UniProt Accession

 RL14_ECOLI; P0ADY3; P02411; Q2M6X5 

Genbank Protein ID

 X01563; U18997; U00096; AP009048; V00357 

Genbank Nucleotide ID

 CAA25715.1; AAA58107.1; AAC76335.1; BAE77981.1; CAA23653.1 

Protein Name

 50S ribosomal protein L14 

Protein Synonyms/Alias

  

Gene Name

 rplN 

Gene Synonyms/Alias

 b3310; JW3272 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
23	ARRVMCIKVLGGSHR	acetylation	[1]
40	AGVGDIIKITIKEAI	acetylation	[1]
44	DIIKITIKEAIPRGK	acetylation	[1]
54	IPRGKVKKGDVLKAV	acetylation	[1]
59	VKKGDVLKAVVVRTK	acetylation	[1]
111	TRELRSEKFMKIISL	acetylation	[1]
114	LRSEKFMKIISLAPE	acetylation	[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] 

Functional Description

 This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8. 

Sequence Annotation

  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 123 AA 

Protein Sequence

Gene Ontology

 GO:0022625; C:cytosolic large ribosomal subunit; IDA:EcoCyc.
 GO:0070180; F:LSU rRNA binding; IDA:EcoCyc.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0006412; P:translation; IEA:HAMAP. 

Interpro

 IPR005745; Ribosomal_L14_bac-type.
 IPR019972; Ribosomal_L14_CS.
 IPR023571; Ribosomal_L14_dom.
 IPR000218; Ribosomal_L14b/L23e. 

Pfam

 PF00238; Ribosomal_L14 

SMART

  

PROSITE

 PS00049; RIBOSOMAL_L14 

PRINTS