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; U17100; AAA85820.1; -; Genomic_DNA.
DR   PIR; T14360; T14360.
DR   AlphaFoldDB; P48414; -.
DR   SMR; P48414; -.
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..587
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144578"
FT   BINDING         243..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   587 AA;  64885 MW;  1450652C4FA01E77 CRC64;
     MTTVRVNGMK NGIIKKVSGP VVSAENMDGA AMYELVRVGN EQLVGEIIRL EGSVATIQVY
     EETSGLTIGD PVLCTGSPLS VELGPGLMGN IFDGIQRPLE KIAERSNSVF IPRGVNVPAL
     DRKKVWEFRP ADNLKVGDPI TAGDIYGIVP ETPLIDHKIM LPPNQMGKIV FLAPPGDYTL
     EDTVLEIDFN GQKKKFSMVH QWPVRLPRPV TEKLRADKPL LTGQRVLDAL FPSVQGGTCA
     IPGAFGCGKT VISQALSKFS NSDGIVYVGC GERGNEMAEV LKDFPELTMT VGDREESIMK
     RTLLVANTSN MPVAAREASI YTGITVSEYY RDMGLNISMM ADSTSRWAEA LREISGRLAE
     MPADSGYPAY LAARLASFYE RAGKVSCLGS PNRQGSITIV GAVSPPGGDF SDPVTSATLG
     IVQVFWGLDK KLAQRKHFPS VNWLISYSKY MKALEPYYEE RFPEFLNYQQ KAREILQTED
     DLMEIVQLVG KDSLAENDKI TLEVAKMIRE DFLAQNSFTE YDRFCPFYKS VLMLRNMIHF
     YELANKAVEG SGEQHLTLAQ IKEQMGETIY KISGMKFLDP AQGWSLF