CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009207
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 50S ribosomal protein L2 
Protein Synonyms/Alias
  
Gene Name
 rplB 
Gene Synonyms/Alias
 b3317; JW3279 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
5***MAVVKCKPTSPGacetylation[1]
18PGRRHVVKVVNPELHacetylation[2]
26VVNPELHKGKPFAPLacetylation[2]
28NPELHKGKPFAPLLEacetylation[2]
36PFAPLLEKNSKSGGRacetylation[2]
59RHIGGGHKQAYRIVDacetylation[1]
97NIALVLYKDGERRYIacetylation[2]
108RRYILAPKGLKAGDQacetylation[1, 2]
111ILAPKGLKAGDQIQSacetylation[1, 2]
125SGVDAAIKPGNTLPMacetylation[2]
147TVHNVEMKPGKGGQLacetylation[2]
183LRSGEMRKVEADCRAacetylation[1]
242GEGRNFGKHPVTPWGacetylation[2, 3]
265RSNKRTDKFIVRRRSacetylation[2]
Reference
 [1] 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]
 [2] 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]
 [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
Functional Description
 One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial. 
Sequence Annotation
 MOD_RES 242 242 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 273 AA 
Protein Sequence
MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLLEKNSKS GGRNNNGRIT TRHIGGGHKQ 60
AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE RRYILAPKGL KAGDQIQSGV 120
DAAIKPGNTL PMRNIPVGST VHNVEMKPGK GGQLARSAGT YVQIVARDGA YVTLRLRSGE 180
MRKVEADCRA TLGEVGNAEH MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF 240
GKHPVTPWGV QTKGKKTRSN KRTDKFIVRR RSK 273 
Gene Ontology
 GO:0015934; C:large ribosomal subunit; IEA:InterPro.
 GO:0019843; F:rRNA binding; IEA:HAMAP.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0016740; F:transferase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0006412; P:translation; IEA:HAMAP. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR022666; Rbsml_prot_L2_RNA-bd_dom.
 IPR014722; Rib_L2_dom2.
 IPR002171; Ribosomal_L2.
 IPR005880; Ribosomal_L2_bac/org-type.
 IPR022669; Ribosomal_L2_C.
 IPR022671; Ribosomal_L2_CS.
 IPR014726; Ribosomal_L2_dom3.
 IPR008991; Translation_prot_SH3-like. 
Pfam
 PF00181; Ribosomal_L2
 PF03947; Ribosomal_L2_C 
SMART
  
PROSITE
 PS00467; RIBOSOMAL_L2 
PRINTS