ID VATA_HYPBU Reviewed; 601 AA.
AC A2BKX6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=Hbut_0784;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
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; CP000493; ABM80637.1; -; Genomic_DNA.
DR AlphaFoldDB; A2BKX6; -.
DR SMR; A2BKX6; -.
DR STRING; 415426.Hbut_0784; -.
DR EnsemblBacteria; ABM80637; ABM80637; Hbut_0784.
DR KEGG; hbu:Hbut_0784; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_3_1_2; -.
DR OrthoDB; 115235at2157; -.
DR Proteomes; UP000002593; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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; 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 SMART; SM00382; AAA; 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; ATP-binding; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..601
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000059343"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 601 AA; 67187 MW; 57D712AEEB372063 CRC64;
MPVKGRIIRV AGPLVVAEGM EGIQMYEMVE VGEERLIGEV NRVVGDKAYI QVYESTTGLK
PGEPVYGTGS PLSVELGPGL IGRIYDGIQR PLDVIREVTK SIFVRRGVKV DALDRSRKWH
FKPNTTLKPG DKVSGGDVLG EVQETSLITH KVLVPPDVHG RLKWLASEGD YTVEDVIAVV
EADGKEIELK MYHRWPVRRA RPIIEKLEPV EPLITGMRVI DTMFPMAKGG TGAIPGPFGS
GKTVTLQSLA KWSAAKVVIY IGCGERGNEM TEVLETFPKL TDPWTGKPMM ERTILIANTS
NMPVAAREAS IYTGITLAEY YRDMGYDVLL VADSTSRWAE ALREIAGRLE EMPAEEGYPS
YLASRLAEFY ARAGRVKVPG RPERLGSVTI VGAVSPPGGD FTEPVTANTK RFIRVFWALD
ARLAYSRHYP AINWLVSYSA YVETVAKWWH ENISPKWLEY RNEAYEILLR EDELREIVRL
VGTEGLSEKD KLILEIANII KTGFLQQNAF DPVDAFATPQ KQWKQLETII DFYHAALEAI
KRGVTVKEIR EKLAPKIREL ILARYNVPND QLEKLDKLKQ ELLQALQELI EAKAGRASAA
T
//
