CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003035
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 30S ribosomal protein S4 
Protein Synonyms/Alias
  
Gene Name
 rpsD 
Gene Synonyms/Alias
 ramA; b3296; JW3258 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
22EGTDLFLKSGVRAIDacetylation[1]
77RQFRNYYKEAARLKGacetylation[1, 2]
156AKKQSRVKAALELAEacetylation[1]
156AKKQSRVKAALELAEpupylation[3]
167ELAEQREKPTWLEVDacetylation[1]
167ELAEQREKPTWLEVDpupylation[3]
177WLEVDAGKMEGTFKRacetylation[1, 4]
183GKMEGTFKRKPERSDacetylation[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] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222]
 [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
 One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. 
Sequence Annotation
 DOMAIN 96 156 S4 RNA-binding.  
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
 206 AA 
Protein Sequence
MARYLGPKLK LSRREGTDLF LKSGVRAIDT KCKIEQAPGQ HGARKPRLSD YGVQLREKQK 60
VRRIYGVLER QFRNYYKEAA RLKGNTGENL LALLEGRLDN VVYRMGFGAT RAEARQLVSH 120
KAIMVNGRVV NIASYQVSPN DVVSIREKAK KQSRVKAALE LAEQREKPTW LEVDAGKMEG 180
TFKRKPERSD LSADINEHLI VELYSK 206 
Gene Ontology
 GO:0015935; C:small ribosomal subunit; IEA:InterPro.
 GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc.
 GO:0019843; F:rRNA binding; IDA:EcoliWiki.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0000900; F:translation repressor activity, nucleic acid binding; IMP:EcoCyc.
 GO:0006353; P:DNA-dependent transcription, termination; IEA:UniProtKB-KW.
 GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0031564; P:transcription antitermination; IDA:EcoCyc.
 GO:0006412; P:translation; IEA:HAMAP. 
Interpro
 IPR022801; Ribosomal_S4/S9.
 IPR001912; Ribosomal_S4/S9_N.
 IPR005709; Ribosomal_S4_bac-type.
 IPR018079; Ribosomal_S4_CS.
 IPR002942; S4_RNA-bd. 
Pfam
 PF00163; Ribosomal_S4
 PF01479; S4 
SMART
 SM00363; S4 
PROSITE
 PS00632; RIBOSOMAL_S4
 PS50889; S4 
PRINTS