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P0A7K2

- RL7_ECOLI

UniProt

P0A7K2 - RL7_ECOLI

Protein

50S ribosomal protein L7/L12

Gene

rplL

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G.2 Publications

    GO - Molecular functioni

    1. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10873-MONOMER.
    ECOL316407:JW3949-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L7/L12UniRule annotation
    Alternative name(s):
    L8
    Gene namesi
    Name:rplLUniRule annotation
    Ordered Locus Names:b3986, JW3949
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10873. rplL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi66 – 661K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
    Mutagenesisi67 – 671V → D: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
    Mutagenesisi70 – 701I → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
    Mutagenesisi71 – 711K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
    Mutagenesisi74 – 741R → M: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
    Mutagenesisi85 – 851K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 12112050S ribosomal protein L7/L12PRO_0000157528Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine; in L71 Publication
    Modified residuei82 – 821N6-methyllysine; partial1 Publication

    Post-translational modificationi

    Acetylation of Ser-2 converts L12 to L7.
    Lys-82 was found to be 50% monomethylated.

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    PaxDbiP0A7K2.
    PRIDEiP0A7K2.

    2D gel databases

    SWISS-2DPAGEP0A7K2.

    PTM databases

    PhosSiteiP0810430.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7K2.

    Interactioni

    Subunit structurei

    Homodimer. Part of the 50S ribosomal subunit; present in 4 copies per ribosome. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form part of the ribosomal stalk (called L8). The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Forms a pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion.2 Publications

    Protein-protein interaction databases

    BioGridi852783. 1 interaction.
    DIPiDIP-36009N.
    IntActiP0A7K2. 127 interactions.
    MINTiMINT-1277405.
    STRINGi511145.b3986.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Beta strandi9 – 135
    Helixi17 – 204
    Beta strandi23 – 253
    Helixi26 – 294
    Helixi33 – 5018
    Beta strandi55 – 617
    Helixi63 – 653
    Helixi66 – 7712
    Helixi81 – 899
    Beta strandi92 – 998
    Helixi101 – 11414
    Beta strandi117 – 1215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CTFX-ray1.70A48-121[»]
    1RQSNMR-A48-121[»]
    1RQTNMR-A/B2-38[»]
    1RQUNMR-A/B2-121[»]
    1RQVNMR-A/B2-121[»]
    2BCWelectron microscopy11.20B54-121[»]
    2GYAelectron microscopy15.003/53-121[»]
    2GYCelectron microscopy15.003/53-121[»]
    2XTGelectron microscopy7.80L1-121[»]
    2XUXelectron microscopy7.60L1-121[»]
    3J5Oelectron microscopy6.8061-121[»]
    3J5Welectron microscopy7.60L2-121[»]
    3SGFX-ray3.20J/K/L/M1-121[»]
    3UOSX-ray3.70J/K/L/M1-121[»]
    4KIXX-ray2.9061-121[»]
    ProteinModelPortaliP0A7K2.
    SMRiP0A7K2. Positions 3-121.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7K2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 12168Required for recruitment of EF-Tu and EF-G, and for EF-Tu and EF-G-promoted GTP hydrolysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ribosomal protein L7/L12P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0222.
    HOGENOMiHOG000248813.
    KOiK02935.
    OMAiASMSVME.
    OrthoDBiEOG6WMJ69.
    PhylomeDBiP0A7K2.

    Family and domain databases

    Gene3Di3.30.1390.10. 1 hit.
    HAMAPiMF_00368. Ribosomal_L7_L12.
    InterProiIPR000206. Ribosomal_L7/12.
    IPR014719. Ribosomal_L7/12_C/ClpS-like.
    IPR013823. Ribosomal_L7/L12_C.
    IPR008932. Ribosomal_L7/L12_oligo.
    [Graphical view]
    PANTHERiPTHR11809. PTHR11809. 1 hit.
    PfamiPF00542. Ribosomal_L12. 1 hit.
    [Graphical view]
    ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF48300. SSF48300. 1 hit.
    SSF54736. SSF54736. 1 hit.
    TIGRFAMsiTIGR00855. L12. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P0A7K2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE    50
    EKTEFDVILK AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS 100
    KDDAEALKKA LEEAGAEVEV K 121
    Length:121
    Mass (Da):12,295
    Last modified:January 23, 2007 - v2
    Checksum:i08B051A0CDAA527E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61D → F AA sequence (PubMed:9868784)Curated

    Mass spectrometryi

    Molecular mass is 12206.7 Da from positions 2 - 121. Determined by MALDI. Non-methylated.1 Publication
    Molecular mass is 66643±13 Da from positions 2 - 121. Determined by ESI. Isolated L10(L12)4.1 Publication
    Molecular mass is 12223±1 Da from positions 2 - 121. Determined by ESI. L7, acetylated Ser-2.1 Publication
    Molecular mass is 12164±1 Da from positions 2 - 121. Determined by ESI. L12, unacetylated.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23624.1.
    M38301 Genomic DNA. Translation: AAA24573.1.
    U00006 Genomic DNA. Translation: AAC43084.1.
    U00096 Genomic DNA. Translation: AAC76960.1.
    AP009048 Genomic DNA. Translation: BAE77334.1.
    PIRiS12575. R5EC7.
    RefSeqiNP_418413.1. NC_000913.3.
    YP_491475.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76960; AAC76960; b3986.
    BAE77334; BAE77334; BAE77334.
    GeneIDi12930512.
    948489.
    KEGGiecj:Y75_p3211.
    eco:b3986.
    PATRICi32123493. VBIEscCol129921_4099.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23624.1 .
    M38301 Genomic DNA. Translation: AAA24573.1 .
    U00006 Genomic DNA. Translation: AAC43084.1 .
    U00096 Genomic DNA. Translation: AAC76960.1 .
    AP009048 Genomic DNA. Translation: BAE77334.1 .
    PIRi S12575. R5EC7.
    RefSeqi NP_418413.1. NC_000913.3.
    YP_491475.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CTF X-ray 1.70 A 48-121 [» ]
    1RQS NMR - A 48-121 [» ]
    1RQT NMR - A/B 2-38 [» ]
    1RQU NMR - A/B 2-121 [» ]
    1RQV NMR - A/B 2-121 [» ]
    2BCW electron microscopy 11.20 B 54-121 [» ]
    2GYA electron microscopy 15.00 3/5 3-121 [» ]
    2GYC electron microscopy 15.00 3/5 3-121 [» ]
    2XTG electron microscopy 7.80 L 1-121 [» ]
    2XUX electron microscopy 7.60 L 1-121 [» ]
    3J5O electron microscopy 6.80 6 1-121 [» ]
    3J5W electron microscopy 7.60 L 2-121 [» ]
    3SGF X-ray 3.20 J/K/L/M 1-121 [» ]
    3UOS X-ray 3.70 J/K/L/M 1-121 [» ]
    4KIX X-ray 2.90 6 1-121 [» ]
    ProteinModelPortali P0A7K2.
    SMRi P0A7K2. Positions 3-121.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852783. 1 interaction.
    DIPi DIP-36009N.
    IntActi P0A7K2. 127 interactions.
    MINTi MINT-1277405.
    STRINGi 511145.b3986.

    Chemistry

    ChEMBLi CHEMBL2363135.

    PTM databases

    PhosSitei P0810430.

    2D gel databases

    SWISS-2DPAGE P0A7K2.

    Proteomic databases

    PaxDbi P0A7K2.
    PRIDEi P0A7K2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76960 ; AAC76960 ; b3986 .
    BAE77334 ; BAE77334 ; BAE77334 .
    GeneIDi 12930512.
    948489.
    KEGGi ecj:Y75_p3211.
    eco:b3986.
    PATRICi 32123493. VBIEscCol129921_4099.

    Organism-specific databases

    EchoBASEi EB0866.
    EcoGenei EG10873. rplL.

    Phylogenomic databases

    eggNOGi COG0222.
    HOGENOMi HOG000248813.
    KOi K02935.
    OMAi ASMSVME.
    OrthoDBi EOG6WMJ69.
    PhylomeDBi P0A7K2.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10873-MONOMER.
    ECOL316407:JW3949-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7K2.
    PROi P0A7K2.

    Gene expression databases

    Genevestigatori P0A7K2.

    Family and domain databases

    Gene3Di 3.30.1390.10. 1 hit.
    HAMAPi MF_00368. Ribosomal_L7_L12.
    InterProi IPR000206. Ribosomal_L7/12.
    IPR014719. Ribosomal_L7/12_C/ClpS-like.
    IPR013823. Ribosomal_L7/L12_C.
    IPR008932. Ribosomal_L7/L12_oligo.
    [Graphical view ]
    PANTHERi PTHR11809. PTHR11809. 1 hit.
    Pfami PF00542. Ribosomal_L12. 1 hit.
    [Graphical view ]
    ProDomi PD001326. Ribosomal_L7/L12_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF48300. SSF48300. 1 hit.
    SSF54736. SSF54736. 1 hit.
    TIGRFAMsi TIGR00855. L12. 1 hit.
    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. "Sequence determination in 3'-end proximalely labelled DNA."
      Gurevich A.I., Avakov A.E.
      Bioorg. Khim. 5:301-304(1979)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T."
      Terhorst C., Moeller W., Laursen R., Wittmann-Liebold B.
      Eur. J. Biochem. 34:138-152(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-121.
      Strain: MRE-600.
    7. "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 2-121.
      Strain: MRE-600.
    8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    9. "Small genes/gene-products in Escherichia coli K-12."
      Wasinger V.C., Humphery-Smith I.
      FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Strain: K12.
    10. Cited for: PROTEIN SEQUENCE OF 2-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    11. "The nucleotide sequence at the proximal end of rpoB gene of Escherichia coli."
      Gurevich A.I., Avakov A.E., Kolosov M.N.
      Bioorg. Khim. 5:1735-1739(1979)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-121.
    12. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    13. "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.
    14. "Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation."
      Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M., Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.
      Cell 121:991-1004(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BINDING OF EF-TU AND EF-G, SUBUNIT, MUTAGENESIS OF LYS-66; VAL-67; ILE-70; LYS-71; ARG-74 AND LYS-85.
    15. "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.
    16. "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: FUNCTION IN IF-2 (INFB) AND EF-G (FUSA) ASSOCIATION WITH RIBOSOME.
      Strain: K12 / MG1655 / ATCC 47076.
    17. "Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A."
      Leijonmarck M., Liljas A.
      J. Mol. Biol. 195:555-580(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    18. "Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution."
      Bocharov E.V., Gudkov A.T., Arseniev A.S.
      FEBS Lett. 379:291-294(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    19. "Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10."
      Bocharov E.V., Gudkov A.T., Budovskaya E.V., Arseniev A.S.
      FEBS Lett. 423:347-350(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiRL7_ECOLI
    AccessioniPrimary (citable) accession number: P0A7K2
    Secondary accession number(s): P02392, Q2M8S2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 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, 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