ID ATPA_UREPA Reviewed; 799 AA. AC Q9PR12; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 04-NOV-2026, entry version 138. DE RecName: Full=ATP synthase subunit alpha; DE EC=7.1.2.2; DE AltName: Full=ATP synthase F1 sector subunit alpha; DE AltName: Full=F-ATPase subunit alpha; GN Name=atpA; OrderedLocusNames=UU132; OS Ureaplasma parvum serovar 3 (strain ATCC 700970). OC Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Ureaplasma. OX NCBI_TaxID=273119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700970; RX PubMed=11048724; DOI=10.1038/35037619; RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., RA Cassell G.H.; RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum."; RL Nature 407:757-762(2000). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient CC across the membrane. The alpha chain is a regulatory subunit (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out); 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 -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core CC - and CF(0) - the membrane proton channel. CF(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an CC alternating ring which encloses part of the gamma chain. CF(1) is CC attached to CF(0) by a central stalk formed by the gamma and epsilon CC chains, while a peripheral stalk is formed by the delta and b chains CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF222894; AAF30538.1; -; Genomic_DNA. DR RefSeq; WP_006689132.1; NC_002162.1. DR AlphaFoldDB; Q9PR12; -. DR SMR; Q9PR12; -. DR STRING; 273119.UU132; -. DR EnsemblBacteria; AAF30538; AAF30538; UU132. DR GeneID; 77133460; -. DR KEGG; uur:UU132; -. DR eggNOG; COG0056; Bacteria. DR HOGENOM; CLU_019180_0_0_14; -. DR OMA; AEEWMHQ; -. DR OrthoDB; 9803053at2; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:InterPro. DR GO; GO:0043531; F:ADP binding; IEA:TreeGrafter. 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 CDD; cd18113; ATP-synt_F1_alpha_C; 1. DR CDD; cd18116; ATP-synt_F1_alpha_N; 1. DR CDD; cd01132; F1-ATPase_alpha_CD; 1. DR FunFam; 3.40.50.300:FF:000002; ATP synthase subunit alpha; 1. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1. DR Gene3D; 2.30.130.30; Hypothetical protein; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1. DR InterPro; IPR023366; ATP_synth_asu-like_sf. DR InterPro; IPR000793; ATP_synth_asu_C. DR InterPro; IPR038376; ATP_synth_asu_C_sf. DR InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom. DR InterPro; IPR005294; ATP_synth_F1_asu. 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; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00962; atpA; 1. DR NCBIfam; NF009884; PRK13343.1; 1. DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport; KW Ion transport; Membrane; Nucleotide-binding; Translocase; Transport. FT CHAIN 1..799 FT /note="ATP synthase subunit alpha" FT /id="PRO_0000238393" FT REGION 1..549 FT /note="ATP synthase alpha chain" FT REGION 550..799 FT /note="Unknown" FT BINDING 170..177 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT SITE 363 FT /note="Required for activity" FT /evidence="ECO:0000250" SQ SEQUENCE 799 AA; 89447 MW; 1A63E0F5C8982C8B CRC64; MTDNKNHSLI SDIKSQIKKF SEKALTLEVG NVISLGDGIV LVDGLDNVML NEIVRFENGV EGMALNLEED AVGVVLLGDY SNIKEGDRVY RTKRIVEVPV GDVMLGRVVD ALGKAVDNKG NIVANKFSVI EKIAPGVMDR KSVHQPLETG ILSIDAMFPI GKGQRELIIG DRQTGKTTIA IDAIINQKGR NVNCVYVAIG QKNSTIANVV RELEAHGAME YTTVVTANAS ELPALQYIAP FTGVTIAEEW MHQGKDVLIV YDDLSKHAIA YRTLSLLLRR PPGREAYPGD VFYLHSRLLE RACKLKDELG AGSITALPII ETQAGDISAY IPTNVISITD GQIFMMTSLF NAGQRPAIDA GQSVSRVGSA AQIKSVKQTG ASLKLELANY RELEAFSQFG SDLDDETKRI LKLGKAVMAV IKQAPNKPYN QTDEAIILFT VKEKLIPQVP VERIQDFKEY LLNYFKGTKL RADLEDKKAF DKENTPAFRC AIQKAINSFL NNSQDFKPCE EAEQTAFDKF FNENESIVVD GENDFNFINE EVSLKPTTET SEAVQIEEKV QDFVEPQEIL ETNKMEENHI FEEVEPEKII CEHHEFEIAE NQEKIEGQQV LEDTNHEYSI YETVEQSGEV DNDESKDDDL EVLVPVAEIE HDEAILDERE NRNWVFSDSA VSEVEKQTIM ISISSNEAEQ LFDNAKSVVF FKVTPKYPVE KVLVYVTSPV QKVVGEFDLL KIDVNSVNTS WNKYRSSSVI SSRKEYLEYF NSHKEAHALL ASKVYKYRKP KDLASFNMNK GPSGFTYLK //