CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001853
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamine--tRNA ligase 
Protein Synonyms/Alias
 Glutaminyl-tRNA synthetase; GlnRS 
Gene Name
 glnS 
Gene Synonyms/Alias
 b0680; JW0666 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
24DEDLASGKHTTVHTRacetylation[1]
73FDDTNPVKEDIEYVEacetylation[1]
160ENLALFEKMRAGGFEacetylation[1]
170AGGFEEGKACLRAKIacetylation[1]
176GKACLRAKIDMASPFacetylation[1]
195DPVLYRIKFAEHHQTacetylation[1, 2]
271LEYTVMSKRKLNLLVacetylation[1]
273YTVMSKRKLNLLVTDacetylation[1, 2]
281LNLLVTDKHVEGWDDacetylation[1]
399DFREEANKQYKRLVLacetylation[1]
408YKRLVLGKEVRLRNAacetylation[1, 2]
419LRNAYVIKAERVEKDacetylation[1]
454PADGRKVKGVIHWVSacetylation[1, 2]
509GFAEPSLKDAVAGKAacetylation[1]
515LKDAVAGKAFQFEREacetylation[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 34 44 "HIGH" region.
 MOTIF 268 272 "KMSKS" region.
 BINDING 271 271 ATP (By similarity).  
Keyword
 3D-structure; 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
 554 AA 
Protein Sequence
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG 60
QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA 120
YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA 180
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 240
YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 300
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE 360
GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA 420
ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP 480
NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN 540
RTVGLRDTWA KVGE 554 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0004819; F:glutamine-tRNA ligase activity; IDA:EcoCyc.
 GO:0006425; P:glutaminyl-tRNA aminoacylation; IDA:EcoCyc.
 GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:HAMAP. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR004514; Gln-tRNA-synth_Ib.
 IPR022861; Gln_tRNA_ligase_bac.
 IPR000924; Glu/Gln-tRNA-synth_Ib.
 IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
 IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
 IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
 IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl.
 IPR011035; Ribosomal_L25/Gln-tRNA_synth.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00749; tRNA-synt_1c
 PF03950; tRNA-synt_1c_C 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00987; TRNASYNTHGLU.