CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003109
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysine--tRNA ligase 
Protein Synonyms/Alias
 Lysyl-tRNA synthetase; LysRS 
Gene Name
 lysS 
Gene Synonyms/Alias
 asuD; herC; b2890; JW2858 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
20VDLNNELKTRREKLAacetylation[1]
82MTRRIMGKASFVTLQacetylation[1, 2]
114GVYNEQFKKWDLGDIacetylation[1, 2]
115VYNEQFKKWDLGDILacetylation[1, 2]
125LGDILGAKGKLFKTKacetylation[1]
132KGKLFKTKTGELSIHacetylation[1]
148TELRLLTKALRPLPDacetylation[1]
156ALRPLPDKFHGLQDQacetylation[1, 2]
245IAPELYLKRLVVGGFacetylation[1]
308LAQDILGKTEVTYGDacetylation[1]
322DVTLDFGKPFEKLTMacetylation[1]
326DFGKPFEKLTMREAIacetylation[1]
352LDNFDSAKAIAESIGacetylation[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
  
Sequence Annotation
 METAL 415 415 Magnesium 1 (By similarity).
 METAL 422 422 Magnesium 1 (By similarity).
 METAL 422 422 Magnesium 2 (By similarity).  
Keyword
 3D-structure; 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
MSEQHAQGAD AVVDLNNELK TRREKLANLR EQGIAFPNDF RRDHTSDQLH AEFDGKENEE 60
LEALNIEVAV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDDLPEGVYN EQFKKWDLGD 120
ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES 180
RNTFKVRSQI LSGIRQFMVN RGFMEVETPM MQVIPGGAAA RPFITHHNAL DLDMYLRIAP 240
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT 300
LAQDILGKTE VTYGDVTLDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS AKAIAESIGI 360
HVEKSWGLGR IVTEIFEEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG 420
REIGNGFSEL NDAEDQAQRF LDQVAAKDAG DDEAMFYDED YVTALEHGLP PTAGLGIGID 480
RMVMLFTNSH TIRDVILFPA MRPVK 505 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004824; F:lysine-tRNA ligase activity; IGI:EcoliWiki.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006430; P:lysyl-tRNA aminoacylation; IGI:EcoliWiki. 
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.