CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009236
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 50S ribosomal protein L4 
Protein Synonyms/Alias
  
Gene Name
 rplD 
Gene Synonyms/Alias
 eryA; b3319; JW3281 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
74RARSGSIKSPIWRSGacetylation[1]
106KMYRGALKSILSELVacetylation[1, 2]
123DRLIVVEKFSVEAPKacetylation[1, 3]
132SVEAPKTKLLAQKLKacetylation[1]
137KTKLLAQKLKDMALEacetylation[1, 3]
166LAARNLHKVDVRDATacetylation[1]
185VSLIAFDKVVMTADAacetylation[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] 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] 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
 One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. 
Sequence Annotation
  
Keyword
 3D-structure; Antibiotic resistance; Complete proteome; Direct protein sequencing; Reference proteome; Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Transcription; Transcription regulation; Transcription termination; Translation regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 201 AA 
Protein Sequence
MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA EVTGSGKKPW 60
RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM YRGALKSILS ELVRQDRLIV 120
VEKFSVEAPK TKLLAQKLKD MALEDVLIIT GELDENLFLA ARNLHKVDVR DATGIDPVSL 180
IAFDKVVMTA DAVKQVEEML A 201 
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:0030371; F:translation repressor activity; IDA:EcoliWiki.
 GO:0006353; P:DNA-dependent transcription, termination; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0006412; P:translation; IEA:HAMAP. 
Interpro
 IPR002136; Ribosomal_L4/L1e.
 IPR013005; Ribosomal_L4/L1e_bac-type.
 IPR023574; Ribosomal_L4_dom. 
Pfam
 PF00573; Ribosomal_L4 
SMART
  
PROSITE
  
PRINTS