CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003288
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase subunit beta 
Protein Synonyms/Alias
 ATP synthase F1 sector subunit beta; F-ATPase subunit beta 
Gene Name
 atpD 
Gene Synonyms/Alias
 papB; uncD; b3732; JW3710 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
70LRRGLDVKDLEHPIEacetylation[1, 2, 3]
82PIEVPVGKATLGRIMacetylation[2, 3]
99LGEPVDMKGEIGEEEacetylation[3]
142DLMCPFAKGGKVGLFacetylation[2, 3]
156FGGAGVGKTVNMMELacetylation[3]
202TDSNVIDKVSLVYGQacetylation[3]
230TGLTMAEKFRDEGRDacetylation[3]
372LQRYQELKDIIAILGacetylation[3]
417VFTGSPGKYVSLKDTacetylation[3]
422PGKYVSLKDTIRGFKacetylation[3]
Reference
 [1] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [3] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. 
Sequence Annotation
 NP_BIND 150 157 ATP (By similarity).  
Keyword
 3D-structure; ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Hydrolase; Ion transport; Membrane; Nucleotide-binding; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 460 AA 
Protein Sequence
MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG IVRTIAMGSS 60
DGLRRGLDVK DLEHPIEVPV GKATLGRIMN VLGEPVDMKG EIGEEERWAI HRAAPSYEEL 120
SNSQELLETG IKVIDLMCPF AKGGKVGLFG GAGVGKTVNM MELIRNIAIE HSGYSVFAGV 180
GERTREGNDF YHEMTDSNVI DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL 240
FVDNIYRYTL AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSVQAVYVP 300
ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV GQEHYDTARG 360
VQSILQRYQE LKDIIAILGM DELSEEDKLV VARARKIQRF LSQPFFVAEV FTGSPGKYVS 420
LKDTIRGFKG IMEGEYDHLP EQAFYMVGSI EEAVEKAKKL 460 
Gene Ontology
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IMP:EcoliWiki.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:HAMAP.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:EcoCyc.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:HAMAP. 
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