ID   VATA_METTH              Reviewed;         584 AA.
AC   O27036;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 141.
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=MTH_955;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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       (By similarity). {ECO:0000250}.
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; AE000666; AAB85451.1; -; Genomic_DNA.
DR   PIR; G69227; G69227.
DR   RefSeq; WP_010876586.1; NC_000916.1.
DR   AlphaFoldDB; O27036; -.
DR   SMR; O27036; -.
DR   IntAct; O27036; 3.
DR   STRING; 187420.MTH_955; -.
DR   EnsemblBacteria; AAB85451; AAB85451; MTH_955.
DR   GeneID; 1471363; -.
DR   KEGG; mth:MTH_955; -.
DR   PATRIC; fig|187420.15.peg.938; -.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OMA; TAFVQVY; -.
DR   Proteomes; UP000005223; 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; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR005726; ATP_synth_asu_arc.
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   TIGRFAMs; TIGR01043; ATP_syn_A_arch; 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..584
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000144601"
FT   BINDING         233..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   584 AA;  64895 MW;  90F01BD38B3D6D78 CRC64;
     MTQEGRIIKI AGPVIIAEGM RGSQMYEMVK VGEDKLIGEI IELEGDTATI QVYEETAGIK
     PGETVERTGG PLSVELGPGI LGSIFDGIQR PLENIKALTG DYIERGVDVP SLPKDKKWTF
     KPTAREGQMV KGGDIIGEVE ETSSITHRIM IPPNVEGKLT MIAPQGEYTV LDDIAEVETE
     SGTEKIQMLQ KWPVRKGRPY KKKLDPDVPL VTGQRAQDTF FSVAKGGTAA IPGPFGSGKT
     VTQQQLAKWA DADIIVYVGC GERGNEMTEV LKEFPELEDP KTGNPLMDRT VLIANTSNMP
     VAAREACVYT GITIAEYFRD MGYDVALMAD STSRWAEAMR EISGRLEEMP GEEGYPAYLA
     SRLAQFYERA GRVTTIGSED KIASVSVVGA VSPPGGDLSE PVTQNTLRIC KVFWALDASL
     ADKRHFPSID WLQSYSLYID SVQEWWASNV DPEWRKFRDE AMALLQKEAE LQEIVQLVGP
     DALPDRERIT LETTRMIRED FLQQNAYHEV DTYCSPSKQF EMLRTIIMFH RNATAALEKG
     APAADIISLP VKEDIGRMKY IPEEEFPARI KEIQERIVKE CSEV