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P0A7J3

- RL10_ECOLI

UniProt

P0A7J3 - RL10_ECOLI

Protein

50S ribosomal protein L10

Gene

rplJ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
    Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA.

    GO - Molecular functioni

    1. large ribosomal subunit rRNA binding Source: UniProtKB-HAMAP
    2. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. regulation of translation Source: UniProtKB-KW
    2. ribosome biogenesis Source: InterPro
    3. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Translation regulation

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10871-MONOMER.
    ECOL316407:JW3948-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L10
    Alternative name(s):
    50S ribosomal protein L8
    Gene namesi
    Name:rplJ
    Ordered Locus Names:b3985, JW3948
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10871. rplJ.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi156 – 16510Missing: Generation time doubles, only 1 L12 dimer binds to the ribosome. Decreased association of IF-2 with L7/L12 and decreased stimulation of GTPase activity of EF-G by L7/L12. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 16516450S ribosomal protein L10PRO_0000154627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371N6-acetyllysine1 Publication
    Modified residuei105 – 1051N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A7J3.
    PRIDEiP0A7J3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7J3.

    Interactioni

    Subunit structurei

    Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)(L12)2 complex. Two L12 dimers associate with a copy of L10 to form a very strong complex (called L8).1 Publication

    Protein-protein interaction databases

    BioGridi852784. 1 interaction.
    DIPiDIP-35816N.
    IntActiP0A7J3. 52 interactions.
    MINTiMINT-1264502.
    STRINGi511145.b3985.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74
    Helixi9 – 1810
    Beta strandi24 – 263
    Helixi34 – 4613
    Beta strandi49 – 524
    Helixi60 – 634
    Turni64 – 696
    Turni75 – 773
    Beta strandi79 – 813
    Beta strandi86 – 905
    Helixi95 – 1039
    Beta strandi105 – 1084
    Turni117 – 1204
    Beta strandi128 – 1303
    Helixi134 – 1385
    Helixi140 – 1478
    Turni148 – 1569
    Helixi158 – 1603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J0Telectron microscopy12.10J2-165[»]
    3J0Welectron microscopy14.70J2-165[»]
    3J0Yelectron microscopy13.50J2-165[»]
    3J11electron microscopy13.10J2-165[»]
    3J12electron microscopy11.50J2-165[»]
    3J14electron microscopy11.50J2-165[»]
    3J37electron microscopy9.80J2-165[»]
    3J5Oelectron microscopy6.8051-165[»]
    3J5Uelectron microscopy7.60J1-165[»]
    3J5Welectron microscopy7.60J1-165[»]
    3SGFX-ray3.20H1-165[»]
    3UOSX-ray3.70H1-165[»]
    4KIXX-ray2.9051-165[»]
    4KIZX-ray2.9051-165[»]
    4KJ1X-ray2.9051-165[»]
    4KJ5X-ray2.9051-165[»]
    4KJ9X-ray2.9051-165[»]
    ProteinModelPortaliP0A7J3.
    SMRiP0A7J3. Positions 1-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L10P family.Curated

    Phylogenomic databases

    eggNOGiCOG0244.
    HOGENOMiHOG000004851.
    KOiK02864.
    OMAiFSMEDPG.
    OrthoDBiEOG6DNTDR.
    PhylomeDBiP0A7J3.

    Family and domain databases

    HAMAPiMF_00362. Ribosomal_L10.
    InterProiIPR022973. Ribosomal_L10.
    IPR001790. Ribosomal_L10/acidic_P0.
    IPR002363. Ribosomal_L10_eubac_CS.
    [Graphical view]
    PfamiPF00466. Ribosomal_L10. 1 hit.
    [Graphical view]
    PROSITEiPS01109. RIBOSOMAL_L10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7J3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALNLQDKQA IVAEVSEVAK GALSAVVADS RGVTVDKMTE LRKAGREAGV    50
    YMRVVRNTLL RRAVEGTPFE CLKDAFVGPT LIAYSMEHPG AAARLFKEFA 100
    KANAKFEVKA AAFEGELIPA SQIDRLATLP TYEEAIARLM ATMKEASAGK 150
    LVRTLAAVRD AKEAA 165
    Length:165
    Mass (Da):17,712
    Last modified:January 23, 2007 - v2
    Checksum:iF15822B0EDB6AC02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841Y → YR AA sequence (PubMed:773698)Curated
    Sequence conflicti84 – 841Y → YR AA sequence (PubMed:782920)Curated
    Sequence conflicti84 – 841Y → YR AA sequence (PubMed:797648)Curated
    Sequence conflicti116 – 1161E → Q AA sequence (PubMed:773698)Curated

    Mass spectrometryi

    Molecular mass is 17581.1 Da from positions 2 - 165. Determined by MALDI. 1 Publication
    Molecular mass is 66643±13 Da from positions 2 - 165. Determined by ESI. Isolated L10(L12)4.1 Publication
    Molecular mass is 17580±2 Da from positions 2 - 165. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23623.1.
    U00006 Genomic DNA. Translation: AAC43083.1.
    U00096 Genomic DNA. Translation: AAC76959.1.
    AP009048 Genomic DNA. Translation: BAE77335.1.
    PIRiS12574. R5EC10.
    RefSeqiNP_418412.1. NC_000913.3.
    YP_491476.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76959; AAC76959; b3985.
    BAE77335; BAE77335; BAE77335.
    GeneIDi12930514.
    948490.
    KEGGiecj:Y75_p3212.
    eco:b3985.
    PATRICi32123491. VBIEscCol129921_4098.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23623.1 .
    U00006 Genomic DNA. Translation: AAC43083.1 .
    U00096 Genomic DNA. Translation: AAC76959.1 .
    AP009048 Genomic DNA. Translation: BAE77335.1 .
    PIRi S12574. R5EC10.
    RefSeqi NP_418412.1. NC_000913.3.
    YP_491476.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J0T electron microscopy 12.10 J 2-165 [» ]
    3J0W electron microscopy 14.70 J 2-165 [» ]
    3J0Y electron microscopy 13.50 J 2-165 [» ]
    3J11 electron microscopy 13.10 J 2-165 [» ]
    3J12 electron microscopy 11.50 J 2-165 [» ]
    3J14 electron microscopy 11.50 J 2-165 [» ]
    3J37 electron microscopy 9.80 J 2-165 [» ]
    3J5O electron microscopy 6.80 5 1-165 [» ]
    3J5U electron microscopy 7.60 J 1-165 [» ]
    3J5W electron microscopy 7.60 J 1-165 [» ]
    3SGF X-ray 3.20 H 1-165 [» ]
    3UOS X-ray 3.70 H 1-165 [» ]
    4KIX X-ray 2.90 5 1-165 [» ]
    4KIZ X-ray 2.90 5 1-165 [» ]
    4KJ1 X-ray 2.90 5 1-165 [» ]
    4KJ5 X-ray 2.90 5 1-165 [» ]
    4KJ9 X-ray 2.90 5 1-165 [» ]
    ProteinModelPortali P0A7J3.
    SMRi P0A7J3. Positions 1-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852784. 1 interaction.
    DIPi DIP-35816N.
    IntActi P0A7J3. 52 interactions.
    MINTi MINT-1264502.
    STRINGi 511145.b3985.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7J3.
    PRIDEi P0A7J3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76959 ; AAC76959 ; b3985 .
    BAE77335 ; BAE77335 ; BAE77335 .
    GeneIDi 12930514.
    948490.
    KEGGi ecj:Y75_p3212.
    eco:b3985.
    PATRICi 32123491. VBIEscCol129921_4098.

    Organism-specific databases

    EchoBASEi EB0864.
    EcoGenei EG10871. rplJ.

    Phylogenomic databases

    eggNOGi COG0244.
    HOGENOMi HOG000004851.
    KOi K02864.
    OMAi FSMEDPG.
    OrthoDBi EOG6DNTDR.
    PhylomeDBi P0A7J3.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10871-MONOMER.
    ECOL316407:JW3948-MONOMER.

    Miscellaneous databases

    PROi P0A7J3.

    Gene expression databases

    Genevestigatori P0A7J3.

    Family and domain databases

    HAMAPi MF_00362. Ribosomal_L10.
    InterProi IPR022973. Ribosomal_L10.
    IPR001790. Ribosomal_L10/acidic_P0.
    IPR002363. Ribosomal_L10_eubac_CS.
    [Graphical view ]
    Pfami PF00466. Ribosomal_L10. 1 hit.
    [Graphical view ]
    PROSITEi PS01109. RIBOSOMAL_L10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
      Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
      Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The ribosomal protein L8 is a complex L7/L12 and L10."
      Pettersson I., Hardy S.J.S., Liljas A.
      FEBS Lett. 64:135-138(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-165.
      Strain: MRE-600.
    6. "The primary structure of protein L10 from Escherichia coli ribosomes."
      Dovgas N.V., Vinokurov L.M., Velmoga I.S., Alakhov Y.B., Ovchinnikov Y.A.
      FEBS Lett. 67:58-61(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-165, SEQUENCE REVISION.
      Strain: MRE-600.
    7. "Primary structure of protein L10 from the large subunit of Escherichia coli ribosomes."
      Heiland I., Brauer D., Wittmann-Liebold B.
      Hoppe-Seyler's Z. Physiol. Chem. 357:1751-1770(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-165.
      Strain: K12.
    8. "Feedback regulation of the rplJL-rpoBC ribosomal protein operon of Escherichia coli requires a region of mRNA secondary structure."
      Climie S.C., Friesen J.D.
      J. Mol. Biol. 198:371-381(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSLATION REGULATION.
    9. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
      Arnold R.J., Reilly J.P.
      Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
    10. "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria."
      Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H., Robinson C.V.
      Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, STOICHIOMETRY, MASS SPECTROMETRY.
    11. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-37 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    12. "Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G."
      Mandava C.S., Peisker K., Ederth J., Kumar R., Ge X., Szaflarski W., Sanyal S.
      Nucleic Acids Res. 40:2054-2064(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 156-ALA--ALA-165.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiRL10_ECOLI
    AccessioniPrimary (citable) accession number: P0A7J3
    Secondary accession number(s): P02408, Q2M8S1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Ribosomal proteins
      Ribosomal proteins families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3