ExPASy Proteomics Server

Accession	MF_01336
Dates	16-JUN-2005 (Created) 25-NOV-2009 (Last updated, Version 8)

Data class

Protein

Predictors

HAMAP; MF_01336; [distribution of match scores in UniProtKB];[seed alignment for MF_01336]

Names

Ribosomal_L25

Identifier

RL25

Protein name

RecName: Full=50S ribosomal protein L25;

Gene name

rplY

FUNCTION: This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance (By similarity).

SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA independently of L5 and L18 (By similarity).

SIMILARITY: Belongs to the ribosomal protein L25P family.

Pfam	PF01386; Ribosomal_L25p; 1;
PRINTS	PR00453; VWFADOMAIN; 1;

Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding.

GO:0003723; Molecular function: RNA binding.
GO:0006412; Biological process: translation.

Size range:	92-103 amino acids
Related UniRules:	MF_01334 (RL25 (supersedes the current rule))
Template:	P68919 (RL25_ECOLI); Q5SHZ1 (RL25_THET8); P56930 (RL25_THETH): [Recover all]
Scope:	Bacteria
Fusion:	Nter: None; Cter: None
Duplicate:	None
Plasmid encoded:	None
Comments:	This family is specific for proteins with only the L25 domain. This protein varies in length; most bacteria encode both the L25 and CTC domains (see MF_01334). However a number of bacteria, including some Gammaproteobacteria, Cyanobacteria and at least one Betaproteobacteria have only the L25 domain (see MF_01336), while A. aeolicus only has the CTC domain (and cannot bind 5S rRNA). The function of the CTC domain is unknown. In at least some cases RL25 is dispensible for translation; in B. subtilis this protein is only expressed in vegetatively growing cells. L25 is missing from some Bacillus, Cyanobacteria and Lactobacillus. The equivalent of the highly conserved Asp-87 in Thermus thermophilus (AC P56930) is altered in the Enterococcus and Cyanobacterial genera. There are compensatory changes in the 5S rRNA that are thought to alter its secondary structure and thus permit binding of the protein to rRNA, see: PubMed=15718233; DOI=10.1074/jbc.M413596200; Gongadze G.M., Korepanov A.P., Stolboushkina E.A., Zelinskaya N.V., Korobeinikova A.V., Ruzanov M.V., Eliseev B.D., Nikonov O.S., Nikonov S.V., Garber M.B., Lim V.I.; "The crucial role of conserved intermolecular H-bonds inaccessible to the solvent in formation and stabilization of the TL5.5 SrRNA complex."; J. Biol. Chem. 280:16151-16156(2005).