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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}.
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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
 
 
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