UniProt Accession

 RS5_ECOLI; P0A7W1; O54299; P02356; Q2M6W8 

Genbank Protein ID

 X01563; U18997; U00096; AP009048 

Genbank Nucleotide ID

 CAA25722.1; AAA58100.1; AAC76328.1; BAE77988.1 

Protein Name

 30S ribosomal protein S5 

Protein Synonyms/Alias

  

Gene Name

 rpsE 

Gene Synonyms/Alias

 spc; b3303; JW3265 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
6	**MAHIEKQAGELQE	acetylation	[1, 2]
14	QAGELQEKLIAVNRV	acetylation	[1, 2]
86	GTLQHPVKGVHTGSR	acetylation	[2]
126	GVHNVLAKAYGSTNP	acetylation	[1]
159	MVAAKRGKSVEEILG	acetylation	[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] 

Functional Description

 With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). 

Sequence Annotation

 DOMAIN 11 74 S5 DRBM.
 MOD_RES 2 2 N-acetylalanine.  

Keyword

 3D-structure; Acetylation; Antibiotic resistance; Complete proteome; Direct protein sequencing; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 167 AA 

Protein Sequence

Gene Ontology

 GO:0015935; C:small ribosomal subunit; IEA:InterPro.
 GO:0019843; F:rRNA binding; IEA:HAMAP.
 GO:0003735; F:structural constituent of ribosome; IEA:HAMAP.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0006412; P:translation; IEA:HAMAP. 

Interpro

 IPR014720; dsRNA-bd-like_dom.
 IPR000851; Ribosomal_S5.
 IPR005712; Ribosomal_S5_bac-type.
 IPR005324; Ribosomal_S5_C.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR013810; Ribosomal_S5_N.
 IPR018192; Ribosomal_S5_N_CS. 

Pfam

 PF00333; Ribosomal_S5
 PF03719; Ribosomal_S5_C 

SMART

  

PROSITE

 PS00585; RIBOSOMAL_S5
 PS50881; S5_DSRBD 

PRINTS