ID ATPA_BIFA0 Reviewed; 546 AA. AC B8DWS4; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 29-MAY-2024, entry version 84. DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=BLA_0632; OS Bifidobacterium animalis subsp. lactis (strain AD011). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=442563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AD011; RX PubMed=19011029; DOI=10.1128/jb.01515-08; RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H., RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.; RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp. RT lactis AD011."; RL J. Bacteriol. 191:678-679(2009). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient CC across the membrane. The alpha chain is a regulatory subunit. CC {ECO:0000255|HAMAP-Rule:MF_01346}. 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_01346}; 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 {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01346}; CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000255|HAMAP-Rule:MF_01346}. 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; CP001213; ACL28925.1; -; Genomic_DNA. DR RefSeq; WP_004219176.1; NC_011835.1. DR AlphaFoldDB; B8DWS4; -. DR SMR; B8DWS4; -. DR STRING; 442563.BLA_0632; -. DR GeneID; 66533763; -. DR KEGG; bla:BLA_0632; -. DR PATRIC; fig|442563.4.peg.663; -. DR HOGENOM; CLU_010091_2_1_11; -. DR Proteomes; UP000002456; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. 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 GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC. 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 Gene3D; 2.40.30.20; -; 1. DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 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 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; Reference proteome; KW Translocase; Transport. FT CHAIN 1..546 FT /note="ATP synthase subunit alpha" FT /id="PRO_1000166520" FT REGION 520..546 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 173..180 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346" FT SITE 374 FT /note="Required for activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346" SQ SEQUENCE 546 AA; 58987 MW; 73BB353714D66C6A CRC64; MAELTIDPAT IRKALDDFVE AYTPSETPTQ EVGHVATAGD GIAHVTGLPG CMANELLTFE DGTLGLAFNL DAREIGVVIL GDFVGIEEGQ EVRRTGEVLS VPVGDGFLGR VVDPLGRPID GMGEIKSEGR RILEAQAPDV MHRHPVDQPM STGLKAIDAM TPIGRGQRQL IIGDRQTGKT AIAIDTIINQ KKNWESGDPK KQVRCIYVAI GQKGSTIASV KQSLEEAGAM EYTTIVASPA SDSAGFKYIA PYTGSAIGQH WMYNGKDVLI VFDDLSKQAE AYRSISLLLR RPPGREAYPG DVFYLHSRLL ERCARVSDDL GGGSMTGLPI VETKANDVSA YIPTNVISIT DGQIFLQSDL FNAGQRPAVD VGISVSRVGG AAQTKALKKV SGTLKISLAR YRSLESFAMF ASDLDAASKA QLNRGARLTE LLKQPQFSPY SMEQEVVSVW AGTHGKFDDL AIADVLPFEH GLLEYVDRNT DILTTIRDTG DFTKETEEAL DKAVDAFRET YVTKAGKPLV DKKTAPKSVT PVDQEQIKAG KAQEKK //