O06047 (RL2_MYCBO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 71.
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 | ||||
| Gene names |
| ||||
| Organism | Mycobacterium bovis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1765 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 280 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 | Complete proteome |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 280 | 280 | 50S ribosomal protein L2 HAMAP MF_01320_B | PRO_0000129578 | |||||
Experimental info | |||||||||
| Sequence conflict | 20 | 1 | D → Y in CAA73675. Ref.1 | ||||||
| Sequence conflict | 77 | 1 | A → P in CAA73675. Ref.1 | ||||||
| Sequence conflict | 216 | 1 | G → A in CAA73675. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The role of ribosomal RNAs in macrolide resistance." Sander P., Prammananan T., Meier A., Frischkorn K., Boettger E.C. Mol. Microbiol. 26:469-480(1997) [PubMed: 9402018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BCG. |
| [2] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y13228 Genomic DNA. Translation: CAA73675.1. BX248336 Genomic DNA. Translation: CAD93586.1. |
| RefSeq | NP_854382.1. NC_002945.3. |
3D structure databases | |
| ProteinModelPortal | O06047. |
| SMR | O06047. Positions 2-271. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000017672; EBMYCP00000017507; EBMYCG00000017667. |
| GeneID | 1091853. |
| GenomeReviews | Gene locus Mb0724 in contig BX248333_GR. |
| KEGG | mbo:Mb0724. |
| PATRIC | 18003252. VBIMycBov88188_0790. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000016403. |
| HOGENOM | HBG748739. |
| OMA | QSNINWG. |
| ProtClustDB | PRK09374. |
Enzyme and pathway databases | |
| BioCyc | MBOV233413:MB0724-MONOMER. |
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. |
| KO | K02886. |
| 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_MYCBO | ||||||||
| Accession | Primary (citable) accession number: O06047 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Ribosomal proteins Ribosomal proteins families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with