ATPBM_ORYSJ
ID ATPBM_ORYSJ Reviewed; 552 AA.
AC Q01859; Q0DG48; Q6I636;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=ATPB; OrderedLocusNames=Os05g0553000, LOC_Os05g47980;
GN ORFNames=OJ1263_E10.1, OSJNBa0079H23.20;
OS Oryza sativa subsp. japonica (Rice).
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].
RC STRAIN=cv. Nipponbare;
RX PubMed=1387558; DOI=10.1007/bf00029164;
RA Sakamoto M., Shimada H., Fujimura T.;
RT "Nucleotide sequence of a cDNA encoding a beta subunit of the mitochondrial
RT ATPase from rice (Oryza sativa).";
RL Plant Mol. Biol. 20:171-174(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 47-53, AND IDENTIFICATION BY
RP MASS 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).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
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 -!- 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 three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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; D10491; BAA01372.1; -; Genomic_DNA.
DR EMBL; AC093956; AAT58723.1; -; Genomic_DNA.
DR EMBL; AC129717; AAT85199.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18175.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS95236.1; -; Genomic_DNA.
DR EMBL; AK061681; BAG88054.1; -; mRNA.
DR PIR; S25304; S25304.
DR RefSeq; XP_015640019.1; XM_015784533.1.
DR AlphaFoldDB; Q01859; -.
DR SMR; Q01859; -.
DR STRING; 4530.OS05T0553000-02; -.
DR PaxDb; Q01859; -.
DR PRIDE; Q01859; -.
DR EnsemblPlants; Os05t0553000-02; Os05t0553000-02; Os05g0553000.
DR GeneID; 4339546; -.
DR Gramene; Os05t0553000-02; Os05t0553000-02; Os05g0553000.
DR KEGG; osa:4339546; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; Q01859; -.
DR OMA; NDLYHET; -.
DR OrthoDB; 495235at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q01859; baseline and differential.
DR Genevisible; Q01859; OS.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:Gramene.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEP:Gramene.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.10.10.910; -; 1.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR042079; ATP_synt_F1_beta_sf.
DR InterPro; IPR020971; ATP_synth_F1_beta_su.
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 Pfam; PF11421; Synthase_beta; 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 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Translocase; Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:16758443"
FT CHAIN 47..552
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002441"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 55..56
FT /note="AA -> R (in Ref. 1; BAA01372)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="V -> I (in Ref. 1; BAA01372)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="L -> V (in Ref. 1; BAA01372)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="E -> V (in Ref. 1; BAA01372)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="K -> R (in Ref. 1; BAA01372)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="K -> R (in Ref. 1; BAA01372)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> R (in Ref. 1; BAA01372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 58934 MW; 04069EF7CD7DF463 CRC64;
MATRRALSSL VRAASRLRGA SPAPRPRGPL HRPSPSGYLF NRAAAYATAA AAKEAAPPAP
ATGKATGGGK ITDEFTGAGA VGQVCQVIGA VVDVRFDEGL PPILTALEVL DHNIRLVLEV
AQHLGENMVR TIAMDGTEGL VRGQRVLNTG SPITVPVGRA TLGRIMNVIG EPIDEKGDIT
TNHFLPIHRE APAFVEQATE QQILVTGIKV VDLLAPYQRG GKIGLFGGAG VGKTVLIMEL
INNVAKAHGG FSVFAGVGER TREGNDLYRE MIESGVIKLG DKQSESKCAL VYGQMNEPPG
ARARVGLTGL TVAEHFRDAE GQDVLLFIDN IFRFTQANSE VSALLGRIPS AVGYQPTLAT
DLGGLQERIT TTKKGSITSV QAIYVPADDL TDPAPATTFA HLDATTVLSR QISELGIYPA
VDPLDSTSRM LSPHVLGEDH YNTARGVQKV LQNYKNLQDI IAILGMDELS EDDKLTVARA
RKIQRFLSQP FHVAEVFTGA PGKYVELKES VNSFQGVLDG KYDDLPEQSF YMVGGIEEVI
AKAEKIAKES AS
