CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003110
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine--tRNA ligase, heat inducible 
Protein Synonyms/Alias
 Lysyl-tRNA synthetase; LysRS 
Gene Name
 lysU 
Gene Synonyms/Alias
 b4129; JW4090 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
114GVYNDQFKKWDLGDIacetylation[1, 2, 3]
115VYNDQFKKWDLGDIIacetylation[2, 3]
156ALRPLPDKFHGLQDQacetylation[1, 2, 3]
179LDLIANDKSRQTFVVacetylation[3]
310QEVLGTTKVTYGEHVacetylation[2, 3]
322EHVFDFGKPFEKLTMacetylation[2, 3]
335TMREAIKKYRPETDMacetylation[2]
Reference
 [1] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [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
 Also can synthesize a number of adenyl dinucleotides (in particular AppppA). These dinucleotides have been proposed to act as modulators of the heat-shock response and stress response. 
Sequence Annotation
 METAL 415 415 Magnesium 1.
 METAL 422 422 Magnesium 1.
 METAL 422 422 Magnesium 2.
 MOD_RES 114 114 N6-acetyllysine.
 MOD_RES 156 156 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 505 AA 
Protein Sequence
MSEQETRGAN EAIDFNDELR NRREKLAALR QQGVAFPNDF RRDHTSDQLH EEFDAKDNQE 60
LESLNIEVSV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDSLPEGVYN DQFKKWDLGD 120
IIGARGTLFK TQTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEVRYRQR YLDLIANDKS 180
RQTFVVRSKI LAAIRQFMVA RGFMEVETPM MQVIPGGASA RPFITHHNAL DLDMYLRIAP 240
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYHDL IELTESLFRT 300
LAQEVLGTTK VTYGEHVFDF GKPFEKLTMR EAIKKYRPET DMADLDNFDA AKALAESIGI 360
TVEKSWGLGR IVTEIFDEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG 420
REIGNGFSEL NDAEDQAERF QEQVNAKAAG DDEAMFYDED YVTALEYGLP PTAGLGIGID 480
RMIMLFTNSH TIRDVILFPA MRPQK 505 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:EcoliWiki.
 GO:0004824; F:lysine-tRNA ligase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006430; P:lysyl-tRNA aminoacylation; IDA:EcoCyc. 
Interpro
 IPR004364; aa-tRNA-synt_II.
 IPR018150; aa-tRNA-synt_II-like.
 IPR006195; aa-tRNA-synth_II.
 IPR002313; Lys-tRNA-ligase_II.
 IPR018149; Lys-tRNA-synth_II_C.
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase. 
Pfam
 PF00152; tRNA-synt_2
 PF01336; tRNA_anti 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR00982; TRNASYNTHLYS.