VATA_PARUW
ID VATA_PARUW Reviewed; 593 AA.
AC Q6MAJ5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=pc1680;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The V-type 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; BX908798; CAF24404.1; -; Genomic_DNA.
DR RefSeq; WP_011176226.1; NC_005861.1.
DR AlphaFoldDB; Q6MAJ5; -.
DR SMR; Q6MAJ5; -.
DR STRING; 264201.pc1680; -.
DR EnsemblBacteria; CAF24404; CAF24404; PC_RS08040.
DR KEGG; pcu:PC_RS08040; -.
DR eggNOG; COG1155; Bacteria.
DR HOGENOM; CLU_008162_1_1_0; -.
DR OMA; RIVKTFW; -.
DR OrthoDB; 875807at2; -.
DR Proteomes; UP000000529; 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; 3.40.50.300; -; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
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; 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..593
FT /note="V-type ATP synthase alpha chain"
FT /id="PRO_0000322468"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00309"
SQ SEQUENCE 593 AA; 66546 MW; AF0581E4A7E2167F CRC64;
MKTLETRKEK KAQGKVLKAF GNLLQVTFEG NIRQGEVAMV HVDNLQLKSE VIEILGNQAK
IQVFEDTKGV RLGSLVSFTG DLLEAELGPG LLSSIFDGLQ NPLVDVADQA GLFLPKGIYL
SALDRQRKWD FESSAKVGDV LFRGDRIGST KEGRFHHFIM VPFSLYGKYR LTWVINSGSY
TVDTVVAKAI DESGQEHSFT MVQKWPVKNA LIHGEKIKPT KMMDTGERII DTQFPLMKGG
TFCTPGPFGA GKTVLQHHLS KYAAVDIVLF VACGERAGEV VEVLREFPHL IDPHTDEALM
KRTVIICNTS SMPVAARESS IYMGITIAEY YRQMGLDVLV LADSTSRWAQ ALREMSGRLE
EIPGEEAFPA YLSSRIAEFY ERSGVVSLRH GKPGSITIGG AVSPAGGNFE EPVTQATLSV
VGAFLGLSRA RSDSRRYPAI DPLLSWSKYV DTVGNELSHQ VDGWDQMVKR ARHILFNGNE
IGKRMEVVGE EGISMEDMLT YLKAELYDFS YLQQNAFDKE DAYCPLKRQI ALFQLINQIF
DTTFDFHTHD QAREFFLDLQ NRIKNMNFIS FDTEQYRKVF AEIKSIIEQQ SRK