CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003164
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase 
Protein Synonyms/Alias
 Tetrahydrodipicolinate N-succinyltransferase; THDP succinyltransferase; THP succinyltransferase; Tetrahydropicolinate succinylase 
Gene Name
 dapD 
Gene Synonyms/Alias
 b0166; JW0161 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
48GALRVAEKIDGQWVTacetylation[1]
60WVTHQWLKKAVLLSFacetylation[1]
61VTHQWLKKAVLLSFRacetylation[1, 2]
85AESRYFDKVPMKFADacetylation[1, 3]
89YFDKVPMKFADYDEAacetylation[1]
100YDEARFQKEGFRVVPacetylation[1, 3]
100YDEARFQKEGFRVVPpupylation[4]
241VSGNLPSKDGKYSLYacetylation[1]
244NLPSKDGKYSLYCAVacetylation[1]
254LYCAVIVKKVDAKTRacetylation[1]
263VDAKTRGKVGINELLacetylation[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]
 [3] 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]
 [4] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222
Functional Description
  
Sequence Annotation
 BINDING 104 104 Substrate (By similarity).
 BINDING 141 141 Substrate (By similarity).  
Keyword
 Acyltransferase; Amino-acid biosynthesis; Complete proteome; Cytoplasm; Diaminopimelate biosynthesis; Direct protein sequencing; Lysine biosynthesis; Reference proteome; Repeat; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 274 AA 
Protein Sequence
MQQLQNIIET AFERRAEITP ANADTVTREA VNQVIALLDS GALRVAEKID GQWVTHQWLK 60
KAVLLSFRIN DNQVIEGAES RYFDKVPMKF ADYDEARFQK EGFRVVPPAA VRQGAFIARN 120
TVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED 180
NCFIGARSEV VEGVIVEEGS VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVSGNLPS 240
KDGKYSLYCA VIVKKVDAKT RGKVGINELL RTID 274 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IDA:EcoCyc.
 GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP.
 GO:0009085; P:lysine biosynthetic process; IDA:EcoCyc.
 GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:HAMAP. 
Interpro
 IPR005664; DapD_Trfase_Hexpep_rpt_fam.
 IPR001451; Hexapep_transf.
 IPR018357; Hexapep_transf_CS.
 IPR023180; THP_succinylTrfase_dom1.
 IPR011004; Trimer_LpxA-like. 
Pfam
 PF00132; Hexapep 
SMART
  
PROSITE
 PS00101; HEXAPEP_TRANSFERASES 
PRINTS