CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003189
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphate acetyltransferase 
Protein Synonyms/Alias
 Phosphotransacetylase 
Gene Name
 pta 
Gene Synonyms/Alias
 b2297; JW2294 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
38GVRLSVFKPIAQPRTacetylation[1]
71TTAAEPLKMSYVEGLacetylation[1, 2]
84GLLSSNQKDVLMEEIacetylation[1]
115EGLVPTRKHQFAQSLacetylation[1, 2]
174ITGVIVNKLNAPVDEacetylation[1]
198EIFDDSSKAKVNNVDacetylation[1]
208VNNVDPAKLQESSPLacetylation[1]
317EMDARISKLCERAFAacetylation[1, 2]
615ATRLAQEKRPDLMIDacetylation[1]
665NTGNTTYKAVQRSADacetylation[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
 Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. 
Sequence Annotation
 REGION 391 714 Phosphate acetyltransferase.  
Keyword
 Acyltransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 714 AA 
Protein Sequence
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRTGGDAP DQTTTIVRAN 60
SSTTTAAEPL KMSYVEGLLS SNQKDVLMEE IVANYHANTK DAEVVLVEGL VPTRKHQFAQ 120
SLNYEIAKTL NAEIVFVMSQ GTDTPEQLKE RIELTRNSFG GAKNTNITGV IVNKLNAPVD 180
EQGRTRPDLS EIFDDSSKAK VNNVDPAKLQ ESSPLPVLGA VPWSFDLIAT RAIDMARHLN 240
ATIINEGDIN TRRVKSVTFC ARSIPHMLEH FRAGSLLVTS ADRPDVLVAA CLAAMNGVEI 300
GALLLTGGYE MDARISKLCE RAFATGLPVF MVNTNTWQTS LSLQSFNLEV PVDDHERIEK 360
VQEYVANYIN ADWIESLTAT SERSRRLSPP AFRYQLTELA RKAGKRIVLP EGDEPRTVKA 420
AAICAERGIA TCVLLGNPAE INRVAASQGV ELGAGIEIVD PEVVRESYVG RLVELRKNKG 480
MTETVAREQL EDNVVLGTLM LEQDEVDGLV SGAVHTTANT IRPPLQLIKT APGSSLVSSV 540
FFMLLPEQVY VYGDCAINPD PTAEQLAEIA IQSADSAAAF GIEPRVAMLS YSTGTSGAGS 600
DVEKVREATR LAQEKRPDLM IDGPLQYDAA VMADVAKSKA PNSPVAGRAT VFIFPDLNTG 660
NTTYKAVQRS ADLISIGPML QGMRKPVNDL SRGALVDDIV YTIALTAIQS AQQQ 714 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008959; F:phosphate acetyltransferase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0019413; P:acetate biosynthetic process; IMP:EcoCyc.
 GO:0045733; P:acetate catabolic process; IMP:EcoCyc.
 GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IMP:EcoCyc.
 GO:0070689; P:L-threonine catabolic process to propionate; IMP:EcoCyc. 
Interpro
 IPR010766; DRTGG.
 IPR016475; P-Actrans_bac.
 IPR027417; P-loop_NTPase.
 IPR004614; P_AcTrfase.
 IPR002505; PTA_PTB. 
Pfam
 PF07085; DRTGG
 PF01515; PTA_PTB 
SMART
  
PROSITE
  
PRINTS