CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013891
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 50S ribosomal protein L1 
Protein Synonyms/Alias
  
Gene Name
 rplA 
Gene Synonyms/Alias
 TTHA0246 
Created Date
 July 27, 2013 
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 
NCBI Taxa ID
 300852 
Lysine Modification
Position
Peptide
Type
References
14RYRALLEKVDPNKVYacetylation[1]
Reference
 [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus.
 Okanishi H, Kim K, Masui R, Kuramitsu S.
 J Proteome Res. 2013 Aug 1;. [PMID: 23901841
Functional Description
 Directly binds to 23S rRNA. Forms what is known as the L1 stalk, which protrudes beyond the 70S ribosome surface. The stalk is preferentially stabilized in 70S versus 50S crystals. Interacts with the E site tRNA, blocking the exit path. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA. 
Sequence Annotation
  
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
 229 AA 
Protein Sequence
MPKHGKRYRA LLEKVDPNKV YTIDEAARLV KELATAKFDE TVEVHAKLGI DPRRSDQNVR 60
GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI IQKILDGWMD FDAVVATPDV 120
MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI GEIIREIKAG RIEFRNDKTG AIHAPVGKAS 180
FPPEKLADNI RAFIRALEAH KPEGAKGTFL RSVYVTTTMG PSVRINPHS 229 
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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
 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