UniProt Accession

 RL1_ECOLI; P0A7L0; P02384; Q2M8S0 

Genbank Protein ID

 V00339; U00006; U00096; AP009048 

Genbank Nucleotide ID

 CAA23622.1; AAC43082.1; AAC76958.1; BAE77336.1 

Protein Name

 50S ribosomal protein L1 

Protein Synonyms/Alias

  

Gene Name

 rplA 

Gene Synonyms/Alias

 b3984; JW3947 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
14	RMRVIREKVDATKQY	acetylation	[1]
19	REKVDATKQYDINEA	acetylation	[1]
31	NEAIALLKELATAKF	acetylation	[1]
88	GANAEAAKAAGAELV	acetylation	[1]
105	EDLADQIKKGEMNFD	acetylation	[1, 2]
141	RGLMPNPKVGTVTPN	acetylation	[1, 2]
154	PNVAEAVKNAKAGQV	acetylation	[1]
167	QVRYRNDKNGIIHTT	acetylation	[1, 2]
177	IIHTTIGKVDFDADK	acetylation	[1]
184	KVDFDADKLKENLEA	acetylation	[1]
186	DFDADKLKENLEALL	acetylation	[1]
197	EALLVALKKAKPTQA	acetylation	[1, 3]
198	ALLVALKKAKPTQAK	acetylation	[1]
200	LVALKKAKPTQAKGV	acetylation	[1]
205	KAKPTQAKGVYIKKV	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]
 [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, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms (PubMed:12859903). This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation (PubMed:12859903). Contacts the P and E site tRNAs. 

Sequence Annotation

 MOD_RES 105 105 N6-succinyllysine.
 MOD_RES 154 154 N6-succinyllysine.
 MOD_RES 186 186 N6-succinyllysine.
 MOD_RES 197 197 N6-succinyllysine.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 234 AA 

Protein Sequence

Gene Ontology

 GO:0015934; C:large ribosomal subunit; IEA:InterPro.
 GO:0019843; F:rRNA binding; IEA:HAMAP.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
 GO:0006412; P:translation; IEA:HAMAP. 

Interpro

 IPR005878; Ribosom_L1_bac-type.
 IPR002143; Ribosomal_L1.
 IPR016094; Ribosomal_L1_2-a/b-sand.
 IPR016095; Ribosomal_L1_3-a/b-sand.
 IPR023673; Ribosomal_L1_CS.
 IPR023674; Ribosomal_L1_SF. 

Pfam

 PF00687; Ribosomal_L1 

SMART

  

PROSITE

 PS01199; RIBOSOMAL_L1 

PRINTS