ID A0A139ZS18_9LILI Unreviewed; 480 AA. AC A0A139ZS18; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 03-MAY-2023, entry version 22. DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553}; DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553}; DE Flags: Fragment; GN Name=atpB {ECO:0000313|EMBL:AKA43878.1}; OS Ripogonum album. OG Plastid; Chloroplast {ECO:0000313|EMBL:AKA43878.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Ripogonaceae; OC Ripogonum. OX NCBI_TaxID=1159551 {ECO:0000313|EMBL:AKA43878.1}; RN [1] {ECO:0000313|EMBL:AKA43878.1} RP NUCLEOTIDE SEQUENCE. RA Nguyen V.L., Jang H.W., Kim J.S., Kim J.-H.; RT "Molecular phylogeny of family Liliaceae."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient CC across the membrane. {ECO:0000256|RuleBase:RU003553}. 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, CC 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). CC {ECO:0000256|RuleBase:RU003553}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|ARBA:ARBA00008936}. 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; KM198733; AKA43878.1; -; Genomic_DNA. DR AlphaFoldDB; A0A139ZS18; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. 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-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC. 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; 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 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 TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, KW ECO:0000256|RuleBase:RU003553}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553}; KW Chloroplast {ECO:0000313|EMBL:AKA43878.1}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000313|EMBL:AKA43878.1}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 161..353 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AKA43878.1" FT NON_TER 480 FT /evidence="ECO:0000313|EMBL:AKA43878.1" SQ SEQUENCE 480 AA; 51648 MW; 610E34B5019CA1CF CRC64; NPTTSGTGVS TLEEKNLGRI AQIIGPVLDV VFPPGKMPNI YNALVVKGRD TVGQQINVTC EVQQLLGNNR VRTVAMSATD GLMRGMEVID TGAPLSVPVG GATLGRIFNV LGEPVDDLGP VDTRTTSPIH RSAPAFIQLD TKLSIFETGI KVVDLLAPYR RGGKIGLFGG AGVGKTVLIM ELINNIAKAH GGVSVFGGVG ERTREGNDLY MEMKESGVIN EKNIAESKVA LVYGQMNEPP GARMRVGLTA LTMAEYFRDV NEQDVLLFID NIFRFVQAGS EVSALLGRMP SAVGYQPTLS TEMGSLQERI TSTKEGSITS IQAVYVPADD LTDPAPATTF AHLDATTVLS RGLAAKGIYP AVDPLDSTST MLQPRIVGEE HYEIAQRVKQ TSQRYKELQD IIAILGLDEL SEEDRLTVAR ARKIERFLSQ PFFVAEVFTG SPGKYVGLAE TIRGFQLILS GELDGLSEQA FYLVGNIDEA //