CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
101EGLVRGQKVLDTGYPacetylation[1]
175DLLAPYAKGGKIGLFacetylation[1]
403NVARGVQKILQDYKSacetylation[1]
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
 IPR003593; AAA+_ATPase.
 IPR020003; ATPase_a/bsu_AS.
 IPR004100; ATPase_a/bsu_N.
 IPR005722; ATPase_F1-cplx_bsu.
 IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
 IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
 IPR024034; ATPase_F1_bsu/V1_C.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N 
SMART
 SM00382; AAA 
PROSITE
 PS00152; ATPASE_ALPHA_BETA 
PRINTS