CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010218
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA 2-thiocytidine biosynthesis protein TtcA 
Protein Synonyms/Alias
  
Gene Name
 ttcA 
Gene Synonyms/Alias
 ydaO; b1344; JW1338 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
10ENQQITKKEQYNLNKacetylation[1]
17KEQYNLNKLQKRLRRacetylation[1]
20YNLNKLQKRLRRNVGacetylation[1]
112ENTYGIVKEKIPEGKacetylation[1]
233DMLRDWDKRYPGRIEacetylation[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] 
Functional Description
 Required for the thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). 
Sequence Annotation
 NP_BIND 47 52 ATP (Potential).
 MOTIF 122 125 CXXC.
 MOTIF 210 213 CXXC.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 311 AA 
Protein Sequence
MQENQQITKK EQYNLNKLQK RLRRNVGEAI ADFNMIEEGD RIMVCLSGGK DSYTMLEILR 60
NLQQSAPINF SLVAVNLDQK QPGFPEHVLP EYLEKLGVEY KIVEENTYGI VKEKIPEGKT 120
TCSLCSRLRR GILYRTATEL GATKIALGHH RDDILQTLFL NMFYGGKMKG MPPKLMSDDG 180
KHIVIRPLAY CREKDIQRFA DAKAFPIIPC NLCGSQPNLQ RQVIADMLRD WDKRYPGRIE 240
TMFSAMQNVV PSHLCDTNLF DFKGITHGSE VVNGGDLAFD REEIPLQPAC WQPEEDENQL 300
DELRLNVVEV K 311 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0006400; P:tRNA modification; IMP:EcoCyc. 
Interpro
 IPR012089; 2-thiocytidine_tRNA_synth_TtcA.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR011063; tRNA-lysidine/thiocyt_synth. 
Pfam
 PF01171; ATP_bind_3 
SMART
  
PROSITE
  
PRINTS