CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003106
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonine--tRNA ligase 
Protein Synonyms/Alias
 Threonyl-tRNA synthetase; ThrRS 
Gene Name
 thrS 
Gene Synonyms/Alias
 b1719; JW1709 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
33DIGPGLAKACIAGRVacetylation[1]
122EDVEALEKRMHELAEacetylation[1]
130RMHELAEKNYDVIKKacetylation[1]
169ENIAHDDKPGLYFHEacetylation[1]
197MRFCHHFKLMKTAGAacetylation[1, 2]
200CHHFKLMKTAGAYWRacetylation[1, 2]
226YGTAWADKKALNAYLacetylation[1, 2]
227GTAWADKKALNAYLQacetylation[1, 2]
286VFVRSKLKEYQYQEVacetylation[1, 2, 3]
294EYQYQEVKGPFMMDRacetylation[1]
306MDRVLWEKTGHWDNYacetylation[1]
314TGHWDNYKDAMFTTSacetylation[1]
330ENREYCIKPMNCPGHacetylation[2]
426KLSTRPEKRIGSDEMacetylation[1]
577KADLRNEKIGFKIREacetylation[1, 2]
599YMLVCGDKEVESGKVacetylation[1]
614AVRTRRGKDLGSMDVacetylation[1]
627DVNEVIEKLQQEIRSacetylation[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] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842] 
Functional Description
 ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA. 
Sequence Annotation
 REGION 243 534 Catalytic.
 METAL 334 334 Zinc; catalytic.
 METAL 385 385 Zinc; catalytic.
 METAL 511 511 Zinc; catalytic.
 MOD_RES 286 286 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; Repressor; RNA-binding; Translation regulation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 642 AA 
Protein Sequence
MPVITLPDGS QRHYDHAVSP MDVALDIGPG LAKACIAGRV NGELVDACDL IENDAQLSII 60
TAKDEEGLEI IRHSCAHLLG HAIKQLWPHT KMAIGPVIDN GFYYDVDLDR TLTQEDVEAL 120
EKRMHELAEK NYDVIKKKVS WHEARETFAN RGESYKVSIL DENIAHDDKP GLYFHEEYVD 180
MCRGPHVPNM RFCHHFKLMK TAGAYWRGDS NNKMLQRIYG TAWADKKALN AYLQRLEEAA 240
KRDHRKIGKQ LDLYHMQEEA PGMVFWHNDG WTIFRELEVF VRSKLKEYQY QEVKGPFMMD 300
RVLWEKTGHW DNYKDAMFTT SSENREYCIK PMNCPGHVQI FNQGLKSYRD LPLRMAEFGS 360
CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE EQIRDEVNGC IRLVYDMYST FGFEKIVVKL 420
STRPEKRIGS DEMWDRAEAD LAVALEENNI PFEYQLGEGA FYGPKIEFTL YDCLDRAWQC 480
GTVQLDFSLP SRLSASYVGE DNERKVPVMI HRAILGSMER FIGILTEEFA GFFPTWLAPV 540
QVVIMNITDS QSEYVNELTQ KLSNAGIRVK ADLRNEKIGF KIREHTLRRV PYMLVCGDKE 600
VESGKVAVRT RRGKDLGSMD VNEVIEKLQQ EIRSRSLKQL EE 642 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0005524; F:ATP binding; IDA:EcoliWiki.
 GO:0008144; F:drug binding; IDA:EcoliWiki.
 GO:0003723; F:RNA binding; IDA:EcoliWiki.
 GO:0004829; F:threonine-tRNA ligase activity; IDA:EcoCyc.
 GO:0000900; F:translation repressor activity, nucleic acid binding; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IMP:EcoliWiki.
 GO:0045947; P:negative regulation of translational initiation; IMP:EcoCyc.
 GO:0006435; P:threonyl-tRNA aminoacylation; IDA:EcoCyc. 
Interpro
 IPR002314; aa-tRNA-synt_IIb_cons-dom.
 IPR006195; aa-tRNA-synth_II.
 IPR004154; Anticodon-bd.
 IPR012675; Beta-grasp_dom.
 IPR004095; TGS.
 IPR012676; TGS-like.
 IPR002320; Thr-tRNA-ligase_IIa.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF03129; HGTP_anticodon
 PF02824; TGS
 PF00587; tRNA-synt_2b
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01047; TRNASYNTHTHR.