ID A0A386B0H5_CODAR Unreviewed; 480 AA. AC A0A386B0H5; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 24-JUL-2024, entry version 21. 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; TCBD clade; OC Bryopsidales; Bryopsidineae; 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) based on RT chloroplast phylogenomic analyses."; RL Mol. Phylogenet. Evol. 130:397-405(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; MH591107; AYC65195.1; -; Genomic_DNA. DR AlphaFoldDB; A0A386B0H5; -. 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:AYC65195.1}; 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:AYC65195.1}; 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 152..344 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT BINDING 160..167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="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 //