CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002542
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Leucine--tRNA ligase 
Protein Synonyms/Alias
 Leucyl-tRNA synthetase; LeuRS 
Gene Name
 leuS 
Gene Synonyms/Alias
 b0642; JW0637 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
21VQLHWDEKRTFEVTEacetylation[1]
32EVTEDESKEKYYCLSacetylation[1]
92PAEGAAVKNNTAPAPacetylation[1]
109YDNIAYMKNQLKMLGacetylation[1]
113AYMKNQLKMLGFGYDacetylation[1]
138EYYRWEQKFFTELYKacetylation[1]
145KFFTELYKKGLVYKKacetylation[1, 2]
186CDTKVERKEIPQWFIacetylation[1, 2]
208ELLNDLDKLDHWPDTacetylation[1]
217DHWPDTVKTMQRNWIacetylation[1]
300AEMATMEKKGVDTGFacetylation[1]
351RDYEFASKYGLNIKPacetylation[1]
357SKYGLNIKPVILAADacetylation[1]
378SQQALTEKGVLFNSGacetylation[1]
598AIVERDEKGRIVKAKacetylation[1]
605KGRIVKAKDAAGHELacetylation[1]
619LVYTGMSKMSKSKNNacetylation[1, 2]
622TGMSKMSKSKNNGIDacetylation[1]
624MSKMSKSKNNGIDPQacetylation[1]
675RFLKRVWKLVYEHTAacetylation[1]
707ALRRDVHKTIAKVTDacetylation[2]
738ELMNKLAKAPTDGEQacetylation[2]
837GQEHLVAKYLDGVTVacetylation[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
 MOTIF 42 52 "HIGH" region.
 MOTIF 619 623 "KMSKS" region.
 BINDING 622 622 ATP (By similarity).  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 860 AA 
Protein Sequence
MQEQYRPEEI ESKVQLHWDE KRTFEVTEDE SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD 60
VIARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIAYMKN QLKMLGFGYD 120
WSRELATCTP EYYRWEQKFF TELYKKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD 180
TKVERKEIPQ WFIKITAYAD ELLNDLDKLD HWPDTVKTMQ RNWIGRSEGV EITFNVNDYD 240
NTLTVYTTRP DTFMGCTYLA VAAGHPLAQK AAENNPELAA FIDECRNTKV AEAEMATMEK 300
KGVDTGFKAV HPLTGEEIPV WAANFVLMEY GTGAVMAVPG HDQRDYEFAS KYGLNIKPVI 360
LAADGSEPDL SQQALTEKGV LFNSGEFNGL DHEAAFNAIA DKLTAMGVGE RKVNYRLRDW 420
GVSRQRYWGA PIPMVTLEDG TVMPTPDDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG 480
MPALRETDTF DTFMESSWYY ARYTCPQYKE GMLDSEAANY WLPVDIYIGG IEHAIMHLLY 540
FRFFHKLMRD AGMVNSDEPA KQLLCQGMVL ADAFYYVGEN GERNWVSPVD AIVERDEKGR 600
IVKAKDAAGH ELVYTGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PADMTLEWQE 660
SGVEGANRFL KRVWKLVYEH TAKGDVAALN VDALTENQKA LRRDVHKTIA KVTDDIGRRQ 720
TFNTAIAAIM ELMNKLAKAP TDGEQDRALM QEALLAVVRM LNPFTPHICF TLWQELKGEG 780
DIDNAPWPVA DEKAMVEDST LVVVQVNGKV RAKITVPVDA TEEQVRERAG QEHLVAKYLD 840
GVTVRKVIYV PGKLLNLVVG 860 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004823; F:leucine-tRNA ligase activity; IDA:EcoCyc.
 GO:0006429; P:leucyl-tRNA aminoacylation; IDA:EcoCyc.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR002302; Leu-tRNA-ligase_bac/mito.
 IPR025709; Leu_tRNA-synth_edit.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd.
 IPR013155; V/L/I-tRNA-synth_anticodon-bd.
 IPR009008; Val/Leu/Ile-tRNA-synth_edit. 
Pfam
 PF08264; Anticodon_1
 PF00133; tRNA-synt_1
 PF13603; tRNA-synt_1_2 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00985; TRNASYNTHLEU.