CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003254
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK 
Protein Synonyms/Alias
  
Gene Name
 ybaK 
Gene Synonyms/Alias
 b0481; JW0470 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
6**MTPAVKLLEKNKIacetylation[1]
10PAVKLLEKNKISFQIacetylation[1]
12VKLLEKNKISFQIHTacetylation[1]
35NFGDEVVKKLGLNPDacetylation[1]
46LNPDQVYKTLLVAVNacetylation[1]
73VAGQLDLKKVAKALGacetylation[1]
74AGQLDLKKVAKALGAacetylation[1]
82VAKALGAKKVEMADPacetylation[1]
83AKALGAKKVEMADPMacetylation[1]
109GISPLGQKKRLPTIIacetylation[1]
110ISPLGQKKRLPTIIDacetylation[1]
132TIYVSGGKRGLDIELacetylation[1]
146LAAGDLAKILDAKFAacetylation[1]
151LAKILDAKFADIARRacetylation[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
Functional Description
 Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity. May compensate for the lack of Cys-tRNA(Pro) editing by ProRS. Is also able to deacylate Cys-tRNA(Cys), and displays weak deacylase activity in vitro against Gly-tRNA(Gly), as well as, at higher concentrations, some other correctly charged tRNAs. Unlike some of its orthologs it is not able to remove the amino acid moiety from incorrectly charged Ala-tRNA(Pro). 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Lyase; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 159 AA 
Protein Sequence
MTPAVKLLEK NKISFQIHTY EHDPAETNFG DEVVKKLGLN PDQVYKTLLV AVNGDMKHLA 60
VAVTPVAGQL DLKKVAKALG AKKVEMADPM VAQRSTGYLV GGISPLGQKK RLPTIIDAPA 120
QEFATIYVSG GKRGLDIELA AGDLAKILDA KFADIARRD 159 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0043907; F:Cys-tRNA(Pro) hydrolase activity; IDA:EcoCyc.
 GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
 GO:0006412; P:translation; IEA:UniProtKB-KW. 
Interpro
 IPR004369; Prolyl-tRNA_editing_YbaK/EbsC.
 IPR007214; YbaK/aa-tRNA-synth-assoc-dom. 
Pfam
 PF04073; YbaK 
SMART
  
PROSITE
  
PRINTS