※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proline--tRNA ligase
Protein Synonyms/Alias
 ProRS
Gene Name
 proS
Gene Synonyms/Alias
 drpA; OrderedLocusNames=b0194, JW0190
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
37 GMIRKLASGLYTWLP S HTP [1]
460 AAAIEQNYDERGIVW Y HTP [2]
Reference
 [1]Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium.
 Soares NC,Spät P,Krug K,Macek B
 J. Proteome Res. 2013, Jun, 7;12(6):2611-21. [PMID:23590516]
 [2]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence.
 Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A
 PLoS Pathog. 2013;9(6):e1003403. [PMID:23785281]
Functional Description From UniProt
 FUNCTION: 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 From UniProt
 
Key Word From UniProt
 Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Directproteinsequencing; Ligase; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome
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
  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
  GO:0006450   P:regulation of translational fidelity IDA:GOC
  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.
  PF03129   HGTP_anticodon.
  PF00587   tRNA-synt_2b.
  PF04073   tRNA_edit.
  PS50862   AA_TRNA_LIGASE_II.
  PR01046   TRNASYNTHPRO.