CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003394
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome-associated inhibitor A 
Protein Synonyms/Alias
 Protein Y; SpotY; pY 
Gene Name
 raiA 
Gene Synonyms/Alias
 yfiA; b2597; JW2578 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
29DRLAKLEKWQTHLINacetylation[1]
43NPHIILSKEPQGFVAacetylation[1]
66GVLVASGKHEDMYTAacetylation[2]
80AINELINKLERQLNKacetylation[1]
87KLERQLNKLQHKGEAacetylation[1]
91QLNKLQHKGEARRAAacetylation[3]
102RRAATSVKDANFVEEacetylation[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] 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]
 [3] 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
Functional Description
 During stationary phase, prevents 70S dimer formation, probably in order to regulate translation efficiency during transition between the exponential and the stationary phases. In addition, during environmental stress such as cold shock or excessive cell density at stationary phase, stabilizes the 70S ribosome against dissociation, inhibits translation initiation and increase translation accuracy. When normal growth conditions are restored, is quickly released from the ribosome. Inhibits translation initiation by blocking the A-site (aminoacyl-tRNA site) and P-site (peptidyl-tRNA site) of the ribosome. Counteracts miscoding (translation errors) particularly efficiently at magnesium concentrations close to those observed in vivo but less efficiently at higher concentrations. Counteraction of miscoding was shown to be stronger than inhibition of translation, suggesting that the former activity could be the main function of RaiA in vivo. 
Sequence Annotation
 REGION 23 26 Interaction with rRNA (Potential).
 REGION 83 91 Interaction with rRNA (Potential).
 MOD_RES 66 66 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Reference proteome; Stress response; Translation regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 113 AA 
Protein Sequence
MTMNITSKQM EITPAIRQHV ADRLAKLEKW QTHLINPHII LSKEPQGFVA DATINTPNGV 60
LVASGKHEDM YTAINELINK LERQLNKLQH KGEARRAATS VKDANFVEEV EEE 113 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoliWiki.
 GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
 GO:0045900; P:negative regulation of translational elongation; IDA:EcoCyc.
 GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
 GO:0044238; P:primary metabolic process; IEA:InterPro.
 GO:0009409; P:response to cold; IEP:EcoCyc. 
Interpro
 IPR003489; Ribosomal_S30Ae/sigma54_mod. 
Pfam
 PF02482; Ribosomal_S30AE 
SMART
  
PROSITE
  
PRINTS