CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004489
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proline--tRNA ligase 
Protein Synonyms/Alias
 Global RNA synthesis factor; Prolyl-tRNA synthetase; ProRS 
Gene Name
 proS 
Gene Synonyms/Alias
 drpA; b0194; JW0190 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
12QYLLSTLKETPADAEacetylation[1]
34LRAGMIRKLASGLYTacetylation[1, 2]
126RNELSSYKQLPLNFYacetylation[1]
276QFNLPIEKTVKTLLVacetylation[1]
279LPIEKTVKTLLVKAVacetylation[1]
311LNEVKAEKLPQVASPacetylation[1]
420HIFQLGTKYSEALKAacetylation[1]
426TKYSEALKASVQGEDpupylation[3]
485ILPMNMHKSFRVQELacetylation[1]
495RVQELAEKLYSELRAacetylation[1]
495RVQELAEKLYSELRApupylation[3]
513EVLLDDRKERPGVMFacetylation[1]
547DNDDIEYKYRRNGEKacetylation[1]
554KYRRNGEKQLIKTGDacetylation[1]
568DIVEYLVKQIKG***acetylation[1]
571EYLVKQIKG******pupylation[3]
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
 Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by YbaK. 
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
 572 AA 
Protein Sequence
MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGVRVL KKVENIVREE 60
MNNAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG ERPFVLGPTH EEVITDLIRN 120
ELSSYKQLPL NFYQIQTKFR DEVRPRFGVM RSREFLMKDA YSFHTSQESL QETYDAMYAA 180
YSKIFSRMGL DFRAVQADTG SIGGSASHEF QVLAQSGEDD VVFSDTSDYA ANIELAEAIA 240
PKEPRAAATQ EMTLVDTPNA KTIAELVEQF NLPIEKTVKT LLVKAVEGSS FPQVALLVRG 300
DHELNEVKAE KLPQVASPLT FATEEEIRAV VKAGPGSLGP VNMPIPVVID RTVAAMSDFA 360
AGANIDGKHY FGINWDRDVA TPEVADIRNV VAGDPSPDGQ GRLLIKRGIE VGHIFQLGTK 420
YSEALKASVQ GEDGRNQILT MGCYGIGVTR VVAAAIEQNY DERGIVWPDA IAPFQVAILP 480
MNMHKSFRVQ ELAEKLYSEL RAQGIEVLLD DRKERPGVMF ADMELIGIPH TIVLGDRNLD 540
NDDIEYKYRR NGEKQLIKTG DIVEYLVKQI KG 572 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0043906; F:Ala-tRNA(Pro) hydrolase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004827; F:proline-tRNA ligase activity; IDA:EcoCyc.
 GO:0006433; P:prolyl-tRNA aminoacylation; IMP:EcoCyc. 
Interpro
 IPR002314; aa-tRNA-synt_IIb_cons-dom.
 IPR006195; aa-tRNA-synth_II.
 IPR004154; Anticodon-bd.
 IPR002316; Pro-tRNA-ligase_IIa.
 IPR004500; Pro-tRNA-synth_IIa_bac-type.
 IPR023717; Pro-tRNA-Synthase_IIa_type1.
 IPR007214; YbaK/aa-tRNA-synth-assoc-dom. 
Pfam
 PF03129; HGTP_anticodon
 PF00587; tRNA-synt_2b
 PF04073; YbaK 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01046; TRNASYNTHPRO.