CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003287
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP synthase subunit alpha 
Protein Synonyms/Alias
 ATP synthase F1 sector subunit alpha; F-ATPase subunit alpha 
Gene Name
 atpA 
Gene Synonyms/Alias
 papA; uncA; b3734; JW3712 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
87ADLAEGMKVKCTGRIacetylation[1]
118LGAPIDGKGPLDHDGacetylation[1]
151QPVQTGYKAVDSMIPacetylation[1]
192NQRDSGIKCIYVAIGacetylation[1]
265IIYDDLSKQAVAYRQacetylation[1]
314EYVEAFTKGEVKGKTacetylation[1]
318AFTKGEVKGKTGSLTacetylation[1]
384VGGAAQTKIMKKLSGacetylation[1, 2]
387AAQTKIMKKLSGGIRacetylation[1]
388AQTKIMKKLSGGIRTacetylation[1]
419DLDDATRKQLDHGQKacetylation[2]
426KQLDHGQKVTELLKQacetylation[1]
432QKVTELLKQKQYAPMacetylation[1]
499YNDEIEGKLKGILDSacetylation[1]
501DEIEGKLKGILDSFKacetylation[1]
508KGILDSFKATQSW**acetylation[1]
Reference
 [1] 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]
 [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] 
Functional Description
 Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. 
Sequence Annotation
 NP_BIND 169 176 ATP (Probable).  
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
 513 AA 
Protein Sequence
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG EMISLPGNRY 60
AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG RGLLGRVVNT LGAPIDGKGP 120
LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY KAVDSMIPIG RGQRELIIGD RQTGKTALAI 180
DAIINQRDSG IKCIYVAIGQ KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY 240
AGCAMGEYFR DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER 300
AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLETNLF 360
NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY RELAAFSQFA SDLDDATRKQ 420
LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA AERGYLADVE LSKIGSFEAA LLAYVDRDHA 480
PLMQEINQTG GYNDEIEGKL KGILDSFKAT QSW 513 
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; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0015986; P:ATP synthesis coupled proton transport; IMP:EcoliWiki.
 GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:HAMAP. 
Interpro
 IPR020003; ATPase_a/bsu_AS.
 IPR004100; ATPase_a/bsu_N.
 IPR005294; ATPase_F1-cplx_asu.
 IPR023366; ATPase_F1/A1-cplx_a_su_N.
 IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
 IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
 IPR018538; HAS-barrel.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF09378; HAS-barrel 
SMART
  
PROSITE
 PS00152; ATPASE_ALPHA_BETA 
PRINTS