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 05-DEC-2018, entry version 62. 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}; GN OrderedLocusNames=BLA_0632; OS Bifidobacterium animalis subsp. lactis (strain AD011). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC 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., RA Yoon S.H., Kim D.-W., Ji G.E., Park H.-S., Oh T.K.; RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis RT subsp. lactis AD011."; RL J. Bacteriol. 191:678-679(2009). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. {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; CC EC=7.1.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01346}; CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000255|HAMAP- CC Rule:MF_01346}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP- CC 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 SMR; B8DWS4; -. DR PRIDE; B8DWS4; -. DR EnsemblBacteria; ACL28925; ACL28925; BLA_0632. DR GeneID; 29696592; -. DR KEGG; bla:BLA_0632; -. DR PATRIC; fig|442563.4.peg.663; -. DR HOGENOM; HOG000130111; -. DR KO; K02111; -. DR OMA; GNAQIKS; -. DR BioCyc; BANI442563:G1GTZ-690-MONOMER; -. 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: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:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule. DR CDD; cd01132; F1_ATPase_alpha; 1. DR Gene3D; 1.20.150.20; -; 1. DR Gene3D; 2.40.30.20; -; 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. 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 Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome; KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding; KW Reference proteome; Translocase; Transport. FT CHAIN 1 546 ATP synthase subunit alpha. FT /FTId=PRO_1000166520. FT NP_BIND 173 180 ATP. {ECO:0000255|HAMAP-Rule:MF_01346}. FT SITE 374 374 Required for activity. FT {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 //