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Annotation rule MF_01334
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General rule information [?]

Accession MF_01334
Dates 6-JUN-2005 (Created)
19-NOV-2019 (Last updated, Version 18)
Name Ribosomal_L25_CTC
Templates P14194 (CTC_BACSU); Q9RX88 (RL25_DEIRA); P68919 (RL25_ECOLI); Q5SHZ1 (RL25_THET8); P56930 (RL25_THETH): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=50S ribosomal protein L25;
AltName: Full=General stress protein CTC;
Gene name
rplY, ctc

Comments [?]

Function This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
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.
Similarity Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.

Keywords [?]

Gene Ontology [?]

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

Cross-references [?]

Pfam PF01386; Ribosomal_L25p; 1;
TIGRFAMs TIGR00731; Ctc_TL5; 1;

Additional information [?]

Size range 151-250 amino acids
Related rules MF_01336 (RL25)
Fusion None
Comments This family is specific for proteins that encode both the L25 and CTC domains. This protein varies in length; most bacteria encode both the L25 and CTC domains. 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).