Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27150

- RL1_THETH

UniProt

P27150 - RL1_THETH

Protein

50S ribosomal protein L1

Gene

rplA

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release By similarity. Binds directly to 23S rRNA.By similarity
    Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.UniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. regulation of translation Source: UniProtKB-KW
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Translation regulation

    Keywords - Ligandi

    RNA-binding, rRNA-binding, tRNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L1UniRule annotation
    Gene namesi
    Name:rplAUniRule annotation
    Synonyms:rpl1UniRule annotation
    OrganismiThermus thermophilus
    Taxonomic identifieri274 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Subcellular locationi

    GO - Cellular componenti

    1. large ribosomal subunit Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 22922850S ribosomal protein L1PRO_0000125765Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi262724.TTC1739.

    Structurei

    Secondary structure

    1
    229
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 133
    Helixi23 – 3311
    Beta strandi36 – 383
    Beta strandi41 – 5010
    Helixi55 – 573
    Beta strandi60 – 645
    Beta strandi66 – 683
    Beta strandi75 – 784
    Helixi82 – 898
    Beta strandi93 – 964
    Helixi100 – 1056
    Beta strandi112 – 1165
    Helixi118 – 1203
    Helixi121 – 13515
    Helixi141 – 1433
    Beta strandi146 – 1483
    Helixi150 – 1589
    Beta strandi161 – 1655
    Beta strandi170 – 1789
    Helixi183 – 19917
    Beta strandi209 – 2168
    Beta strandi218 – 2203
    Beta strandi223 – 2253

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AD2X-ray1.90A2-229[»]
    1ZHOX-ray2.60A/C/E/G2-229[»]
    2HW8X-ray2.10A2-229[»]
    2OUMX-ray2.55A2-229[»]
    2OV7X-ray2.30A/B/C2-229[»]
    2VPLX-ray2.30A/C2-229[»]
    3U42X-ray1.35A1-229[»]
    3U4MX-ray2.00A1-229[»]
    3U56X-ray2.10A1-229[»]
    3UMYX-ray1.90A2-229[»]
    4F9TX-ray1.46A1-229[»]
    ProteinModelPortaliP27150.
    SMRiP27150. Positions 2-229.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27150.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L1P family.UniRule annotation

    Family and domain databases

    Gene3Di3.30.190.20. 2 hits.
    3.40.50.790. 1 hit.
    HAMAPiMF_01318_B. Ribosomal_L1_B.
    InterProiIPR005878. Ribosom_L1_bac-type.
    IPR002143. Ribosomal_L1.
    IPR023674. Ribosomal_L1-like.
    IPR028364. Ribosomal_L1/biogenesis.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    IPR016095. Ribosomal_L1_3-a/b-sand.
    IPR023673. Ribosomal_L1_CS.
    [Graphical view]
    PfamiPF00687. Ribosomal_L1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
    SUPFAMiSSF56808. SSF56808. 1 hit.
    TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
    PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P27150-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKHGKRYRA LLEKVDPNKI YTIDEAAHLV KELATAKFDE TVEVHAKLGI    50
    DPRRSDQNVR GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI 100
    IQKILDGWMD FDAVVATPDV MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI 150
    GEIIREIKAG RIEFRNDKTG AIHAPVGKAS FPPEKLADNI RAFIRALEAH 200
    KPEGAKGTFL RSVYVTTTMG PSVRINPHS 229
    Length:229
    Mass (Da):24,826
    Last modified:January 23, 2007 - v3
    Checksum:i38C14B2563718175
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21P → V AA sequence (PubMed:1637860)Curated
    Sequence conflicti4 – 52HG → TN AA sequence (PubMed:1637860)Curated
    Sequence conflicti14 – 141K → F AA sequence (PubMed:1637860)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81375 Genomic DNA. Translation: CAA57139.1.
    PIRiS66577.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81375 Genomic DNA. Translation: CAA57139.1 .
    PIRi S66577.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AD2 X-ray 1.90 A 2-229 [» ]
    1ZHO X-ray 2.60 A/C/E/G 2-229 [» ]
    2HW8 X-ray 2.10 A 2-229 [» ]
    2OUM X-ray 2.55 A 2-229 [» ]
    2OV7 X-ray 2.30 A/B/C 2-229 [» ]
    2VPL X-ray 2.30 A/C 2-229 [» ]
    3U42 X-ray 1.35 A 1-229 [» ]
    3U4M X-ray 2.00 A 1-229 [» ]
    3U56 X-ray 2.10 A 1-229 [» ]
    3UMY X-ray 1.90 A 2-229 [» ]
    4F9T X-ray 1.46 A 1-229 [» ]
    ProteinModelPortali P27150.
    SMRi P27150. Positions 2-229.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262724.TTC1739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P27150.

    Family and domain databases

    Gene3Di 3.30.190.20. 2 hits.
    3.40.50.790. 1 hit.
    HAMAPi MF_01318_B. Ribosomal_L1_B.
    InterProi IPR005878. Ribosom_L1_bac-type.
    IPR002143. Ribosomal_L1.
    IPR023674. Ribosomal_L1-like.
    IPR028364. Ribosomal_L1/biogenesis.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    IPR016095. Ribosomal_L1_3-a/b-sand.
    IPR023673. Ribosomal_L1_CS.
    [Graphical view ]
    Pfami PF00687. Ribosomal_L1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002155. Ribosomal_L1. 1 hit.
    SUPFAMi SSF56808. SSF56808. 1 hit.
    TIGRFAMsi TIGR01169. rplA_bact. 1 hit.
    PROSITEi PS01199. RIBOSOMAL_L1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and overexpression of the ribosomal protein L1 gene from Thermus thermophilus VK1. Crystallization of the recombinant protein L1."
      Ossina N., Eliseikina I.A., Garber M.B., Jonsson B.-H.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: VK1.
    2. "The complete primary structure of ribosomal protein L1 from Thermus thermophilus."
      Amons R., Muranova T.A., Rykunova A.I., Eliseikina I.A., Sedelnikova S.E.
      J. Protein Chem. 12:725-734(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-229.
    3. Cited for: PROTEIN SEQUENCE OF 2-16.
      Strain: VK1.
    4. "Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA."
      Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W.
      Eur. J. Biochem. 256:97-105(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING TO METHANOCOCCUS VANNIELII 23S RRNA AND TO M.VANNIELII L1 MRNA.
      Strain: VK1.
    5. "Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus."
      Nikonov S.V., Nevskaya N., Eliseikina I.A., Fomenkova N.P., Nikulin A., Ossina N., Garber M.B., Jonsson B.-H., Briand C., Al-Karadaghi S., Svensson L.A., Aevarsson A., Liljas A.
      EMBO J. 15:1350-1359(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
      Strain: VK1.
    6. "A mutant form of the ribosomal protein L1 reveals conformational flexibility."
      Unge J., Al-Karadaghi S., Liljas A., Jonsson B.H., Eliseikina I., Ossina N., Nevskaya N., Fomenkova N., Garber M., Nikonov S.
      FEBS Lett. 411:53-59(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT CYS-180.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH A M.VANNIELII L1 MRNA FRAGMENT.
      Strain: VK1.
    8. "Solution structure of the E. coli 70S ribosome at 11.5 A resolution."
      Gabashvili I.S., Agrawal R.K., Spahn C.M., Grassucci R.A., Svergun D.I., Frank J., Penczek P.
      Cell 100:537-549(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.5 ANGSTROMS).

    Entry informationi

    Entry nameiRL1_THETH
    AccessioniPrimary (citable) accession number: P27150
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 98 of the entry and version 3 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