CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001848
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isoleucine--tRNA ligase 
Protein Synonyms/Alias
 Isoleucyl-tRNA synthetase; IleRS 
Gene Name
 ileS 
Gene Synonyms/Alias
 ilvS; b0026; JW0024 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
23PMRGDLAKREPGMLAacetylation[1]
49RAAKKGKKTFILHDGacetylation[1, 2]
75HSVNKILKDIIVKSKacetylation[1]
105HGLPIELKVEQEYGKacetylation[1]
112KVEQEYGKPGEKFTAacetylation[1]
116EYGKPGEKFTAAEFRacetylation[1]
160PYLTMDFKTEANIIRacetylation[1]
183GHLHKGAKPVHWCVDacetylation[3]
390VVALLQEKGALLHVEacetylation[1, 2]
398GALLHVEKMQHSYPCacetylation[1, 2]
410YPCCWRHKTPIIFRAacetylation[1]
428WFVSMDQKGLRAQSLacetylation[1]
436GLRAQSLKEIKGVQWacetylation[1]
439AQSLKEIKGVQWIPDacetylation[1]
480PMSLFVHKDTEELHPacetylation[1]
498ELMEEVAKRVEVDGIacetylation[1]
605GQGRKMSKSIGNTVSacetylation[1]
619SPQDVMNKLGADILRacetylation[1, 2]
673LNGFDPAKDMVKPEEacetylation[1]
677DPAKDMVKPEEMVVLacetylation[1]
701AAQEDILKAYEAYDFacetylation[1]
814AFWDELLKVRGEVNKpupylation[4]
821KVRGEVNKVIEQARAacetylation[1]
887AQQSEVLKGLKVALSacetylation[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]
 [4] 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
 Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). 
Sequence Annotation
 MOTIF 58 68 "HIGH" region.
 MOTIF 602 606 "KMSKS" region.
 METAL 901 901 Zinc (By similarity).
 METAL 904 904 Zinc (By similarity).
 METAL 921 921 Zinc (By similarity).
 METAL 924 924 Zinc (By similarity).
 BINDING 561 561 Aminoacyl-adenylate (By similarity).
 BINDING 605 605 ATP (By similarity).
 MOD_RES 183 183 N6-acetyllysine.  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; Antibiotic resistance; 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
 938 AA 
Protein Sequence
MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT FILHDGPPYA 60
NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL PIELKVEQEY GKPGEKFTAA 120
EFRAKCREYA ATQVDGQRKD FIRLGVLGDW SHPYLTMDFK TEANIIRALG KIIGNGHLHK 180
GAKPVHWCVD CRSALAEAEV EYYDKTSPSI DVAFQAVDQD ALKAKFAVSN VNGPISLVIW 240
TTTPWTLPAN RAISIAPDFD YALVQIDGQA VILAKDLVES VMQRIGVTDY TILGTVKGAE 300
LELLRFTHPF MGFDVPAILG DHVTLDAGTG AVHTAPGHGP DDYVIGQKYG LETANPVGPD 360
GTYLPGTYPT LDGVNVFKAN DIVVALLQEK GALLHVEKMQ HSYPCCWRHK TPIIFRATPQ 420
WFVSMDQKGL RAQSLKEIKG VQWIPDWGQA RIESMVANRP DWCISRQRTW GVPMSLFVHK 480
DTEELHPRTL ELMEEVAKRV EVDGIQAWWD LDAKEILGDE ADQYVKVPDT LDVWFDSGST 540
HSSVVDVRPE FAGHAADMYL EGSDQHRGWF MSSLMISTAM KGKAPYRQVL THGFTVDGQG 600
RKMSKSIGNT VSPQDVMNKL GADILRLWVA STDYTGEMAV SDEILKRAAD SYRRIRNTAR 660
FLLANLNGFD PAKDMVKPEE MVVLDRWAVG CAKAAQEDIL KAYEAYDFHE VVQRLMRFCS 720
VEMGSFYLDI IKDRQYTAKA DSVARRSCQT ALYHIAEALV RWMAPILSFT ADEVWGYLPG 780
EREKYVFTGE WYEGLFGLAD SEAMNDAFWD ELLKVRGEVN KVIEQARADK KVGGSLEAAV 840
TLYAEPELSA KLTALGDELR FVLLTSGATV ADYNDAPADA QQSEVLKGLK VALSKAEGEK 900
CPRCWHYTQD VGKVAEHAEI CGRCVSNVAG DGEKRKFA 938 
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:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP.
 GO:0008270; F:zinc ion binding; IEA:HAMAP.
 GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR002301; Ile-tRNA-ligase.
 IPR023585; Ile-tRNA-ligase_type1.
 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.
 IPR010663; Znf_DNA_glyclase/IsotRNA_synth. 
Pfam
 PF08264; Anticodon_1
 PF00133; tRNA-synt_1
 PF06827; zf-FPG_IleRS 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00984; TRNASYNTHILE.