VATA_METBA
ID VATA_METBA Reviewed; 578 AA.
AC P22662;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 117.
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;
OS Methanosarcina barkeri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2208;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544575; DOI=10.1016/s0021-9258(18)60411-9;
RA Inatomi K., Eya S., Maeda M., Futai M.;
RT "Amino acid sequence of the alpha and beta subunits of Methanosarcina
RT barkeri ATPase deduced from cloned genes. Similarity to subunits of
RT eukaryotic vacuolar and F0F1-ATPases.";
RL J. Biol. Chem. 264:10954-10959(1989).
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; J04836; AAA72215.1; -; Genomic_DNA.
DR PIR; A34283; A34283.
DR AlphaFoldDB; P22662; -.
DR SMR; P22662; -.
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; Translocase; Transport.
FT CHAIN 1..578
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000144597"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 63638 MW; 195019833C89552B CRC64;
MEVKGEIYRV SGPVVTAIGL QAKMYDLVKV GNEGLMGEVI QILGPKTIIQ VYEETAGIKP
GEPCVSTGSS LSVELGPGLL SSIYDGVQRP LHVLLEKMGS FIQRGVSADG LDHKKLWDFK
PIVKKGDSVK GGDVIGVVQE TVNIEHKIMV PPDISGTISD IKSGNFTVVD TICTLTDGTE
LQMMQRWPVR RPRPVKAKLT PTRPLVTGMR ILDGLFPVAK GGTAAIPGPF GSGKTVTQQS
LAKWSDTEIV VYIGCGERGN EMADVLSEFP ELEDPQTGRP LMERTVLIAN TSNMPVAARE
ASVYTGITIA EYYRDMGLDV SLMADSTSRW AEAMREISSR LEEMPGEEGY PAYLSARLAE
FYERAGVAES LCGETGSITV IGAVSPPGGD FSEPVTQNTL RIVKVFWALD AKLSQRRHFP
AINWLNSYSL YKDSLNDWFA DNVAPDYVPL RERAMEMLQT ESELQEIVQL VGSDALPDDQ
QLLLEITRML REIFLQQNAF HPVDAYSPFD QQYKILKAIM KWGDAAMDAL KSGVPVTEII
KLESKNVLAK VKYEEKFDES MNAVLAQMDK EFASLRGR