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Database: UniProt
Entry: D7E6E6_METEZ
LinkDB: D7E6E6_METEZ
Original site: D7E6E6_METEZ 
ID   D7E6E6_METEZ            Unreviewed;       578 AA.
AC   D7E6E6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|ARBA:ARBA00018003, ECO:0000256|HAMAP-Rule:MF_00309};
DE            EC=7.1.2.2 {ECO:0000256|ARBA:ARBA00012473, ECO:0000256|HAMAP-Rule:MF_00309};
DE   AltName: Full=V-ATPase subunit A {ECO:0000256|ARBA:ARBA00031719, ECO:0000256|HAMAP-Rule:MF_00309};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN   OrderedLocusNames=Metev_0238 {ECO:0000313|EMBL:ADI73168.1};
OS   Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634
OS   / OCM 161 / Z-7303).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalobium.
OX   NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI73168.1, ECO:0000313|Proteomes:UP000000391};
RN   [1] {ECO:0000313|EMBL:ADI73168.1, ECO:0000313|Proteomes:UP000000391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303
RC   {ECO:0000313|Proteomes:UP000000391};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence chromosome of Methanohalobium evestigatum Z-7303.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003912, ECO:0000256|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:0000256|ARBA:ARBA00001741, ECO:0000256|HAMAP-
CC         Rule:MF_00309};
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00309}.
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DR   EMBL; CP002069; ADI73168.1; -; Genomic_DNA.
DR   RefSeq; WP_013193736.1; NC_014253.1.
DR   AlphaFoldDB; D7E6E6; -.
DR   STRING; 644295.Metev_0238; -.
DR   GeneID; 9345850; -.
DR   KEGG; mev:Metev_0238; -.
DR   HOGENOM; CLU_008162_3_1_2; -.
DR   OrthoDB; 115235at2157; -.
DR   Proteomes; UP000000391; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR   CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR   CDD; cd01134; V_A-ATPase_A; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01043; ATP_syn_A_arch; 1.
DR   PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR   PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00309};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00309}; Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00309};
KW   Hydrolase {ECO:0000313|EMBL:ADI73168.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00309};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00309}; Reference proteome {ECO:0000313|Proteomes:UP000000391};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_00309};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00309}.
FT   DOMAIN          7..68
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          84..200
FT                   /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT                   /evidence="ECO:0000259|Pfam:PF16886"
FT   DOMAIN          209..430
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   BINDING         229..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ   SEQUENCE   578 AA;  64367 MW;  0DFD9A00B9E632CB CRC64;
     MEVKGEIYRV SGPVVIATGI RPKMYDVVKV GHEGLMGEVI KIEGDKSTIQ VYEDTSGIKP
     GEPVENTGLP LSVELGPGLL ESIYDGIQRP LQVLQDKMGD FIARGATANG IDREKQWEFK
     PIVDKGDKVE PGDIIGVVQE TPNLEHQIMV PPNMQGGTVS DIYSGKFTVD ETVCVLSNGK
     ELSMLQKWPV RTPRPTKRKL KPDKPLLTGQ RILDGMFPVA KGGTAAIPGP FGSGKTVTQQ
     QLAKWSDTDI VVYVGCGERG NEMADVLDEF PELEDPKAGR PLMERTVLIA NTSNMPVAAR
     EASVYTGITI SEYYRDMGYD VALMADSTSR WAEAMREISS RLEEMPGEEG YPAYLAARLS
     EFYERAGYVK SNSGYDGSIT VIGAVSPPGG DFSEPVTQNT LRIVKVFWAL DAKLSQRRHF
     PAINWLTSYS LYTESLSDWL SENVASDWID LRNYAMDILE EESELQEIVQ LVGSDALPES
     QQLKLEVARM FREYFLQQNA FHEIDRYCPF YKQYKLVQAI HKFSETANSK LEAGYSINDI
     MAMESKDELA KVRYEEDFDG ALNKVLSKMD DEFSQIGG
//
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