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VATA1_METHJ
ID   VATA1_METHJ             Reviewed;         582 AA.
AC   Q2FP52;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=V-type ATP synthase alpha chain 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00309};
GN   Name=atpA1 {ECO:0000255|HAMAP-Rule:MF_00309}; OrderedLocusNames=Mhun_1183;
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; ABD40931.1; -; Genomic_DNA.
DR   RefSeq; WP_011448208.1; NC_007796.1.
DR   AlphaFoldDB; Q2FP52; -.
DR   SMR; Q2FP52; -.
DR   STRING; 323259.Mhun_1183; -.
DR   PRIDE; Q2FP52; -.
DR   EnsemblBacteria; ABD40931; ABD40931; Mhun_1183.
DR   GeneID; 3923385; -.
DR   KEGG; mhu:Mhun_1183; -.
DR   eggNOG; arCOG00868; Archaea.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 6736at2157; -.
DR   Proteomes; UP000001941; 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; 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   SMART; SM00382; AAA; 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..582
FT                   /note="V-type ATP synthase alpha chain 1"
FT                   /id="PRO_0000322482"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   582 AA;  64780 MW;  EF04DF51526F5605 CRC64;
     MEVKRTKGVL KRIAGPVVTA VNLDAHMYDV VKVGDEQLMG EVIKIKGEDI IIQVYEDTSG
     IKPGEPVENT GLSLSVELGP GLLTSIYDGI QRPLEVLVEK MGNFIERGVT APGLSHDKKW
     EFKPIKKAGD MVTPGTIIGE VQETNIVHKI MVPPYCDAGK IKDIKSGSFT IDEIICTLDN
     GAEIAMMHKW PVRMPRPVTE KLNPDIPLIT GQRILDGLFP VAKGGTAAIP GPFGSGKTVT
     QQALAKWSDA EIVVYIGCGE RGNEMTEVLT EFPELEDPKT GRPLMERTVL IANTSNMPVA
     AREASVYTGI TIAEYFRDMG YDVSLMADST SRWAEAMREI SSRLEEMPGE EGYPAYLAAR
     LSEFYERAGR VNTLNKDFGS VTVIGAVSPP GGDFSEPVTQ NTLRIVKCFW ALDAKLSQRR
     HFPAINWLNS YSLYLDTLSQ YYDENVSPEW NPLRTWAMEV LQKEAELQEI VQLVGSDALP
     DEEQVTIEVA RMLREIFLQQ NAFDPVDTYC DMTKQFDILK AIRFYSDQAY AALKAGVITS
     QITGLKAKND LPQIKYVKEY KPEIERIVKT MESEFTKLRE AA
 
 
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