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Q5SLP7

- RL1_THET8

UniProt

Q5SLP7 - RL1_THET8

Protein

50S ribosomal protein L1

Gene

rplA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Directly binds to 23S rRNA. Forms what is known as the L1 stalk, which protrudes beyond the 70S ribosome surface. The stalk is preferentially stabilized in 70S versus 50S crystals. Interacts with the E site tRNA, blocking the exit path. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA.
    Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.By similarity

    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

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-256-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L1
    Gene namesi
    Name:rplA
    Ordered Locus Names:TTHA0246
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    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 – 22922850S ribosomal protein L1PRO_0000125764Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit.

    Protein-protein interaction databases

    STRINGi300852.TTHA0246.

    Structurei

    Secondary structure

    1
    229
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 127
    Turni13 – 153
    Beta strandi17 – 193
    Turni20 – 223
    Helixi23 – 3210
    Beta strandi36 – 383
    Beta strandi41 – 5010
    Beta strandi52 – 543
    Helixi55 – 573
    Beta strandi60 – 645
    Helixi70 – 723
    Beta strandi75 – 784
    Beta strandi79 – 813
    Helixi82 – 898
    Beta strandi93 – 964
    Helixi98 – 1003
    Helixi101 – 1055
    Turni108 – 1103
    Beta strandi112 – 1165
    Helixi118 – 1203
    Helixi121 – 13212
    Turni133 – 1364
    Helixi141 – 1433
    Beta strandi146 – 1483
    Helixi150 – 1578
    Beta strandi161 – 1655
    Beta strandi170 – 1789
    Beta strandi179 – 1813
    Helixi183 – 19917
    Beta strandi204 – 2063
    Beta strandi209 – 2179
    Beta strandi218 – 2203
    Beta strandi222 – 2254

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GIYX-ray5.50C2-229[»]
    1YL3X-ray5.50C2-229[»]
    2HGJX-ray5.00C1-229[»]
    2HGQX-ray5.50C1-229[»]
    2HGUX-ray4.51C1-229[»]
    2J01X-ray2.80C2-229[»]
    2J03X-ray2.80C2-229[»]
    2OM7electron microscopy7.30K1-229[»]
    2V47X-ray3.50C2-229[»]
    2V49X-ray3.50C2-229[»]
    2WDIX-ray3.30C1-229[»]
    2WDJX-ray3.30C1-229[»]
    2WDLX-ray3.50C1-229[»]
    2WDNX-ray3.50C1-229[»]
    2WH2X-ray3.45C1-229[»]
    2WH4X-ray3.45C1-229[»]
    2WRJX-ray3.60C1-229[»]
    2WRLX-ray3.60C1-229[»]
    2WROX-ray3.60C1-229[»]
    2WRRX-ray3.60C1-229[»]
    2X9SX-ray3.10C1-229[»]
    2X9UX-ray3.10C1-229[»]
    2XG0X-ray3.20C1-229[»]
    2XG2X-ray3.20C1-229[»]
    2XQEX-ray3.10C1-229[»]
    2XTGelectron microscopy7.80C1-229[»]
    2XUXelectron microscopy7.60C1-229[»]
    2Y0VX-ray3.10C1-229[»]
    2Y0XX-ray3.10C1-229[»]
    2Y0ZX-ray3.10C1-229[»]
    2Y11X-ray3.10C1-229[»]
    2Y13X-ray3.10C1-229[»]
    2Y15X-ray3.10C1-229[»]
    2Y17X-ray3.10C1-229[»]
    2Y19X-ray3.10C1-229[»]
    3FINelectron microscopy6.40C19-225[»]
    3HUXX-ray3.10C1-229[»]
    3HUZX-ray3.10C1-229[»]
    3KIRX-ray3.30C1-229[»]
    3KITX-ray3.30C1-229[»]
    3KIWX-ray3.60C1-229[»]
    3KIYX-ray3.60C1-229[»]
    3KNIX-ray3.00C1-229[»]
    3KNKX-ray3.00C1-229[»]
    3KNMX-ray3.45C1-229[»]
    3KNOX-ray3.45C1-229[»]
    3TG8X-ray1.95A1-229[»]
    3V6WX-ray3.90C1-229[»]
    3V6XX-ray3.90C1-229[»]
    3ZN9X-ray3.10C1-229[»]
    3ZNEX-ray3.10C1-229[»]
    3ZVPX-ray3.80C1-229[»]
    4ABSX-ray3.10C1-229[»]
    4B8GX-ray3.70C1-229[»]
    4B8IX-ray3.70C1-229[»]
    4BTDX-ray2.95C2-229[»]
    4BYCX-ray3.35C1-229[»]
    4BYEX-ray3.35C1-229[»]
    4EJBX-ray3.52C1-229[»]
    4EJCX-ray3.52C1-229[»]
    4JUXX-ray2.86C1-229[»]
    4K0MX-ray3.30C19-102[»]
    4K0QX-ray3.30C19-102[»]
    ProteinModelPortaliQ5SLP7.
    SMRiQ5SLP7. Positions 2-229.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SLP7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L1P family.Curated

    Phylogenomic databases

    eggNOGiCOG0081.
    HOGENOMiHOG000207015.
    KOiK02863.
    OMAiNEGWTDF.
    OrthoDBiEOG6FBX2G.
    PhylomeDBiQ5SLP7.

    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.

    Q5SLP7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKHGKRYRA LLEKVDPNKV YTIDEAARLV 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):24,831
    Last modified:January 23, 2007 - v3
    Checksum:i99EE7BE00801B1B4
    GO

    Mass spectrometryi

    Molecular mass is 24698 Da from positions 2 - 229. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD70069.1.
    RefSeqiWP_011227804.1. NC_006461.1.
    YP_143512.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD70069; BAD70069; BAD70069.
    GeneIDi3168861.
    KEGGittj:TTHA0246.
    PATRICi23955439. VBITheThe93045_0246.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD70069.1 .
    RefSeqi WP_011227804.1. NC_006461.1.
    YP_143512.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GIY X-ray 5.50 C 2-229 [» ]
    1YL3 X-ray 5.50 C 2-229 [» ]
    2HGJ X-ray 5.00 C 1-229 [» ]
    2HGQ X-ray 5.50 C 1-229 [» ]
    2HGU X-ray 4.51 C 1-229 [» ]
    2J01 X-ray 2.80 C 2-229 [» ]
    2J03 X-ray 2.80 C 2-229 [» ]
    2OM7 electron microscopy 7.30 K 1-229 [» ]
    2V47 X-ray 3.50 C 2-229 [» ]
    2V49 X-ray 3.50 C 2-229 [» ]
    2WDI X-ray 3.30 C 1-229 [» ]
    2WDJ X-ray 3.30 C 1-229 [» ]
    2WDL X-ray 3.50 C 1-229 [» ]
    2WDN X-ray 3.50 C 1-229 [» ]
    2WH2 X-ray 3.45 C 1-229 [» ]
    2WH4 X-ray 3.45 C 1-229 [» ]
    2WRJ X-ray 3.60 C 1-229 [» ]
    2WRL X-ray 3.60 C 1-229 [» ]
    2WRO X-ray 3.60 C 1-229 [» ]
    2WRR X-ray 3.60 C 1-229 [» ]
    2X9S X-ray 3.10 C 1-229 [» ]
    2X9U X-ray 3.10 C 1-229 [» ]
    2XG0 X-ray 3.20 C 1-229 [» ]
    2XG2 X-ray 3.20 C 1-229 [» ]
    2XQE X-ray 3.10 C 1-229 [» ]
    2XTG electron microscopy 7.80 C 1-229 [» ]
    2XUX electron microscopy 7.60 C 1-229 [» ]
    2Y0V X-ray 3.10 C 1-229 [» ]
    2Y0X X-ray 3.10 C 1-229 [» ]
    2Y0Z X-ray 3.10 C 1-229 [» ]
    2Y11 X-ray 3.10 C 1-229 [» ]
    2Y13 X-ray 3.10 C 1-229 [» ]
    2Y15 X-ray 3.10 C 1-229 [» ]
    2Y17 X-ray 3.10 C 1-229 [» ]
    2Y19 X-ray 3.10 C 1-229 [» ]
    3FIN electron microscopy 6.40 C 19-225 [» ]
    3HUX X-ray 3.10 C 1-229 [» ]
    3HUZ X-ray 3.10 C 1-229 [» ]
    3KIR X-ray 3.30 C 1-229 [» ]
    3KIT X-ray 3.30 C 1-229 [» ]
    3KIW X-ray 3.60 C 1-229 [» ]
    3KIY X-ray 3.60 C 1-229 [» ]
    3KNI X-ray 3.00 C 1-229 [» ]
    3KNK X-ray 3.00 C 1-229 [» ]
    3KNM X-ray 3.45 C 1-229 [» ]
    3KNO X-ray 3.45 C 1-229 [» ]
    3TG8 X-ray 1.95 A 1-229 [» ]
    3V6W X-ray 3.90 C 1-229 [» ]
    3V6X X-ray 3.90 C 1-229 [» ]
    3ZN9 X-ray 3.10 C 1-229 [» ]
    3ZNE X-ray 3.10 C 1-229 [» ]
    3ZVP X-ray 3.80 C 1-229 [» ]
    4ABS X-ray 3.10 C 1-229 [» ]
    4B8G X-ray 3.70 C 1-229 [» ]
    4B8I X-ray 3.70 C 1-229 [» ]
    4BTD X-ray 2.95 C 2-229 [» ]
    4BYC X-ray 3.35 C 1-229 [» ]
    4BYE X-ray 3.35 C 1-229 [» ]
    4EJB X-ray 3.52 C 1-229 [» ]
    4EJC X-ray 3.52 C 1-229 [» ]
    4JUX X-ray 2.86 C 1-229 [» ]
    4K0M X-ray 3.30 C 19-102 [» ]
    4K0Q X-ray 3.30 C 19-102 [» ]
    ProteinModelPortali Q5SLP7.
    SMRi Q5SLP7. Positions 2-229.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA0246.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD70069 ; BAD70069 ; BAD70069 .
    GeneIDi 3168861.
    KEGGi ttj:TTHA0246.
    PATRICi 23955439. VBITheThe93045_0246.

    Phylogenomic databases

    eggNOGi COG0081.
    HOGENOMi HOG000207015.
    KOi K02863.
    OMAi NEGWTDF.
    OrthoDBi EOG6FBX2G.
    PhylomeDBi Q5SLP7.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-256-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5SLP7.

    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. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    2. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
      Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
      Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26.
    3. "Identification of the gene encoding transcription factor NusG of Thermus thermophilus."
      Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K.
      J. Bacteriol. 174:7859-7863(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-181.
      Strain: HB8 / ATCC 27634 / DSM 579.
    4. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
      Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
      Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
    5. "The path of messenger RNA through the ribosome."
      Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
      Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

    Entry informationi

    Entry nameiRL1_THET8
    AccessioniPrimary (citable) accession number: Q5SLP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 90 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, Complete proteome, Direct protein sequencing, Reference proteome

    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