※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||
Theoretical PI | 6.01 | ||||||||||||||||||||||||||||||
Molecular Weight | 59103.4 | ||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||
Protein Name | ATP synthase subunit beta, mitochondrial | ||||||||||||||||||||||||||||||
Gene Name | ATPB; ATP2 | ||||||||||||||||||||||||||||||
Created Date | 1990-11-01 | ||||||||||||||||||||||||||||||
Organism | Zea mays(Maize) | ||||||||||||||||||||||||||||||
NCBI Taxa ID | 4577 | ||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Sequence Annotation transit peptide 1 47 Mitochondrion chain 48 553 ATP synthase subunit beta, mitochondrial nucleotide phosphate-binding region 228 235 ATP Keyword ATP synthesis,ATP-binding,CF(1),Complete proteome,Hydrogen ion transport,Hydrolase,Ion transport,Membrane,Mitochondrion,Mitochondrion inner membrane,Nucleotide-binding,Reference proteome,Transit peptide,Transport Sequence Source UniProt Protein Sequence MASRRVVSSL LRSASRLRAA SPAAPRPRAP PHRPSPAGYL FNRAAAYASS AAAQAAPATP 60 PPATGKTGGG KITDEFTGAG AIGQVCQVIG AVVDVRFDEG LPPILTALEV LDNNIRLVLE 120 VAQHLGENMV RTIAMDGTEG LVRGQRVLNT GSPITVPVGR ATLGRIINVI GEPIDEKGDI 180 KTNHFLPIHR EAPAFVEQAT EQQILVTGIK VVDLLAPYQR GGKIGLFGGA GVGKTVLIME 240 LINNVAKAHG GFSVFAGVGE RTREGNDLYR EMIESGVIKL DDKQSESKCA LVYGQMNEPP 300 GARARVGLTG LTVAEHFRDA EGQDVLLFID NIFRFTQANS EVSALLGRIP SAVGYQPTLA 360 TDLGGLQERI TTTKKGSITS VQAIYVPADD LTDPAPATTF AHLDATTVLS RQISELGIYP 420 AVDPLDSTSR MLSPHVLGED HYNTARGVQK VLQNYKNLQD IIAILGMDEL SEDDKLTVAR 480 ARKIQRFLSQ PFHVAEVFTG APGKYVELKE SVKSFQGVLD GKYDDLPEQS FYMVGGIEEV 540 IAKAEKIAKE SAS 553 Gene Ontology GO:0000275; C: mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); IEA: InterPro GO:0005524; F: ATP binding; IEA: UniProtKB-KW GO:0046933; F: proton-transporting ATP synthase activity, rotational mechanism; IEA: InterPro GO:0015991; P: ATP hydrolysis coupled proton transport; IEA: InterPro GO:0015986; P: ATP synthesis coupled proton transport; IEA: InterPro Interpro InterPro; IPR003593; AAA+_ATPase InterPro; IPR020971; ATP_synthase_F1_beta_su InterPro; IPR020003; ATPase_a/bsu_AS InterPro; IPR005722; ATPase_F1-cplx_bsu InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd InterPro; IPR004100; ATPase_F1_a/bsu_N InterPro; IPR024034; ATPase_F1_bsu/V1_C InterPro; IPR027417; P-loop_NTPase Pfam SMART SMART; SM00382; AAA PROSITE PS00152; ATPASE_ALPHA_BETA PRINTS |