ID   VATA_SULAC              Reviewed;         592 AA.
AC   Q4J8L9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=V-type ATP synthase alpha chain;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase subunit A;
GN   Name=atpA; OrderedLocusNames=Saci_1548;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The archaeal alpha chain is a catalytic subunit.
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   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; CP000077; AAY80861.1; -; Genomic_DNA.
DR   RefSeq; WP_011278363.1; NC_007181.1.
DR   AlphaFoldDB; Q4J8L9; -.
DR   SMR; Q4J8L9; -.
DR   STRING; 330779.Saci_1548; -.
DR   EnsemblBacteria; AAY80861; AAY80861; Saci_1548.
DR   GeneID; 3474583; -.
DR   KEGG; sai:Saci_1548; -.
DR   PATRIC; fig|330779.12.peg.1488; -.
DR   eggNOG; arCOG00868; Archaea.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OMA; RIVKTFW; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR005726; ATP_synth_asu_arc.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01043; ATP_syn_A_arch; 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..592
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144605"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   592 AA;  66143 MW;  E631DEB6BBAF3490 CRC64;
     MAGEGRVVRV NGPLVVADGM RNAQMFEVVE VGELRLVGEI TRIEGDRAYI QVYEATDGIK
     PGEKAYRTGS LLSVELGPGL MGGIFDGLQR PLDRIAESVK SPFVTRGVKV PALERNKKWH
     VIPVAKKGDK VSPGDIIAKV NETDLIEHRI IVPPNVHGTL KEISPEGDYT VEDVIARVDM
     EGDVKELKLY QRWPVRIPRP FKEKLEPTEP LLTGTRVVDT IFPIAKGGTA AIPGPFGSGK
     TVTLQSLAKW SEAKVVIYVG CGERGNEMTD ELRQFPKLKD PWTGKPLLQR TILVANTSNM
     PVAARESSIY VGVTMAEYFR DQGYDVLLVA DSTSRWAEAL RELGGRMEEM PAEEGFPSYL
     PSRLAEYYER AGRVIALGKP ERFGSVSIAS AVSPPGGDFT EPVTSNTLRF VRVFWPLDVS
     LAQARHYPAI NWIQGFSAYV DLVASWWHKN VDPTWFEMRS VLVKILLRED ELRQIVRLVG
     PESLSDKDKL ILEASKLIRD AFLKQNAFDD IDAFSSPQKQ AKIMRLIYDF YTNASQLLDK
     GLTLKKILEK VGSFEPDIVR VKYTVKNDEL NKIDELDNKL KEAFDSLLKE VA