ID   VATA3_METHJ             Reviewed;         588 AA.
AC   Q2FQE9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=V-type ATP synthase alpha chain 3 {ECO:0000255|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A 3 {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA3 {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=Mhun_1770;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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       {ECO:0000255|HAMAP-Rule:MF_00309}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00309};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00309}.
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DR   EMBL; CP000254; ABD41491.1; -; Genomic_DNA.
DR   RefSeq; WP_011448755.1; NC_007796.1.
DR   AlphaFoldDB; Q2FQE9; -.
DR   SMR; Q2FQE9; -.
DR   STRING; 323259.Mhun_1770; -.
DR   PRIDE; Q2FQE9; -.
DR   EnsemblBacteria; ABD41491; ABD41491; Mhun_1770.
DR   GeneID; 3924744; -.
DR   KEGG; mhu:Mhun_1770; -.
DR   eggNOG; arCOG00868; Archaea.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OrthoDB; 6736at2157; -.
DR   Proteomes; UP000001941; Chromosome.
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; 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; 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   PROSITE; PS00152; ATPASE_ALPHA_BETA; 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..588
FT                   /note="V-type ATP synthase alpha chain 3"
FT                   /id="PRO_0000322484"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   588 AA;  65582 MW;  B98E963379943A48 CRC64;
     MGEKNGVIIR VTGPVVEAEG MAGSRMYESV RVGNDGLIGE IIILEGDRAT IQVYEETIGL
     TPGEPVVRTY LPLSVELGPG LIGTMYDGIQ RPLEEILKNT GDMIERGSSA PALDRTKKYR
     FYPLAKSGDM VREGDRIGCV RESVSVNHYI LIPPGLSGTI HFIAEQGEYV ITDTIVILDT
     GEEKKELTMI QRWPVRDPRP VRERLDPVEP LLTGQRIIDT LFPLARGGTA AIPGPFGSGK
     TVVQQQLAKW VNADIIIYIG CGERGNEMAD VLEQFPTLKD PRTGHALSSR MVLIANTSNM
     PVAAREASVY TGITIAEYYR DMGYHVALMA DSTSRWAEAM REISGRLEEM PGEEGYPAYL
     SSRLADFYER AGRVSLLGSG DHEGSISVIG AVSPPGGDFS EPVTQNTLRI VKVFWALDAD
     LAYQRHFPAI NWLMSYSLYS PIAGIWWEEH IGPEFIRMKQ EMMEILQREN ELEEIIRLVG
     PETLPESDRL LLLKAEILRE SYLMQYAFDE FDTFTGPKKQ YRMLKAIFTF FSQAERALET
     GISVSRLRGL PVIESFARMG TASPEEEDPL FESIARDTDA IRDLKEVL