VATA_HALMA
ID VATA_HALMA Reviewed; 586 AA.
AC Q5UXY8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=rrnAC3159;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV47865.1; -; Genomic_DNA.
DR RefSeq; WP_004964538.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UXY8; -.
DR SMR; Q5UXY8; -.
DR STRING; 272569.rrnAC3159; -.
DR EnsemblBacteria; AAV47865; AAV47865; rrnAC3159.
DR GeneID; 40153967; -.
DR GeneID; 64823617; -.
DR KEGG; hma:rrnAC3159; -.
DR PATRIC; fig|272569.17.peg.3699; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_3_1_2; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000001169; Chromosome I.
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; IPR001763; Rhodanese-like_dom.
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..586
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_1000059342"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 586 AA; 64904 MW; 97A4734D8AFFCB50 CRC64;
MSQATDTDVR EDGIIESVSG PVVTARDLDA RMNDVVYVGS EGLMGEVIEI EGNITTIQVY
EETSGVSPGE PVEGTGSPLS VDLGPGMLDA IYDGVQRPLD VLEEKMGSAF LDRGVDAPGI
DLEKTWEFTP EVEEGDEVEA GDIVGTVPET PSIDHKVMVP PDSEGGEVVA IESGNFNVEE
TVVELDNGEE IQMHQEWPVR QQRPTVEKET PTEPLISGQR VLDGLFPIAK GGTAAIPGPF
GSGKTVTQHQ LAKWADADIV VYVGCGERGN EMTEVIEDFP ELEDPTTGNA LMDRTCLIAN
TSNMPVAARE SCVYTGITIA EYFRDMGYDV ALMADSTSRW AEAMREISSR LEEMPGEEGY
PAYLSARLSE FYERAGYFEN INGTEGSVSV IGAVSPPGGD FSEPVTQNTL RIVKTFWALD
ADLAERRHFP SINWNESYSL YRDQLDPWFE DNVRADWPET RQWAIDTLDE EAELQEIVQL
VGKDALPEDQ QLTLEIARYL REAWLQQNAF HDVDTFCEPE KTYRIMDAAK TYNDAAFEAL
DAGVPVEEIT DIDAAPRLNR IGVQEDYNEY IDDLEDDIES QLRELY