ID ATPB_ORYSJ Reviewed; 498 AA.
AC P12085; Q9MVP6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
GN OrderedLocusNames=LOC_Osp1g00410;
OS Oryza sativa subsp. japonica (Rice).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2954029; DOI=10.1093/nar/15.10.4358;
RA Moon E., Kao T.-H., Wu R.;
RT "Sequence of the chloroplast-encoded atpB-atpE-trnM gene clusters from
RT rice.";
RL Nucleic Acids Res. 15:4358-4359(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=2534354; DOI=10.1266/jjg.64.223;
RA Nishizawa Y., Hirai A.;
RT "The nucleotide sequences and expression of genes for the beta and epsilon
RT subunits of ATP synthase from rice (Oryza sativa L.).";
RL Jpn. J. Genet. 64:223-229(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nongken 58S; TISSUE=Leaf;
RA Wang T.;
RT "Oryza sativa chloroplast ATP synthase beta subunit gene, mRNA.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=2770692; DOI=10.1007/bf02464880;
RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., Mori M.,
RA Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., Kanno A.,
RA Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.;
RT "The complete sequence of the rice (Oryza sativa) chloroplast genome:
RT intermolecular recombination between distinct tRNA genes accounts for a
RT major plastid DNA inversion during the evolution of the cereals.";
RL Mol. Gen. Genet. 217:185-194(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15122023; DOI=10.1104/pp.103.031245;
RA Tang J., Xia H., Cao M., Zhang X., Zeng W., Hu S., Tong W., Wang J.,
RA Wang J., Yu J., Yang H., Zhu L.;
RT "A comparison of rice chloroplast genomes.";
RL Plant Physiol. 135:412-420(2004).
RN [6]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 1-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
RN [7]
RP INTERACTION WITH YL1.
RX PubMed=27585744; DOI=10.1038/srep32295;
RA Chen F., Dong G., Wu L., Wang F., Yang X., Ma X., Wang H., Wu J., Zhang Y.,
RA Wang H., Qian Q., Yu Y.;
RT "A nucleus-encoded chloroplast protein YL1 is involved in chloroplast
RT development and efficient biogenesis of chloroplast ATP synthase in rice.";
RL Sci. Rep. 6:32295-32295(2016).
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:0000255|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:0000255|HAMAP-Rule:MF_01347};
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) (By similarity). Interacts with
CC YL1 (PubMed:27585744). {ECO:0000255|HAMAP-Rule:MF_01347,
CC ECO:0000269|PubMed:27585744}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; M31464; AAA84588.1; -; Genomic_DNA.
DR EMBL; D00432; BAA00334.1; -; Genomic_DNA.
DR EMBL; AB037543; BAA90397.1; -; mRNA.
DR EMBL; X15901; CAA34003.1; -; Genomic_DNA.
DR EMBL; AY522330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JQ0230; PWRZB.
DR RefSeq; NP_039390.1; NC_001320.1.
DR AlphaFoldDB; P12085; -.
DR SMR; P12085; -.
DR BioGRID; 792830; 1.
DR STRING; 39947.P12085; -.
DR PaxDb; 39947-P12085; -.
DR GeneID; 3131462; -.
DR KEGG; osa:3131462; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_3_1; -.
DR InParanoid; P12085; -.
DR OrthoDB; 351573at2759; -.
DR Proteomes; UP000059680; Chloroplast.
DR Genevisible; P12085; OS.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; ISS:Gramene.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Chloroplast; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW Plastid; Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..498
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000144537"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT CONFLICT 37
FT /note="P -> R (in Ref. 2; BAA00334 and 4; CAA34003)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="D -> E (in Ref. 1; AAA84588)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="G -> V (in Ref. 3; BAA90397)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="N -> I (in Ref. 1; AAA84588)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="K -> N (in Ref. 1; AAA84588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 53955 MW; 1FE3601355A5B719 CRC64;
MRTNPTTSRP GVSTIEEKST GRIDQIIGPV LDVTFPPGKL PYIYNALVVK SRDTDGKQIN
VTCEVQQLLG NNRVRAVAMS ATDGLMRGME VIDTGAPLSV PVGGATLGRI FNVLGEPVDN
LGPVDTSATF PIHRSAPAFI ELDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEKNLEES KVALVYGQMN
EPPGARMRVG LTALTMAEYF RDVNKQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
TLSTEMGSLQ ERITSTKKGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLASKG
IYPAVDPLDS TSTMLQPRIV GNEHYETAQR VKQTLQRYKE LQDIIAILGL DELSEEDRLT
VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDGLP EQAFYLVGNI
DEASTKAINL EEENKLKK
//
