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P04257

- RL2_GEOSE

UniProt

P04257 - RL2_GEOSE

Protein

50S ribosomal protein L2

Gene

rplB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.UniRule annotation

    GO - Molecular functioni

    1. rRNA binding Source: UniProtKB-HAMAP
    2. structural constituent of ribosome Source: InterPro
    3. transferase activity Source: InterPro

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L2UniRule annotation
    Short name:
    BstL2
    Alternative name(s):
    L3
    Gene namesi
    Name:rplBUniRule annotation
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. large ribosomal subunit Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 27627550S ribosomal protein L2PRO_0000129528Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.UniRule annotation

    Structurei

    Secondary structure

    1
    276
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi76 – 849
    Helixi85 – 873
    Beta strandi89 – 968
    Beta strandi101 – 1055
    Beta strandi129 – 1313
    Helixi132 – 1343
    Beta strandi140 – 1478
    Beta strandi152 – 1598
    Beta strandi162 – 1687
    Beta strandi171 – 1755
    Beta strandi181 – 1855
    Beta strandi188 – 1936

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ML5electron microscopy14.00d61-233[»]
    1RL2X-ray2.30A/B61-197[»]
    2B66X-ray5.90D61-197[»]
    2B9NX-ray6.76D61-197[»]
    2B9PX-ray6.46D61-197[»]
    ProteinModelPortaliP04257.
    SMRiP04257. Positions 2-273.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04257.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L2P family.UniRule annotation

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    4.10.950.10. 1 hit.
    HAMAPiMF_01320_B. Ribosomal_L2_B.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR022666. Rbsml_prot_L2_RNA-bd_dom.
    IPR014722. Rib_L2_dom2.
    IPR002171. Ribosomal_L2.
    IPR005880. Ribosomal_L2_bac/org-type.
    IPR022669. Ribosomal_L2_C.
    IPR022671. Ribosomal_L2_CS.
    IPR014726. Ribosomal_L2_dom3.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PANTHERiPTHR13691. PTHR13691. 1 hit.
    PTHR13691:SF5. PTHR13691:SF5. 1 hit.
    PfamiPF00181. Ribosomal_L2. 1 hit.
    PF03947. Ribosomal_L2_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
    SUPFAMiSSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
    PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P04257-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIKKYKPTS NGRRGMTVLD FSEITTDQPE KSLLAPLKKR AGRNNQGKIT    50
    VRHQGGGHKR QYRIIDFKRD KDGIPGRVAT IEYDPNRSAN IALINYADGE 100
    KRYIIAPKNL KVGMEIMSGP DADIKIGNAL PLENIPVGTL VHNIELKPGR 150
    GGQLVRAAGT SAQVLGKEGK YVIVRLASGE VRMILGKCRA TVGEVGNEQH 200
    ELVNIGKAGR ARWLGIRPTV RGSVMNPVDH PHGGGEGKAP IGRKSPMTPW 250
    GKPTLGYKTR KKKNKSDKFI IRRRKK 276
    Length:276
    Mass (Da):30,331
    Last modified:January 23, 2007 - v2
    Checksum:i871DBC74317C3AAD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401R → K in BAA31210. 1 PublicationCurated
    Sequence conflicti106 – 1061A → R in BAA31210. 1 PublicationCurated
    Sequence conflicti163 – 1631Q → L in BAA31210. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015722 Genomic DNA. Translation: BAA31210.1.
    X54994 Genomic DNA. Translation: CAA38737.1.
    PIRiA02759. R5BS2F.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015722 Genomic DNA. Translation: BAA31210.1 .
    X54994 Genomic DNA. Translation: CAA38737.1 .
    PIRi A02759. R5BS2F.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ML5 electron microscopy 14.00 d 61-233 [» ]
    1RL2 X-ray 2.30 A/B 61-197 [» ]
    2B66 X-ray 5.90 D 61-197 [» ]
    2B9N X-ray 6.76 D 61-197 [» ]
    2B9P X-ray 6.46 D 61-197 [» ]
    ProteinModelPortali P04257.
    SMRi P04257. Positions 2-273.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P04257.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    4.10.950.10. 1 hit.
    HAMAPi MF_01320_B. Ribosomal_L2_B.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR022666. Rbsml_prot_L2_RNA-bd_dom.
    IPR014722. Rib_L2_dom2.
    IPR002171. Ribosomal_L2.
    IPR005880. Ribosomal_L2_bac/org-type.
    IPR022669. Ribosomal_L2_C.
    IPR022671. Ribosomal_L2_CS.
    IPR014726. Ribosomal_L2_dom3.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    PANTHERi PTHR13691. PTHR13691. 1 hit.
    PTHR13691:SF5. PTHR13691:SF5. 1 hit.
    Pfami PF00181. Ribosomal_L2. 1 hit.
    PF03947. Ribosomal_L2_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002158. Ribosomal_L2. 1 hit.
    SUPFAMi SSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR01171. rplB_bact. 1 hit.
    PROSITEi PS00467. RIBOSOMAL_L2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 62-197 ONTO THE H.MARISMORTUI 50S RIBOSOME.

    Entry informationi

    Entry nameiRL2_GEOSE
    AccessioniPrimary (citable) accession number: P04257
    Secondary accession number(s): O82995
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3