ID A0A290DR72_9ASPA Unreviewed; 495 AA. AC A0A290DR72; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 31-JUL-2019, entry version 7. 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 RT implication on Asparagaceae s.l."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The catalytic sites are hosted CC primarily by the 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; CC EC=7.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01347, CC ECO:0000256|RuleBase:RU003553}; 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 four main subunits: a(1), b(1), b'(1) and c(9-12). CC {ECO:0000256|HAMAP-Rule:MF_01347, ECO:0000256|RuleBase:RU004289}. 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|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 GO; GO:0009535; C:chloroplast thylakoid 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 Gene3D; 1.10.1140.10; -; 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 Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01347, KW ECO:0000256|RuleBase:RU003553}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01347, KW ECO:0000256|RuleBase:RU003553}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01347, KW ECO:0000256|RuleBase:RU003553}; KW Chloroplast {ECO:0000313|EMBL:ATB18925.1}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01347}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01347}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01347, KW ECO:0000256|RuleBase:RU003553}; KW Plastid {ECO:0000313|EMBL:ATB18925.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01347}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01347}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01347}. FT DOMAIN 164 356 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 172 179 ATP. {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 //