VATA_PYRAE
ID VATA_PYRAE Reviewed; 593 AA.
AC Q8ZYR1;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=PAE0663;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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 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; AE009441; AAL62932.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZYR1; -.
DR SMR; Q8ZYR1; -.
DR STRING; 178306.PAE0663; -.
DR EnsemblBacteria; AAL62932; AAL62932; PAE0663.
DR KEGG; pai:PAE0663; -.
DR PATRIC; fig|178306.9.peg.477; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_3_1_2; -.
DR InParanoid; Q8ZYR1; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000002439; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
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; 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.
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..593
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000144603"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 593 AA; 66320 MW; C3966BF19D7FBCE3 CRC64;
MSGKIEYISG PVVKAELPGA RLYELVFVGE IKLFGEVVRI QGEKAFIQVY EDTTGLKPGE
PVERTGEPLS AWLGPTIIGK IYDGVQRPLR NIEEISKNPF IARGIGYDKA PPLDLKAEFD
FKPAVKPGEE VYPGDVLGSV KETEPMTHYI LYPPLPEHAP GVVEWIADGK YKVDDVIARV
KTKRGVVEVK MWHKWPVRRP RPFKEKLPPV EPLITGVRTV DTMFPIAKGG TAAVPGPFGS
GKTVMIRTLS MFAQSRFIIP VLCGERGNEA ADALQGLLKL KDPSTGRPLL ERTTIIVNTS
NMPVAAREAS VYMGTTLGEY FRDQGYDVLV LADSTSRWAE AMREVALRIG EMPSEEGYPA
YLPTRLAEFY ERAGRVVLYG SKERVGSLTI AASVSPPGGD FTEPVTSNTL RFIGAFWPLS
PRLAYSRHYP AIDWLVAFSR YVDTVEVWWS KNVSPEWRRI RDALQSILVK EAELQEIVRI
LGTEALSEYE KHILNVAFMI REGFLKQDAY NPVDTPSAPI KQFLLMKAIY TYYEEGLKAI
ESGVPASVLR ELETVKRLPR LRMEVTNDVA KEELTKFIES LVAEIRATTN RRG