CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002163
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate--tRNA ligase 
Protein Synonyms/Alias
 Glutamyl-tRNA synthetase; GluRS 
Gene Name
 gltX 
Gene Synonyms/Alias
 b2400; JW2395 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
102AYKCYCSKERLEALRacetylation[1]
215PRQINILKALKAPVPacetylation[1]
236MINGDDGKKLSKRHGacetylation[1]
237INGDDGKKLSKRHGAacetylation[1]
284FTREEMIKYFTLNAVacetylation[1]
284FTREEMIKYFTLNAVpupylation[2]
345PQLADLVKLLGERCKacetylation[1]
377EFDADAAKKHLRPVAacetylation[1]
378FDADAAKKHLRPVARacetylation[3]
423ELEVGMGKVGMPLRVacetylation[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] 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]
 [3] 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
 Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). 
Sequence Annotation
 MOTIF 9 19 "HIGH" region.
 MOTIF 237 241 "KMSKS" region.
 METAL 98 98 Zinc.
 METAL 100 100 Zinc.
 METAL 125 125 Zinc.
 METAL 127 127 Zinc.
 BINDING 240 240 ATP (By similarity).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 471 AA 
Protein Sequence
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST PEAIEAIMDG 60
MNWLSLEWDE GPYYQTKRFD RYNAVIDQML EEGTAYKCYC SKERLEALRE EQMAKGEKPR 120
YDGRCRHSHE HHADDEPCVV RFANPQEGSV VFDDQIRGPI EFSNQELDDL IIRRTDGSPT 180
YNFCVVVDDW DMEITHVIRG EDHINNTPRQ INILKALKAP VPVYAHVSMI NGDDGKKLSK 240
RHGAVSVMQY RDDGYLPEAL LNYLVRLGWS HGDQEIFTRE EMIKYFTLNA VSKSASAFNT 300
DKLLWLNHHY INALPPEYVA THLQWHIEQE NIDTRNGPQL ADLVKLLGER CKTLKEMAQS 360
CRYFYEDFAE FDADAAKKHL RPVARQPLEV VRDKLAAITD WTAENVHHAI QATADELEVG 420
MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK TRSIERINKA LDFIAERENQ Q 471 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004818; F:glutamate-tRNA ligase activity; IDA:EcoCyc.
 GO:0000049; F:tRNA binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0006424; P:glutamyl-tRNA aminoacylation; IMP:EcoCyc. 
Interpro
 IPR008925; aa-tRNA-synth_I_codon-bd.
 IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
 IPR001412; aa-tRNA-synth_I_CS.
 IPR004527; Glu-tRNA-ligase_Ib_bac/mito.
 IPR000924; Glu/Gln-tRNA-synth_Ib.
 IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
 IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00749; tRNA-synt_1c 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00987; TRNASYNTHGLU.