HAMAP rule MF_01334
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01334 |
| 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
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Identifier, protein and gene names
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| Identifier | RL25 |
| Protein name | RecName: Full=Large ribosomal subunit protein bL25; AltName: Full=General stress protein CTC; |
| Gene name | Name=rplY; Synonyms=ctc; |
Comments
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| 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
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Gene Ontology
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| GO:0003723; Molecular function:RNA binding |
| GO:0006412; Biological process:translation |
Cross-references
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Features
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Additional information
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| 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). |