CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001953
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 30S ribosomal protein S7 
Protein Synonyms/Alias
  
Gene Name
 rpsG 
Gene Synonyms/Alias
 b3341; JW3303 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
17RKILPDPKFGSELLAacetylation[1]
56TLAQRSGKSELEAFEacetylation[1]
56TLAQRSGKSELEAFEpupylation[2]
76VRPTVEVKSRRVGGSacetylation[1]
114AARKRGDKSMALRLAacetylation[1]
131LSDAAENKGTAVKKRacetylation[1]
131LSDAAENKGTAVKKRpupylation[2]
149HRMAEANKAFAHYRWacetylation[1, 3]
171HQAGASSKQPALGYLacetylation[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] 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]
 [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
 One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, where it has been shown to contact mRNA. Has been shown to contact tRNA in both the P and E sites; it probably blocks exit of the E site tRNA. 
Sequence Annotation
  
Keyword
 3D-structure; 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
MPRRRVIGQR KILPDPKFGS ELLAKFVNIL MVDGKKSTAE SIVYSALETL AQRSGKSELE 60
AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALA MRWIVEAARK RGDKSMALRL 120
ANELSDAAEN KGTAVKKRED VHRMAEANKA FAHYRWLSLR SFSHQAGASS KQPALGYLN 179 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0003729; F:mRNA binding; IDA:EcoCyc.
 GO:0019843; F:rRNA binding; IDA:EcoCyc.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0000049; F:tRNA binding; IEA:HAMAP.
 GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
 GO:0000028; P:ribosomal small subunit assembly; IDA:EcoCyc.
 GO:0006412; P:translation; IEA:HAMAP. 
Interpro
 IPR000235; Ribosomal_S5/S7.
 IPR005717; Ribosomal_S7_bac/org-type.
 IPR020606; Ribosomal_S7_CS.
 IPR023798; Ribosomal_S7_dom. 
Pfam
 PF00177; Ribosomal_S7 
SMART
  
PROSITE
 PS00052; RIBOSOMAL_S7 
PRINTS