VATA_METMA
ID VATA_METMA Reviewed; 578 AA.
AC Q60186;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
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; Synonyms=ahaA; OrderedLocusNames=MM_0780;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=8702544; DOI=10.1074/jbc.271.31.18843;
RA Wilms R., Freiberg C., Wegerle E., Meier I., Mayer F., Mueller V.;
RT "Subunit structure and organization of the genes of the A1A0 ATPase from
RT the Archaeon Methanosarcina mazei Go1.";
RL J. Biol. Chem. 271:18843-18852(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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 -!- ACTIVITY REGULATION: Stimulated by sulfite, ethanol, glycerol,
CC magnesium and zinc ions.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.2.;
CC -!- SUBUNIT: Composed of seven subunits; A, B, C, D, E, F and G.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; U47274; AAC06375.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM30476.1; -; Genomic_DNA.
DR PIR; T45107; T45107.
DR RefSeq; WP_011032730.1; NC_003901.1.
DR AlphaFoldDB; Q60186; -.
DR SMR; Q60186; -.
DR STRING; 192952.MM_0780; -.
DR TCDB; 3.A.2.3.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PRIDE; Q60186; -.
DR EnsemblBacteria; AAM30476; AAM30476; MM_0780.
DR GeneID; 44085982; -.
DR GeneID; 66137823; -.
DR KEGG; mma:MM_0780; -.
DR PATRIC; fig|192952.21.peg.928; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_3_1_2; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000000595; 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 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..578
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000144598"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 87
FT /note="V -> L (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="R -> G (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..151
FT /note="VR -> LP (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> S (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="K -> R (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..179
FT /note="DGT -> EGP (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="D -> E (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> P (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="L -> P (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 542..543
FT /note="MQ -> IE (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="E -> S (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="F -> Y (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="D -> N (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="G -> D (in Ref. 1; AAC06375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 63883 MW; 861F8D88C659D7D3 CRC64;
MEVKGEIYRV AGPVVTAIGL DAKMYDLCKV GNEGLMGEVI QIVGDKTIIQ VYEETGGVRP
GEPCVTTGMS LAVELGPGLL SSIYDGVQRP LHVLLERTGG FIGRGVTADG LDHKKLWEFK
PVVKKGDRVI GGDVIGVVQE TVNIEHKIMV RPDISGTVAD IKSGSFTVVD TICTLTDGTE
LQMMQRWPVR KPRPVKRKLT PEKPLVTGQR ILDGLFPVAK GGTAAIPGPF GSGKTVTQQQ
LSKWSDTEIV VYIGCGERGN EMADVLWEFP ELEDPQTGRP LMERTILVAN TSNMPVAARE
ASVYTGMTLA EYFRDMGYDV SLMADSTSRW AEAMREISSR LEEMPGEEGY PAYLSARLAE
FYERAGVAET LCGEKGSITA IGAVSPPGGD FSEPVTQNTL RIVKVFWALD AKLSQKRHFP
AINWLNSYSL YKEDLNDWFT ENVAPDYVPM RERAMDMLQT ESELQEIVQL VGSDALPEEQ
QLLLEITRMI REIFLQQNAF HPIDTYSPFE KQYKIMKAIM KWGDAAMDAL KSGVLSSEIL
KMQSKDELPK VKFEEDFEGS LNAVLAKMDK EFAALGGK
