P04257 (RL2_GEOSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 91.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 50S ribosomal protein L2 Short name=BstL2 Alternative name(s): L3 | ||
| Gene names |
| ||
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) | ||
| Taxonomic identifier | 1422 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus |
Protein attributes
| Sequence length | 276 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 | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome By similarity. HAMAP MF_01320_B |
| Subunit structure | Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome By similarity. |
| Sequence similarities | Belongs to the ribosomal protein L2P family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | RNA-binding rRNA-binding |
| Molecular function | Ribonucleoprotein Ribosomal protein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | translation Inferred from electronic annotation. Source: InterPro |
| Cellular component | large ribosomal subunit Inferred from electronic annotation. Source: InterPro |
| Molecular function | rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosomeInferred from electronic annotation. Source: InterPro transferase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.3 | ||||||||||||||||||||||||||||
| Chain | 2 – 276 | 275 | 50S ribosomal protein L2 HAMAP MF_01320_B | PRO_0000129528 | |||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||
| Sequence conflict | 40 | 1 | R → K in BAA31210. Ref.1 | ||||||||||||||||||||||||||||
| Sequence conflict | 106 | 1 | A → R in BAA31210. Ref.1 | ||||||||||||||||||||||||||||
| Sequence conflict | 163 | 1 | Q → L in BAA31210. Ref.1 | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Beta strand | 76 – 84 | 9 | |||||||||||||||||||||||||||||
| Helix | 85 – 87 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 89 – 96 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 101 – 105 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 129 – 131 | 3 | |||||||||||||||||||||||||||||
| Helix | 132 – 134 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 140 – 147 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 152 – 159 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 162 – 168 | 7 | |||||||||||||||||||||||||||||
| Beta strand | 171 – 175 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 181 – 185 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 188 – 193 | 6 | |||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Nucleotide sequence of the genes encoding the ribosomal proteins L23 and L2 from the Bacillus stearothermophilus ribosome." Kimura M. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Nucleotide sequences of Bacillus stearothermophilus ribosomal protein genes: part of the ribosomal S10 operon." Kroemer W.J., Hatakeyama T., Kimura M. Biol. Chem. Hoppe-Seyler 371:631-636(1990) [PubMed: 2222862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-276. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924. |
| [3] | "The primary structure of ribosomal protein L2 from Bacillus stearothermophilus." Kimura M., Kimura J., Watanabe K. Eur. J. Biochem. 153:289-297(1985) [PubMed: 3908098] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-276. |
| [4] | "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies." Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B. EMBO J. 14:4578-4588(1995) [PubMed: 7556101] [Abstract] Cited for: PROTEIN SEQUENCE OF 239-247, CROSS-LINKING TO RRNA. Strain: 799. |
| [5] | "The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome." Nakagawa A., Nakashima T., Taniguchi M., Hosaka H., Kimura M., Tanaka I. EMBO J. 18:1459-1467(1999) [PubMed: 10075918] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 61-202. |
| [6] | "Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit." Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A. Nature 400:841-847(1999) [PubMed: 10476961] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 62-197 ONTO THE H.MARISMORTUI 50S RIBOSOME. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AB015722 Genomic DNA. Translation: BAA31210.1. X54994 Genomic DNA. Translation: CAA38737.1. | ||||||||||||
| PIR | R5BS2F. A02759. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P04257. | ||||||||||||
| SMR | P04257. Positions 2-273. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01320_B. Ribosomal_L2_B. [Tree] | ||||||||||||
| InterPro | IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR022666. Rbsml_prot_L2_RNA-bd_dom. IPR002171. Ribosomal_L2. IPR014726. Ribosomal_L2_3. IPR005880. Ribosomal_L2_bac-type. IPR022669. Ribosomal_L2_C. IPR022671. Ribosomal_L2_CS. IPR014722. Transl_SH3-like_sub. IPR008991. Translation_prot_SH3-like. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:2.30.30.30. Ribosomal_L2. 1 hit. G3DSA:4.10.950.10. Ribosomal_L2. 1 hit. | ||||||||||||
| PANTHER | PTHR13691:SF5. Ribosom_L2_bac. 1 hit. PTHR13691. Ribosomal_L2. 1 hit. | ||||||||||||
| Pfam | PF00181. Ribosomal_L2. 1 hit. PF03947. Ribosomal_L2_C. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF002158. Ribosomal_L2. 1 hit. | ||||||||||||
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. SSF50104. Transl_SH3_like. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR01171. RplB_bact. 1 hit. | ||||||||||||
| PROSITE | PS00467. RIBOSOMAL_L2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RL2_GEOSE | ||||||||
| Accession | Primary (citable) accession number: P04257 Secondary accession number(s): O82995 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Ribosomal proteins Ribosomal proteins families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with