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HAMAP rule MF_01334

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General rule information [?]

Accession MF_01334
Dates 6-JUN-2005 (Created)
22-SEP-2023 (Last updated, Version 23)
Name Ribosomal_bL25_CTC
Scope(s) Bacteria
Template(s) P14194 (CTC_BACSU); Q9RX88 (RL25_DEIRA); P68919 (RL25_ECOLI); Q5SHZ1 (RL25_THET8); P56930 (RL25_THETH); [ Recover all ]
Triggered by HAMAP; MF_01334 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier RL25
Protein name RecName: Full=Large ribosomal subunit protein bL25;
AltName: Full=General stress protein CTC;
Gene name Name=rplY; Synonyms=ctc;

Comments [?]

FUNCTIONThis is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
SUBUNITPart 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.
SIMILARITYBelongs 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;
NCBIfam TIGR00731; Ctc_TL5; 1;

Features [?]

Additional information [?]

Size range 151-250 amino acids
Related rules MF_01336
Fusion Nter: None Cter: None
Comments This family is specific for proteins that encode both the L25 and CTC domains, which includes most bacteria. However a number of bacteria, including some Gammaproteobacteria, Cyanobacteriota 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). In at least some cases bL25 is dispensible for translation; in B. subtilis bL25 is only expressed in vegetatively growing cells. bL25 is missing from some Bacillus, Cyanobacteriota and Lactobacillus. The equivalent of the highly conserved Asp-87 in Thermus thermophilus (AC P56930) is altered in Enterococcus and Cyanobacteriota. 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).

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