VATA_NATPD
ID VATA_NATPD Reviewed; 585 AA.
AC Q3ITC8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=NP_1030A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48606.1; -; Genomic_DNA.
DR RefSeq; WP_011322241.1; NC_007426.1.
DR AlphaFoldDB; Q3ITC8; -.
DR SMR; Q3ITC8; -.
DR STRING; 348780.NP_1030A; -.
DR EnsemblBacteria; CAI48606; CAI48606; NP_1030A.
DR GeneID; 3702538; -.
DR KEGG; nph:NP_1030A; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_3_1_2; -.
DR OMA; RIVKTFW; -.
DR OrthoDB; 6736at2157; -.
DR Proteomes; UP000002698; 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; 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 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Hydrogen ion transport; Ion transport;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..585
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000059348"
FT BINDING 237..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 585 AA; 65070 MW; 7586B161EFA2C1B1 CRC64;
MSQATASEIT DEGVIESVSG PVVTAVDLDA RMNDVVYVGE EGLMGEVIEI EGNLTTIQVY
EETSDVAPGE PVENTGEPLS VDLGPGMMDS IYDGVQRPLD VLEEKMGAFL DRGVDAPGID
LEKTWEFNPE VSEGDEVSPG DVVGIVPETE SIDHKVLVPP DYEGGEVTAV ESGNFTVDET
VVELDSGEEI QMRQEWPVRE PRPTVEKETP TTPLVSGQRV LDGLFPIAKG GTAAIPGPFG
SGKTVTQHQL AKWADADIVV YVGCGERGNE MTEVIEDFPE LEDPKTGKPL MSRTCLIANT
SNMPVAARES CVYTGITIAE YYRDMGYDVA LMADSTSRWA EAMREISSRL EEMPGEEGYP
AYLAARLSEF YERAGKFQNM NGSEGSISVI GAVSPPGGDF SEPVTQNTLR IVKCFWALDA
DLAERRHFPS INWNESYSLY KEQLDPWWRE NVHEEFPEVR QWAVDVLDEE DELQEIVQLV
GKDALPEDQQ LTLEVARYIR EAWLQQNAFH DVDTYCEPEK TYQMLTAIQH FNDEAFEALD
AGVPVEEIID VDAVPQLNRM NTQEDYEEYI EELKGDLTDQ LRELY
