CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001852
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glycine--tRNA ligase beta subunit 
Protein Synonyms/Alias
 Glycyl-tRNA synthetase beta subunit; GlyRS 
Gene Name
 glyS 
Gene Synonyms/Alias
 glyS(B); b3559; JW3530 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
18GTEELPPKALRSLAEacetylation[1]
72QPDREIEKRGPAIAQacetylation[1]
86QAFDAEGKPSKAAEGacetylation[1]
112AERLTTDKGEWLLYRacetylation[1]
141MVATSLAKLPIPKLMacetylation[1]
146LAKLPIPKLMRWGASacetylation[1]
171VTLLLGDKVIPATILacetylation[1]
268LTAKFEEKFLAVPAEacetylation[1]
282EALVYTMKGDQKYFPacetylation[1]
286YTMKGDQKYFPVYANacetylation[1]
310FVANIESKDPQQIISacetylation[1]
321QIISGNEKVVRPRLAacetylation[1]
472FGIGQHPKGDKDPFAacetylation[1]
475GQHPKGDKDPFALRRacetylation[1, 2]
584AALAAANKRVSNILAacetylation[1]
592RVSNILAKSDEVLSDacetylation[1, 2]
607RVNASTLKEPEEIKLacetylation[1]
624QVVVLRDKLEPYFTEacetylation[1]
624QVVVLRDKLEPYFTEpupylation[3]
662VMVMVDDKELRINRLacetylation[1]
674NRLTMLEKLRELFLRacetylation[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]
 [3] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 689 AA 
Protein Sequence
MSEKTFLVEI GTEELPPKAL RSLAESFAAN FTAELDNAGL AHGTVQWFAA PRRLALKVAN 60
LAEAQPDREI EKRGPAIAQA FDAEGKPSKA AEGWARGCGI TVDQAERLTT DKGEWLLYRA 120
HVKGESTEAL LPNMVATSLA KLPIPKLMRW GASDVHFVRP VHTVTLLLGD KVIPATILGI 180
QSDRVIRGHR FMGEPEFTID NADQYPEILR ERGKVIADYE ERKAKIKADA EEAARKIGGN 240
ADLSESLLEE VASLVEWPVV LTAKFEEKFL AVPAEALVYT MKGDQKYFPV YANDGKLLPN 300
FIFVANIESK DPQQIISGNE KVVRPRLADA EFFFNTDRKK RLEDNLPRLQ TVLFQQQLGT 360
LRDKTDRIQA LAGWIAEQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD 420
GEAEDVAVAL NEQYQPRFAG DDLPSNPVAC ALAIADKMDT LAGIFGIGQH PKGDKDPFAL 480
RRAALGVLRI IVEKNLNLDL QTLTEEAVRL YGDKLTNANV VDDVIDFMLG RFRAWYQDEG 540
YTVDTIQAVL ARRPTRPADF DARMKAVSHF RTLDAAAALA AANKRVSNIL AKSDEVLSDR 600
VNASTLKEPE EIKLAMQVVV LRDKLEPYFT EGRYQDALVE LAELREPVDA FFDKVMVMVD 660
DKELRINRLT MLEKLRELFL RVADISLLQ 689 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004820; F:glycine-tRNA ligase activity; IEA:EC.
 GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR008909; DALR_anticod-bd.
 IPR015944; Gly-tRNA-synth_bsu.
 IPR006194; Gly-tRNA-synth_heterodimer. 
Pfam
 PF05746; DALR_1
 PF02092; tRNA_synt_2f 
SMART
 SM00836; DALR_1 
PROSITE
 PS50861; AA_TRNA_LIGASE_II_GLYAB 
PRINTS
 PR01045; TRNASYNTHGB.