ID A0A290DR72_9ASPA Unreviewed; 495 AA. AC A0A290DR72; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 24-JUL-2024, entry version 22. DE RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01347}; DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347}; DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347}; DE AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347}; GN Name=atpB {ECO:0000256|HAMAP-Rule:MF_01347, GN ECO:0000313|EMBL:ATB18925.1}; OS Hosta minor. OG Plastid; Chloroplast {ECO:0000313|EMBL:ATB18925.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae; OC Agavoideae; Hosta. OX NCBI_TaxID=1035810 {ECO:0000313|EMBL:ATB18925.1}; RN [1] {ECO:0000313|EMBL:ATB18925.1} RP NUCLEOTIDE SEQUENCE. RA Park H., Kim C., Kim J.-H.; RT "The comparative plastid genome analysis and its phylogenetic implication RT on Asparagaceae s.l."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QHF17543.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=31706273; RA Lee S.R., Kim K., Lee B.Y., Lim C.E.; RT "Complete chloroplast genomes of all six Hosta species occurring in Korea: RT molecular structures, comparative, and phylogenetic analyses."; RL BMC Genomics 20:0-833(2019). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient CC across the membrane. The catalytic sites are hosted primarily by the CC beta subunits. {ECO:0000256|HAMAP-Rule:MF_01347}. 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, ECO:0000256|HAMAP- CC Rule:MF_01347, 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 four main CC subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000256|HAMAP- CC Rule:MF_01347, ECO:0000256|RuleBase:RU003553}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01347}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01347}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}. 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; KX822777; ATB18925.1; -; Genomic_DNA. DR EMBL; MK732316; QHF17543.1; -; Genomic_DNA. DR AlphaFoldDB; A0A290DR72; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:TreeGrafter. 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:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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 GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:TreeGrafter. 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; IPR050053; ATPase_alpha/beta_chains. 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, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347}; KW Chloroplast {ECO:0000313|EMBL:ATB18925.1}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01347}; Plastid {ECO:0000313|EMBL:ATB18925.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01347}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_01347}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}. FT DOMAIN 164..356 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT BINDING 172..179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347" SQ SEQUENCE 495 AA; 53299 MW; 727EB9E2E462AE50 CRC64; MKINPTTSGP AVSTLEEKNL GRIAQIIGPV LDVVFPPGKM PNIYNALVVK GRDTVGQQIN VTCEVQQLLG NNRVRAVAMS ATDGLTRGME VIDTGAALSV PVGGATLGRI FNVLGEPVDN LGPVDTRTTS PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEKNIAES KVALVYGQMN EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG IYPAVDPLDS TSTMLQPRIV GEEHYETAQR VKQTLQRYKE LQDIIAILGL DELSEEDRLT VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDSLP EQAFYLVGNI DEATAKAMNL EGEKK //