VATA_CENSY
ID VATA_CENSY Reviewed; 592 AA.
AC A0RXK1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=CENSYa_1446;
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A;
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK78068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RXK1; -.
DR SMR; A0RXK1; -.
DR STRING; 414004.CENSYa_1446; -.
DR PRIDE; A0RXK1; -.
DR EnsemblBacteria; ABK78068; ABK78068; CENSYa_1446.
DR KEGG; csy:CENSYa_1446; -.
DR PATRIC; fig|414004.10.peg.1330; -.
DR HOGENOM; CLU_008162_3_1_2; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000000758; 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; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 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..592
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000322470"
FT BINDING 234..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 592 AA; 65212 MW; 48C7087618CE274C CRC64;
MTARGKIVWV SGPAVKADGM SEAKMYETVT VGEARLIGEV IRLTGDVAFI QVYESTSGLK
PGEPVEGTGN PLSVLLGPGI IGQIYDGIQR PLKELSKKSG SFIGRGITTS PVDMTKKYHF
VPSVSVGDDV IPGTVIGTVK ETDLIDHSIM VPPDHAGGKI KSIVSEGEYD LETEMAGIEK
DGKTIPLKMY HRWPVRQPRS YHTKYDPTVP LITGQRVIDT FFPIAKGGTG SIPGGFGTGK
TVTLHQIAKW ADSQVVVYIG CGERGNEMTE VLVEFPHLKD PRTDKPLMDR TVLVANTSNM
PVAAREASIY TGVTIAEYYR DMGKDVVLVA DSTSRWAEAL REMSGRLEEM PAEEGYPSYL
ASRLAEFYER AGRVRALGSP ERNGSVTLVG AVSPSGGDFT EPVTTHTMRF IKTFWALDAK
LAYSRHYPSI NWMNSYSGYL ADIAKWWGEN VSKDWLDTRS EAYGILQRED TLKEIVRLLG
PEALPDEEKL ILEVARMMKI GLLQQNSFDD VDTYCSPEKQ YKLLKMQVDF YKRGQQALKE
GAELADIRAM PVISGLLKAK MDIKDDEMPK LDELAGAMDE QYKGITGVKV AS