Tag | Content |
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CPLM ID | CPLM-011317 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP synthase subunit beta, mitochondrial |
Protein Synonyms/Alias | |
Gene Name | ATPsyn-beta |
Gene Synonyms/Alias | CG11154 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
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101 | EGLVRGQKVLDTGYP | acetylation | [1] | 175 | DLLAPYAKGGKIGLF | acetylation | [1] | 403 | NVARGVQKILQDYKS | acetylation | [1] |
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Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
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 | NP_BIND 183 190 ATP (By similarity). |
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 (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 505 AA |
Protein Sequence | MFALRAASKA DKNLLPFLGQ LSRSHAAKAA KAAAAANGKI VAVIGAVVDV QFDDNLPPIL 60 NALEVDNRSP RLVLEVAQHL GENTVRTIAM DGTEGLVRGQ KVLDTGYPIR IPVGAETLGR 120 IINVIGEPID ERGPIDTDKT AAIHAEAPEF VQMSVEQEIL VTGIKVVDLL APYAKGGKIG 180 LFGGAGVGKT VLIMELINNV AKAHGGYSVF AGVGERTREG NDLYNEMIEG GVISLKDKTS 240 KVALVYGQMN EPPGARARVA LTGLTVAEYF RDQEGQDVLL FIDNIFRFTQ AGSEVSALLG 300 RIPSAVGYQP TLATDMGSMQ ERITTTKKGS ITSVQAIYVP ADDLTDPAPA TTFAHLDATT 360 VLSRAIAELG IYPAVDPLDS TSRIMDPNII GQEHYNVARG VQKILQDYKS LQDIIAILGM 420 DELSEEDKLT VARARKIQRF LSQPFQVAEV FTGHAGKLVP LEQTIKGFSA ILAGDYDHLP 480 EVAFYMVGPI EEVVEKADRL AKEAA 505 |
Gene Ontology | GO:0005811; C:lipid particle; IDA:FlyBase. GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:FlyBase. GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. 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. GO:0046331; P:lateral inhibition; IMP:FlyBase. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |