AC MF_00309; DC Protein; auto TR HAMAP; MF_00309; -; 1; level=0 XX Names: ATP_synth_A_arch XX ID VATA DE RecName: Full=V-type ATP synthase alpha chain; DE EC=7.1.2.2; DE AltName: Full=V-ATPase subunit A; GN Name=atpA; XX case 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. end case case 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. end case 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 -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. XX DR Pfam; PF00006; ATP-synt_ab; 1; trigger=no DR Pfam; PF00306; ATP-synt_ab_C; 1; trigger=no DR NCBIfam; TIGR01043; ATP_syn_A_arch; 1; trigger=no DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1; trigger=no XX KW Translocase KW ATP synthesis KW Nucleotide-binding KW Transport KW Ion transport KW Hydrogen ion transport KW ATP-binding XX GO GO:0005524; F:ATP binding GO GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism GO GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis XX FT From: VATA_METJA (Q57670) FT BINDING 234..241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-x-F-G-[STA]-G-K-T XX Size: 570-605; Related: MF_00310; Template: Q48332; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in TREPA Plasmid: None Comments: Inteins deleted in PYRAB, PYRHO and THEAC XX # Revision 1.35 2023/06/01 //