ID A0A2S1RGD1_9MAGN Unreviewed; 498 AA. AC A0A2S1RGD1; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 10-OCT-2018, entry version 3. DE RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01347}; DE EC=3.6.3.14 {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:AWH98894.1}; GN ORFNames=CUO15_0049 {ECO:0000313|EMBL:AWH98894.1}; OS Dysosma majoensis. OG Plastid; Chloroplast {ECO:0000313|EMBL:AWH98894.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Ranunculales; OC Berberidaceae; Berberidoideae; Dysosma. OX NCBI_TaxID=153728 {ECO:0000313|EMBL:AWH98894.1}; RN [1] {ECO:0000313|EMBL:AWH98894.1} RP NUCLEOTIDE SEQUENCE. RA Ye W.Q.; RT "Plastome organization, genome-based phylogeny and evolution of RT plastid genes in Podophylloideae species adapted to contrasting RT habitats."; RL Submitted (NOV-2017) 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: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {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; MG593047; AWH98894.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-UniRule. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:InterPro. 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:AWH98894.1}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347}; KW Hydrolase {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:AWH98894.1}; KW Thylakoid {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 498 AA; 53705 MW; 6E1D1D499DEB08E3 CRC64; MRINPTTSGP GFSALEEKNL GRIVQIIGPV LDVAFPPGKM PNIYNALVVK GQDTLGQQIN VTCEVQQLLG NNRIRAVAMS ATDGLMRGME VIDTGAALSV PVGGATLGRI FNVLGEPVDN LGPVDTRTTS PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEQNIAES KVALVYGQMN EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG IYPAVDPLDS TSTMLQPRIV GEEHYETAQK VKQTSQRYKE LQDIIAILGL DELSEEDRLT VARARKIERF LSQPFFVAEV FTGSPGKYVG LTETIRGFQL ILSGELDSLP EQAFYLVGNI DEATAKAINL DEESKLKK //