CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009496
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 50S ribosomal protein L5 
Protein Synonyms/Alias
  
Gene Name
 rplE 
Gene Synonyms/Alias
 b3308; JW3270 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
3*****MAKLHDYYKDacetylation[1, 2, 3]
9AKLHDYYKDEVVKKLacetylation[3, 4]
14YYKDEVVKKLMTEFNacetylation[3]
15YKDEVVKKLMTEFNYacetylation[3]
47VGEAIADKKLLDNAAacetylation[3]
48GEAIADKKLLDNAAAacetylation[2, 3]
64LAAISGQKPLITKARacetylation[3]
69GQKPLITKARKSVAGacetylation[3]
72PLITKARKSVAGFKIacetylation[3]
78RKSVAGFKIRQGYPIacetylation[2, 3]
88QGYPIGCKVTLRGERacetylation[3]
120DFRGLSAKSFDGRGNacetylation[2, 3, 4]
145FPEIDYDKVDRVRGLacetylation[3]
161ITITTTAKSDEEGRAacetylation[3]
Reference
 [1] 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]
 [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] 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]
 [4] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508
Functional Description
 This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18. 
Sequence Annotation
 MOD_RES 3 3 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 179 AA 
Protein Sequence
MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL DNAAADLAAI 60
SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF ERLITIAVPR IRDFRGLSAK 120
SFDGRGNYSM GVREQIIFPE IDYDKVDRVR GLDITITTTA KSDEEGRALL AAFDFPFRK 179 
Gene Ontology
 GO:0005840; C:ribosome; IEA:UniProtKB-KW.
 GO:0019843; F:rRNA binding; IEA:HAMAP.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0000049; F:tRNA binding; IEA:HAMAP.
 GO:0006412; P:translation; IEA:HAMAP. 
Interpro
 IPR002132; Ribosomal_L5.
 IPR020930; Ribosomal_L5_bac-type.
 IPR020929; Ribosomal_L5_CS.
 IPR022803; Ribosomal_L5_domain. 
Pfam
 PF00281; Ribosomal_L5
 PF00673; Ribosomal_L5_C 
SMART
  
PROSITE
 PS00358; RIBOSOMAL_L5 
PRINTS