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P0C018

- RL18_ECOLI

UniProt

P0C018 - RL18_ECOLI

Protein

50S ribosomal protein L18

Gene

rplR

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10879-MONOMER.
    ECOL316407:JW3266-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L18
    Gene namesi
    Name:rplR
    Ordered Locus Names:b3304, JW3266
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10879. rplR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11711750S ribosomal protein L18PRO_0000131258Add
    BLAST

    Post-translational modificationi

    The protein has been shown to contain a phosphoserine, which was required for the protein to bind to 5S rRNA (PubMed:10529214). However, the presence of this phosphoserine is controversial, and it has not been seen by mass spectrometry.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP0C018.
    PRIDEiP0C018.

    Expressioni

    Gene expression databases

    GenevestigatoriP0C018.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.

    Protein-protein interaction databases

    DIPiDIP-47908N.
    IntActiP0C018. 35 interactions.
    MINTiMINT-1293631.
    STRINGi511145.b3304.

    Structurei

    Secondary structure

    1
    117
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 2117
    Beta strandi25 – 306
    Beta strandi31 – 333
    Beta strandi35 – 406
    Beta strandi44 – 463
    Beta strandi47 – 504
    Beta strandi53 – 553
    Helixi56 – 594
    Beta strandi63 – 675
    Helixi68 – 8417
    Beta strandi91 – 933
    Beta strandi99 – 1013
    Helixi104 – 1129

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ML5electron microscopy14.00q2-117[»]
    1P85electron microscopy12.30M1-117[»]
    1P86electron microscopy11.50M1-117[»]
    1VS6X-ray3.46O1-117[»]
    1VS8X-ray3.46O1-117[»]
    1VT2X-ray3.30O1-117[»]
    2AW4X-ray3.46O1-117[»]
    2AWBX-ray3.46O1-117[»]
    2GYAelectron microscopy15.00M3-115[»]
    2GYCelectron microscopy15.00M3-115[»]
    2I2TX-ray3.22O1-117[»]
    2I2VX-ray3.22O1-117[»]
    2J28electron microscopy8.00O1-117[»]
    2QAMX-ray3.21O1-117[»]
    2QAOX-ray3.21O1-117[»]
    2QBAX-ray3.54O1-117[»]
    2QBCX-ray3.54O1-117[»]
    2QBEX-ray3.30O1-117[»]
    2QBGX-ray3.30O1-117[»]
    2QBIX-ray4.00O1-117[»]
    2QBKX-ray4.00O1-117[»]
    2QOVX-ray3.93O1-117[»]
    2QOXX-ray3.93O1-117[»]
    2QOZX-ray3.50O1-117[»]
    2QP1X-ray3.50O1-117[»]
    2RDOelectron microscopy9.10O1-117[»]
    2VHMX-ray3.74O1-117[»]
    2VHNX-ray3.74O1-117[»]
    2WWQelectron microscopy5.80O2-117[»]
    2Z4LX-ray4.45O1-117[»]
    2Z4NX-ray4.45O1-117[»]
    3BBXelectron microscopy10.00O1-117[»]
    3DF2X-ray3.50O1-117[»]
    3DF4X-ray3.50O1-117[»]
    3E1Belectron microscopy-H1-117[»]
    3E1Delectron microscopy-H1-117[»]
    3FIKelectron microscopy6.70O2-117[»]
    3I1NX-ray3.19O1-117[»]
    3I1PX-ray3.19O1-117[»]
    3I1RX-ray3.81O1-117[»]
    3I1TX-ray3.81O1-117[»]
    3I20X-ray3.71O1-117[»]
    3I22X-ray3.71O1-117[»]
    3IZTelectron microscopy-P1-117[»]
    3IZUelectron microscopy-P1-117[»]
    3J01electron microscopy-O1-117[»]
    3J0Telectron microscopy12.10Q1-117[»]
    3J0Welectron microscopy14.70Q1-117[»]
    3J0Yelectron microscopy13.50Q1-117[»]
    3J11electron microscopy13.10Q1-117[»]
    3J12electron microscopy11.50Q1-117[»]
    3J14electron microscopy11.50Q1-117[»]
    3J19electron microscopy8.30O2-117[»]
    3J37electron microscopy9.80S1-117[»]
    3J4Xelectron microscopy12.00O1-117[»]
    3J50electron microscopy20.00O1-117[»]
    3J51electron microscopy17.00O1-117[»]
    3J52electron microscopy12.00O1-117[»]
    3J54electron microscopy13.00O1-117[»]
    3J56electron microscopy15.00O1-117[»]
    3J58electron microscopy17.00O1-117[»]
    3J5Aelectron microscopy12.00O1-117[»]
    3J5Celectron microscopy17.00O1-117[»]
    3J5Eelectron microscopy17.00O1-117[»]
    3J5Gelectron microscopy20.00O1-117[»]
    3J5Ielectron microscopy15.00O1-117[»]
    3J5Kelectron microscopy9.00O1-117[»]
    3J5Lelectron microscopy6.60O2-117[»]
    3J5Oelectron microscopy6.80O1-117[»]
    3J5Uelectron microscopy7.60Q1-117[»]
    3J5Welectron microscopy7.60R1-117[»]
    3KCRelectron microscopy-O1-117[»]
    3OASX-ray3.25O2-117[»]
    3OATX-ray3.25O2-117[»]
    3OFCX-ray3.19O2-117[»]
    3OFDX-ray3.19O2-117[»]
    3OFQX-ray3.10O2-117[»]
    3OFRX-ray3.10O2-117[»]
    3OFZX-ray3.29O2-117[»]
    3OG0X-ray3.29O2-117[»]
    3ORBX-ray3.30O1-117[»]
    3R8SX-ray3.00O2-117[»]
    3R8TX-ray3.00O2-117[»]
    3SGFX-ray3.20S1-117[»]
    3UOSX-ray3.70S1-117[»]
    4CSUelectron microscopy5.50O2-117[»]
    4GARX-ray3.30O1-117[»]
    4GAUX-ray3.30O1-117[»]
    4KIXX-ray2.90O1-117[»]
    4KIZX-ray2.90O1-117[»]
    4KJ1X-ray2.90O1-117[»]
    4KJ3X-ray2.90O1-117[»]
    4KJ5X-ray2.90O1-117[»]
    4KJ7X-ray2.90O1-117[»]
    4KJ9X-ray2.90O1-117[»]
    4KJBX-ray2.90O1-117[»]
    ProteinModelPortaliP0C018.
    SMRiP0C018. Positions 2-117.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C018.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1717Required for binding of the 5S rRNA/L5/L18 complex to the 23S rRNAAdd
    BLAST

    Domaini

    The basic N-terminus is not necessary for binding to 5S rRNA. It is however required for cooperative binding of L5 and L18 to 5S rRNA as well as for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA.

    Sequence similaritiesi

    Belongs to the ribosomal protein L18P family.Curated

    Phylogenomic databases

    eggNOGiCOG0256.
    HOGENOMiHOG000248742.
    KOiK02881.
    OMAiIDDEKGH.
    OrthoDBiEOG64NB48.
    PhylomeDBiP0C018.

    Family and domain databases

    HAMAPiMF_01337_B. Ribosomal_L18_B.
    InterProiIPR005484. Ribosomal_L18/L5.
    IPR004389. Ribosomal_L18_bac-type.
    [Graphical view]
    PfamiPF00861. Ribosomal_L18p. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00060. L18_bact. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0C018-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKKSARIRR ATRARRKLQE LGATRLVVHR TPRHIYAQVI APNGSEVLVA    50
    ASTVEKAIAE QLKYTGNKDA AAAVGKAVAE RALEKGIKDV SFDRSGFQYH 100
    GRVQALADAA REAGLQF 117
    Length:117
    Mass (Da):12,770
    Last modified:July 21, 1986 - v1
    Checksum:iCA1082FF9B5D9697
    GO

    Mass spectrometryi

    Molecular mass is 12769.8 Da from positions 1 - 117. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25721.1.
    U18997 Genomic DNA. Translation: AAA58101.1.
    U00096 Genomic DNA. Translation: AAC76329.1.
    AP009048 Genomic DNA. Translation: BAE77987.1.
    PIRiA02803. R5EC18.
    RefSeqiNP_417763.1. NC_000913.3.
    YP_492128.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76329; AAC76329; b3304.
    BAE77987; BAE77987; BAE77987.
    GeneIDi12934402.
    947804.
    KEGGiecj:Y75_p3872.
    eco:b3304.
    PATRICi32122040. VBIEscCol129921_3397.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25721.1 .
    U18997 Genomic DNA. Translation: AAA58101.1 .
    U00096 Genomic DNA. Translation: AAC76329.1 .
    AP009048 Genomic DNA. Translation: BAE77987.1 .
    PIRi A02803. R5EC18.
    RefSeqi NP_417763.1. NC_000913.3.
    YP_492128.1. NC_007779.1.

    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 q 2-117 [» ]
    1P85 electron microscopy 12.30 M 1-117 [» ]
    1P86 electron microscopy 11.50 M 1-117 [» ]
    1VS6 X-ray 3.46 O 1-117 [» ]
    1VS8 X-ray 3.46 O 1-117 [» ]
    1VT2 X-ray 3.30 O 1-117 [» ]
    2AW4 X-ray 3.46 O 1-117 [» ]
    2AWB X-ray 3.46 O 1-117 [» ]
    2GYA electron microscopy 15.00 M 3-115 [» ]
    2GYC electron microscopy 15.00 M 3-115 [» ]
    2I2T X-ray 3.22 O 1-117 [» ]
    2I2V X-ray 3.22 O 1-117 [» ]
    2J28 electron microscopy 8.00 O 1-117 [» ]
    2QAM X-ray 3.21 O 1-117 [» ]
    2QAO X-ray 3.21 O 1-117 [» ]
    2QBA X-ray 3.54 O 1-117 [» ]
    2QBC X-ray 3.54 O 1-117 [» ]
    2QBE X-ray 3.30 O 1-117 [» ]
    2QBG X-ray 3.30 O 1-117 [» ]
    2QBI X-ray 4.00 O 1-117 [» ]
    2QBK X-ray 4.00 O 1-117 [» ]
    2QOV X-ray 3.93 O 1-117 [» ]
    2QOX X-ray 3.93 O 1-117 [» ]
    2QOZ X-ray 3.50 O 1-117 [» ]
    2QP1 X-ray 3.50 O 1-117 [» ]
    2RDO electron microscopy 9.10 O 1-117 [» ]
    2VHM X-ray 3.74 O 1-117 [» ]
    2VHN X-ray 3.74 O 1-117 [» ]
    2WWQ electron microscopy 5.80 O 2-117 [» ]
    2Z4L X-ray 4.45 O 1-117 [» ]
    2Z4N X-ray 4.45 O 1-117 [» ]
    3BBX electron microscopy 10.00 O 1-117 [» ]
    3DF2 X-ray 3.50 O 1-117 [» ]
    3DF4 X-ray 3.50 O 1-117 [» ]
    3E1B electron microscopy - H 1-117 [» ]
    3E1D electron microscopy - H 1-117 [» ]
    3FIK electron microscopy 6.70 O 2-117 [» ]
    3I1N X-ray 3.19 O 1-117 [» ]
    3I1P X-ray 3.19 O 1-117 [» ]
    3I1R X-ray 3.81 O 1-117 [» ]
    3I1T X-ray 3.81 O 1-117 [» ]
    3I20 X-ray 3.71 O 1-117 [» ]
    3I22 X-ray 3.71 O 1-117 [» ]
    3IZT electron microscopy - P 1-117 [» ]
    3IZU electron microscopy - P 1-117 [» ]
    3J01 electron microscopy - O 1-117 [» ]
    3J0T electron microscopy 12.10 Q 1-117 [» ]
    3J0W electron microscopy 14.70 Q 1-117 [» ]
    3J0Y electron microscopy 13.50 Q 1-117 [» ]
    3J11 electron microscopy 13.10 Q 1-117 [» ]
    3J12 electron microscopy 11.50 Q 1-117 [» ]
    3J14 electron microscopy 11.50 Q 1-117 [» ]
    3J19 electron microscopy 8.30 O 2-117 [» ]
    3J37 electron microscopy 9.80 S 1-117 [» ]
    3J4X electron microscopy 12.00 O 1-117 [» ]
    3J50 electron microscopy 20.00 O 1-117 [» ]
    3J51 electron microscopy 17.00 O 1-117 [» ]
    3J52 electron microscopy 12.00 O 1-117 [» ]
    3J54 electron microscopy 13.00 O 1-117 [» ]
    3J56 electron microscopy 15.00 O 1-117 [» ]
    3J58 electron microscopy 17.00 O 1-117 [» ]
    3J5A electron microscopy 12.00 O 1-117 [» ]
    3J5C electron microscopy 17.00 O 1-117 [» ]
    3J5E electron microscopy 17.00 O 1-117 [» ]
    3J5G electron microscopy 20.00 O 1-117 [» ]
    3J5I electron microscopy 15.00 O 1-117 [» ]
    3J5K electron microscopy 9.00 O 1-117 [» ]
    3J5L electron microscopy 6.60 O 2-117 [» ]
    3J5O electron microscopy 6.80 O 1-117 [» ]
    3J5U electron microscopy 7.60 Q 1-117 [» ]
    3J5W electron microscopy 7.60 R 1-117 [» ]
    3KCR electron microscopy - O 1-117 [» ]
    3OAS X-ray 3.25 O 2-117 [» ]
    3OAT X-ray 3.25 O 2-117 [» ]
    3OFC X-ray 3.19 O 2-117 [» ]
    3OFD X-ray 3.19 O 2-117 [» ]
    3OFQ X-ray 3.10 O 2-117 [» ]
    3OFR X-ray 3.10 O 2-117 [» ]
    3OFZ X-ray 3.29 O 2-117 [» ]
    3OG0 X-ray 3.29 O 2-117 [» ]
    3ORB X-ray 3.30 O 1-117 [» ]
    3R8S X-ray 3.00 O 2-117 [» ]
    3R8T X-ray 3.00 O 2-117 [» ]
    3SGF X-ray 3.20 S 1-117 [» ]
    3UOS X-ray 3.70 S 1-117 [» ]
    4CSU electron microscopy 5.50 O 2-117 [» ]
    4GAR X-ray 3.30 O 1-117 [» ]
    4GAU X-ray 3.30 O 1-117 [» ]
    4KIX X-ray 2.90 O 1-117 [» ]
    4KIZ X-ray 2.90 O 1-117 [» ]
    4KJ1 X-ray 2.90 O 1-117 [» ]
    4KJ3 X-ray 2.90 O 1-117 [» ]
    4KJ5 X-ray 2.90 O 1-117 [» ]
    4KJ7 X-ray 2.90 O 1-117 [» ]
    4KJ9 X-ray 2.90 O 1-117 [» ]
    4KJB X-ray 2.90 O 1-117 [» ]
    ProteinModelPortali P0C018.
    SMRi P0C018. Positions 2-117.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47908N.
    IntActi P0C018. 35 interactions.
    MINTi MINT-1293631.
    STRINGi 511145.b3304.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0C018.
    PRIDEi P0C018.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76329 ; AAC76329 ; b3304 .
    BAE77987 ; BAE77987 ; BAE77987 .
    GeneIDi 12934402.
    947804.
    KEGGi ecj:Y75_p3872.
    eco:b3304.
    PATRICi 32122040. VBIEscCol129921_3397.

    Organism-specific databases

    EchoBASEi EB0872.
    EcoGenei EG10879. rplR.

    Phylogenomic databases

    eggNOGi COG0256.
    HOGENOMi HOG000248742.
    KOi K02881.
    OMAi IDDEKGH.
    OrthoDBi EOG64NB48.
    PhylomeDBi P0C018.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10879-MONOMER.
    ECOL316407:JW3266-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0C018.
    PROi P0C018.

    Gene expression databases

    Genevestigatori P0C018.

    Family and domain databases

    HAMAPi MF_01337_B. Ribosomal_L18_B.
    InterProi IPR005484. Ribosomal_L18/L5.
    IPR004389. Ribosomal_L18_bac-type.
    [Graphical view ]
    Pfami PF00861. Ribosomal_L18p. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00060. L18_bact. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of the 5S RNA binding protein L18 from Escherichia coli ribosomes."
      Brosius J., Schiltz E., Chen R.
      FEBS Lett. 56:359-361(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: K.
    2. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
      Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
      Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    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. "Stoichiometry, cooperativity, and stability of interactions between 5S RNA and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia coli."
      Spierer P., Zimmermann R.A.
      Biochemistry 17:2474-2479(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: FORMATION OF THE 5S RRNA/L5/L18/L25 SUBCOMPLEX.
    6. "Fragment of protein L18 from the Escherichia coli ribosome that contains the 5S RNA binding site."
      Newberry V., Brosius J., Garrett R.
      Nucleic Acids Res. 5:1753-1766(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE BASIC N-TERMINUS.
    7. "Cooperative interactions among protein and RNA components of the 50S ribosomal subunit of Escherichia coli."
      Spierer P., Wang C.-C., Marsh T.L., Zimmermann R.A.
      Nucleic Acids Res. 6:1669-1682(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF 5S RRNA/L5/L18 WITH 23S RRNA.
      Strain: MRE-600.
    8. "The role of the basic N-terminal region of protein L18 in 5S RNA-23S RNA complex formation."
      Newberry V., Garrett R.A.
      Nucleic Acids Res. 8:4131-4142(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: REQUIREMENT OF N-TERMINUS FOR FORMATION OF 5S RRNA-23S RRNA COMPLEX.
      Strain: MRE-600.
    9. "Assembly map of the large subunit (50S) of Escherichia coli ribosomes."
      Rohl R., Nierhaus K.H.
      Proc. Natl. Acad. Sci. U.S.A. 79:729-733(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: REQUIREMENT FOR INCORPORATION OF 5S RRNA INTO THE 50S SUBUNIT.
      Strain: MRE-600.
    10. "5S rRNA sugar-phosphate backbone protection in complexes with specific ribosomal proteins."
      Shpanchenko O.V., Zvereva M.I., Dontsova O.A., Nierhaus K.H., Bogdanov A.A.
      FEBS Lett. 394:71-75(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF A 5S RRNA/L5/L18/L25 SUBCOMPLEX.
      Strain: K12 / A19.
    11. "Phosphorylation of ribosomal protein L18 is required for its folding and binding to 5S rRNA."
      Bloemink M.J., Moore P.B.
      Biochemistry 38:13385-13390(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    12. "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.
    13. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
      Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
      Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
      Strain: MRE-600.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL18_ECOLI
    AccessioniPrimary (citable) accession number: P0C018
    Secondary accession number(s): P02419, Q2M6W9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 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