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VATA_METMJ
ID   VATA_METMJ              Reviewed;         584 AA.
AC   A3CS71;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=V-type ATP synthase alpha chain {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 {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=Memar_0287;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN56221.1; -; Genomic_DNA.
DR   RefSeq; WP_011843142.1; NC_009051.1.
DR   AlphaFoldDB; A3CS71; -.
DR   SMR; A3CS71; -.
DR   STRING; 368407.Memar_0287; -.
DR   PRIDE; A3CS71; -.
DR   EnsemblBacteria; ABN56221; ABN56221; Memar_0287.
DR   GeneID; 4846211; -.
DR   KEGG; mem:Memar_0287; -.
DR   eggNOG; arCOG00868; Archaea.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 6736at2157; -.
DR   Proteomes; UP000002146; 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; IPR001763; Rhodanese-like_dom.
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; Translocase; Transport.
FT   CHAIN           1..584
FT                   /note="V-type ATP synthase alpha chain"
FT                   /id="PRO_0000322478"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   584 AA;  64328 MW;  7F4333C5B4E574B4 CRC64;
     MDKGKENRAQ GVLKRISGPV VTAVGLDAHM YDVVKVGNEE LMGEVIKIQG ENIIIQVYED
     TAGIRPGESV GNTGLSLAVE LGPGLLTSIY DGIQRPLEVL VDKMGNFIER GVSAPGLSHE
     KKWEFVPTVK KGDEVKAGDI LGTVQETNIV HKVMVPPKAK GGKIKKISGG SFTVDETVCV
     LEDGTEIAML QRWPVRVPRP VTQKLNPDIP LITGQRILDG LFPIAKGGTA AIPGPFGSGK
     TVTQQQLAKW SDAEIVVYIG CGERGNEMTE VLTEFPELED PKTGKPLMER TVLIANTSNM
     PVAAREASVY TGITIAEYFR DMGYDVSLMA DSTSRWAEAM REISSRLEEM PGEEGYPAYL
     AARLSEFYER AGRVISLNGE GGSVSVIGAV SPPGGDFSEP VTQNTLRIVK VFWALDAKLS
     QRRHFPAINW LNSYSLYLDA LNEWYDKEVS PEWNPLRAWA MGVLQKEAEL QEIVQLVGSD
     ALPDEEQVTI EVARMIREIF LQQNAYDAVD TFCPMSKQYD MMKAIKHYAD LARTAQTGGA
     TPQQVIGIRS KNELPQIKFI RDYEPELAKI MKDMEAEFDA MRAV
 
 
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