ID G7J108_MEDTR Unreviewed; 490 AA. AC G7J108; A0A0C3VEP2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 2. DT 13-SEP-2023, entry version 62. DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553}; DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553}; GN OrderedLocusNames=MTR_3g035730 {ECO:0000313|EMBL:AES69836.2}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES69836.2, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:AES69836.2, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:AES69836.2}, and cv. Jemalong A17 RC {ECO:0000313|EnsemblPlants:AES69836, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K., RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., RA Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [2] {ECO:0000313|EMBL:AES69836.2, ECO:0000313|Proteomes:UP000002051} RP GENOME REANNOTATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES69836, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume Medicago RT truncatula."; RL BMC Genomics 15:312-312(2014). RN [3] {ECO:0000313|EnsemblPlants:AES69836} RP IDENTIFICATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES69836}; RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient CC across the membrane. {ECO:0000256|RuleBase:RU003553}. 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:0000256|ARBA:ARBA00001741, CC ECO:0000256|RuleBase:RU003553}; 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, b and c. {ECO:0000256|RuleBase:RU003553}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|ARBA:ARBA00008936}. 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; CM001219; AES69836.2; -; Genomic_DNA. DR RefSeq; XP_003599585.2; XM_003599537.2. DR AlphaFoldDB; G7J108; -. DR EnsemblPlants; AES69836; AES69836; MTR_3g035730. DR Gramene; AES69836; AES69836; MTR_3g035730. DR HOGENOM; CLU_022398_0_3_1; -. DR Proteomes; UP000002051; Chromosome 3. DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central. DR CDD; cd18110; ATP-synt_F1_beta_C; 1. DR CDD; cd18115; ATP-synt_F1_beta_N; 1. DR CDD; cd01133; F1-ATPase_beta_CD; 1. DR Gene3D; 2.40.10.170; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_01347; ATP_synth_beta_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR005722; ATP_synth_F1_bsu. 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; IPR024034; ATPase_F1/V1_b/a_C. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01039; atpD; 1. DR PANTHER; PTHR15184; ATP SYNTHASE; 1. DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 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 {ECO:0000256|ARBA:ARBA00023310, KW ECO:0000256|RuleBase:RU003553}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU003553}; KW Reference proteome {ECO:0000313|Proteomes:UP000002051}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 164..356 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" SQ SEQUENCE 490 AA; 52678 MW; 76156F253BA46349 CRC64; MRLTPTTSDT EVSGLEKKNI GRITQIIGPV LDVVFPPGKM PNIYNALIVQ GRDTVGQEIN VTCEVQQLLG NNRVRAVAIS ATDGLKRGMV VINTGAPLSV PVGGATLGRI FNVLGEPIDN LGPVDTGTTS PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFG GVGELTREGN DLYMEMKESG VINEKNIAES KVALVYGQMN EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLGTEMGTLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLASKG IYPAVDPLDS TSTMLQPRIV GEEHYETAQR VKQTLQRYKE LQDIIAILGL DELSEEDRLT VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFKL ILSGELDSLP EQAFYLVGNI DEATAKAANL //