Reviewed,
UniProtKB/Swiss-Prot P41201 (RL5_THETH)
Last modified
June 16, 2009.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 50S ribosomal protein L5 Alternative name(s): TthL5 TL4 | ||||
| Gene names |
| ||||
| Organism | Thermus thermophilus | ||||
| Taxonomic identifier | 274 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 182 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (forming bridge B1b) connecting the head of the 30S subunit to the top of the 50S subunit. The bridge itself contacts the P site tRNA and is implicated in movement during ribosome translocation. Also contacts the P site tRNA independently of the intersubunit bridge; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs By similarity. |
| Subunit structure | Forms a bridge to the 30S subunit in the 70S ribosome, contacting protein S13; this bridge is straddled by the 5S rRNA. Contacts the P site tRNA By similarity. Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 (TL5) subcomplex. |
| Sequence similarities | Belongs to the ribosomal protein L5P family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | RNA-binding rRNA-binding tRNA-binding |
| Molecular function | Ribonucleoprotein Ribosomal protein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | translation Inferred from electronic annotation. Source: HAMAP |
| Cellular component | ribosome Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosomeInferred from electronic annotation. Source: InterPro tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | |||||||||||||||||||||||||||||||||||
| Chain | 2 – 182 | 181 | 50S ribosomal protein L5 HAMAP MF_01333 | PRO_0000125015 | ||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 5 | 1 | V → L AA sequence Ref.2 | |||||||||||||||||||||||||||||||||||
| Sequence conflict | 33 | 1 | R → RE AA sequence Ref.2 | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Helix | 6 – 13 | 8 | ||||||||||||||||||||||||||||||||||||
| Helix | 15 – 22 | 8 | ||||||||||||||||||||||||||||||||||||
| Helix | 28 – 30 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 34 – 42 | 9 | ||||||||||||||||||||||||||||||||||||
| Turn | 44 – 46 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 50 – 64 | 15 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 69 – 72 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 80 – 83 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 86 – 94 | 9 | ||||||||||||||||||||||||||||||||||||
| Helix | 96 – 108 | 13 | ||||||||||||||||||||||||||||||||||||
| Turn | 109 – 113 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 127 – 135 | 9 | ||||||||||||||||||||||||||||||||||||
| Turn | 149 – 151 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 155 – 162 | 8 | ||||||||||||||||||||||||||||||||||||
| Helix | 166 – 176 | 11 | ||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Comparative analysis of ribosomal protein L5 sequences from bacteria of the genus Thermus." Jahn O., Hartmann R.K., Boeckh T., Erdmann V.A. Biochimie 73:669-678(1991) [PubMed: 1764514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33923 / DSM 674 / AT-62. |
| [2] | "5S rRNA binding ribosomal proteins from Thermus thermophilus: identification and some structural properties." Gongadze G.M., Kashparov I., Lorenz S., Schroeder W., Erdmann V.A., Liljas A., Garber M.B. FEBS Lett. 386:260-262(1996) [PubMed: 8647295] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-40. Strain: VK1. |
| [3] | "The Thermus thermophilus 5S rRNA-protein complex: identification of specific binding sites for proteins L5 and L18 in 5S rRNA." Gongadze G.M., Perederina A.A., Meshcheriakov V.A., Fedorov R.V., Moskalenko S.E., Rak A.V., Serganov A.A., Shcherbakov D.V., Nikonov S.V., Garber M.B. Mol. Biol. (Mosk.) 35:610-616(2001) [PubMed: 11524947] [Abstract] Cited for: BINDING TO 5S RRNA. Strain: VK1. |
| [4] | "Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex." Perederina A., Nevskaya N., Nikonov O., Nikulin A., Dumas P., Yao M., Tanaka I., Garber M.B., Gongadze G., Nikonov S. RNA 8:1548-1557(2002) [PubMed: 12515387] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF THE PROTEIN IN COMPLEX WITH A 5S RRNA FRAGMENT. Strain: VK1. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| S77826 Genomic DNA. Translation: AAB21093.1. | |||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01333. [Tree] | ||||||||||||
| InterPro | IPR002132. Ribosomal_L5. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.1440.10. Ribosomal_L5. 1 hit. | ||||||||||||
| PANTHER | PTHR11994. Ribosomal_L5. 1 hit. | ||||||||||||
| Pfam | PF00281. Ribosomal_L5. 1 hit. PF00673. Ribosomal_L5_C. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF002161. Ribosomal_L5. 1 hit. | ||||||||||||
| ProDom | PD013434. Ribosomal_L5_mit. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| PROSITE | PS00358. RIBOSOMAL_L5. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RL5_THETH | ||||||||
| Accession | Primary (citable) accession number: P41201 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| Ribosomal proteins Ribosomal proteins families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


