ID A0A386B0H5_CODAR Unreviewed; 480 AA. AC A0A386B0H5; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 10-APR-2019, entry version 4. 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:AYC65195.1}; OS Codium arabicum (Green alga). OG Plastid; Chloroplast {ECO:0000313|EMBL:AYC65195.1}. OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Bryopsidales; OC Codiaceae; Codium. OX NCBI_TaxID=221038 {ECO:0000313|EMBL:AYC65195.1}; RN [1] {ECO:0000313|EMBL:AYC65195.1} RP NUCLEOTIDE SEQUENCE. RA Quirk P.G., Krulwich T.A.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AYC65195.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30227214; DOI=10.1016/j.ympev.2018.09.009; RA Cremen M.C., Leliaert F., West J., Lam D.W., Shimada S., RA Lopez-Bautista J.M., Verbruggen H.; RT "Reassessment of the classification of Bryopsidales (Chlorophyta) RT based on chloroplast phylogenomic analyses."; RL Mol. Phylogenet. Evol. 130:397-405(2019). 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; MH591107; AYC65195.1; -; 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:AYC65195.1}; 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:AYC65195.1}; 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 152 344 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 160 167 ATP. {ECO:0000256|HAMAP-Rule:MF_01347}. SQ SEQUENCE 480 AA; 52138 MW; E854E64A0A89EE58 CRC64; MNTKTQNIGH VTQIIGPVLD ISFPPSKMPN IYNSLIIEGK NSAGDTINVT CEVQQLLGDH CVRAISMSAT DGLMRGMQVF DTGKPLTVPV GIATLGRIFN VLGEAVDNLG PVQADMGFEI HRSAPAFVDL DTKLAIFETG IKVVDLLAPY RRGGKIGLFG GAGVGKTVLI MELINNIAKA HGGVSVFGGV GERTREGNDL YMEMKESKVI NEENLKESKV ALVYGQMNEP PGARMRVGLT ALTMAEYFRD INKQDVLLFI DNIFRFVQAG SEVSALLGRM PSAVGYQPTL ASEMGGLQER ITSTKNGSIT SIQAIYVPAD DLTDPAPATT FAHLDATTVL SRSLASKGIY PAVDPLDSTS TMLQPWIVGD EHYDCAQTVK QTLQRYKELQ DIIAILGLDE LSEEDRLVVA RARKIERFLS QPFFVAEVFT GSPGKYVSLQ ETIRGFNLIL TGQLDNLPEQ SFYLVGTIDE AIEKATTLQD //