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P0ADZ0

- RL23_ECOLI

UniProt

P0ADZ0 - RL23_ECOLI

Protein

50S ribosomal protein L23

Gene

rplW

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

    One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).2 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: IntAct
    3. rRNA binding Source: UniProtKB-HAMAP
    4. 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:EG10883-MONOMER.
    ECOL316407:JW3280-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L23UniRule annotation
    Gene namesi
    Name:rplWUniRule annotation
    Ordered Locus Names:b3318, JW3280
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10883. rplW.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 183VSE → AAA: Strongly reduces trigger factor binding.
    Mutagenesisi18 – 181E → A: Binds normally to ribosomes; strongly reduces trigger factor binding. 1 Publication
    Mutagenesisi18 – 181E → Q: Strongly reduces trigger factor binding. 1 Publication
    Mutagenesisi51 – 533FEV → AAA: No effect on trigger factor binding.
    Mutagenesisi52 – 521E → K: No effect on trigger factor binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10010050S ribosomal protein L23PRO_0000129407Add
    BLAST

    Proteomic databases

    PaxDbiP0ADZ0.
    PRIDEiP0ADZ0.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ADZ0.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Contacts protein L29 and trigger factor. Might also contact SecE and probably does contact SecG and SecY when the SecYEG translocation complex is docked with the ribosome.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rpsEP0A7W12EBI-542264,EBI-543949

    Protein-protein interaction databases

    DIPiDIP-35972N.
    IntActiP0ADZ0. 73 interactions.
    MINTiMINT-1225825.
    STRINGi511145.b3318.

    Structurei

    Secondary structure

    1
    100
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107
    Beta strandi11 – 144
    Helixi18 – 236
    Beta strandi26 – 283
    Beta strandi32 – 343
    Turni35 – 373
    Helixi41 – 499
    Helixi50 – 523
    Beta strandi61 – 633
    Beta strandi71 – 733
    Beta strandi80 – 823
    Beta strandi88 – 903

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ML5electron microscopy14.00t2-85[»]
    1P85electron microscopy12.30R1-100[»]
    1P86electron microscopy11.50R1-100[»]
    1VS6X-ray3.46T1-100[»]
    1VS8X-ray3.46T1-100[»]
    1VT2X-ray3.30T1-100[»]
    2AW4X-ray3.46T1-100[»]
    2AWBX-ray3.46T1-100[»]
    2GYAelectron microscopy15.00R7-98[»]
    2GYCelectron microscopy15.00R7-98[»]
    2I2TX-ray3.22T1-100[»]
    2I2VX-ray3.22T1-100[»]
    2J28electron microscopy8.00T1-99[»]
    2QAMX-ray3.21T1-100[»]
    2QAOX-ray3.21T1-100[»]
    2QBAX-ray3.54T1-100[»]
    2QBCX-ray3.54T1-100[»]
    2QBEX-ray3.30T1-100[»]
    2QBGX-ray3.30T1-100[»]
    2QBIX-ray4.00T1-100[»]
    2QBKX-ray4.00T1-100[»]
    2QOVX-ray3.93T1-100[»]
    2QOXX-ray3.93T1-100[»]
    2QOZX-ray3.50T1-100[»]
    2QP1X-ray3.50T1-100[»]
    2RDOelectron microscopy9.10T1-100[»]
    2VRHelectron microscopy19.00B1-100[»]
    2WWQelectron microscopy5.80T1-93[»]
    2Z4LX-ray4.45T1-100[»]
    2Z4NX-ray4.45T1-100[»]
    3BBXelectron microscopy10.00T1-100[»]
    3E1Belectron microscopy-M1-99[»]
    3E1Delectron microscopy-M1-99[»]
    3FIKelectron microscopy6.70T1-93[»]
    3I1NX-ray3.19T1-100[»]
    3I1PX-ray3.19T1-100[»]
    3I1RX-ray3.81T1-100[»]
    3I1TX-ray3.81T1-100[»]
    3I20X-ray3.71T1-100[»]
    3I22X-ray3.71T1-100[»]
    3IY9electron microscopy14.10T1-99[»]
    3IZTelectron microscopy-U1-100[»]
    3IZUelectron microscopy-U1-100[»]
    3J01electron microscopy-T1-100[»]
    3J0Telectron microscopy12.10V1-100[»]
    3J0Welectron microscopy14.70V1-100[»]
    3J0Yelectron microscopy13.50V1-100[»]
    3J11electron microscopy13.10V1-100[»]
    3J12electron microscopy11.50V1-100[»]
    3J14electron microscopy11.50V1-100[»]
    3J19electron microscopy8.30T1-93[»]
    3J37electron microscopy9.80X1-100[»]
    3J45electron microscopy9.50T1-100[»]
    3J46electron microscopy10.10T1-100[»]
    3J4Xelectron microscopy12.00T1-93[»]
    3J50electron microscopy20.00T1-93[»]
    3J51electron microscopy17.00T1-93[»]
    3J52electron microscopy12.00T1-93[»]
    3J54electron microscopy13.00T1-93[»]
    3J56electron microscopy15.00T1-93[»]
    3J58electron microscopy17.00T1-93[»]
    3J5Aelectron microscopy12.00T1-93[»]
    3J5Celectron microscopy17.00T1-93[»]
    3J5Eelectron microscopy17.00T1-93[»]
    3J5Gelectron microscopy20.00T1-93[»]
    3J5Ielectron microscopy15.00T1-93[»]
    3J5Kelectron microscopy9.00T1-93[»]
    3J5Lelectron microscopy6.60T1-93[»]
    3J5Oelectron microscopy6.80T1-100[»]
    3J5Uelectron microscopy7.60V1-100[»]
    3J5Welectron microscopy7.60W1-100[»]
    3KCRelectron microscopy-T1-100[»]
    3OASX-ray3.25T1-93[»]
    3OATX-ray3.25T1-93[»]
    3OFCX-ray3.19T1-93[»]
    3OFDX-ray3.19T1-93[»]
    3OFQX-ray3.10T1-93[»]
    3OFRX-ray3.10T1-93[»]
    3OFZX-ray3.29T1-93[»]
    3OG0X-ray3.29T1-93[»]
    3ORBX-ray3.30T1-100[»]
    3R8SX-ray3.00T1-93[»]
    3R8TX-ray3.00T1-93[»]
    3SGFX-ray3.20X1-100[»]
    3UOSX-ray3.70X1-100[»]
    4CSUelectron microscopy5.50T1-100[»]
    4GARX-ray3.30T1-100[»]
    4GAUX-ray3.30T1-100[»]
    4KIXX-ray2.90T1-100[»]
    4KIZX-ray2.90T1-100[»]
    4KJ1X-ray2.90T1-100[»]
    4KJ3X-ray2.90T1-100[»]
    4KJ5X-ray2.90T1-100[»]
    4KJ7X-ray2.90T1-100[»]
    4KJ9X-ray2.90T1-100[»]
    4KJBX-ray2.90T1-100[»]
    ProteinModelPortaliP0ADZ0.
    SMRiP0ADZ0. Positions 7-98.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ADZ0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L23P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0089.
    HOGENOMiHOG000231364.
    KOiK02892.
    OMAiFGRRSDW.
    OrthoDBiEOG6HTP4P.
    PhylomeDBiP0ADZ0.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    HAMAPiMF_01369_B. Ribosomal_L23_B.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR012678. Ribosomal_L23/L15e_core_dom.
    IPR001014. Ribosomal_L23/L25_CS.
    IPR013025. Ribosomal_L25/23.
    [Graphical view]
    PfamiPF00276. Ribosomal_L23. 1 hit.
    [Graphical view]
    SUPFAMiSSF54189. SSF54189. 1 hit.
    PROSITEiPS00050. RIBOSOMAL_L23. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ADZ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL    50
    FEVEVEVVNT LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE 100
    Length:100
    Mass (Da):11,199
    Last modified:December 6, 2005 - v1
    Checksum:i30CD1D77CC7CF9EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801Missing AA sequence (PubMed:391594)Curated

    Mass spectrometryi

    Molecular mass is 11198.0 Da from positions 1 - 100. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26462.1.
    U18997 Genomic DNA. Translation: AAA58115.1.
    U00096 Genomic DNA. Translation: AAC76343.1.
    AP009048 Genomic DNA. Translation: BAE77973.1.
    PIRiA65125. R5EC23.
    RefSeqiNP_417777.1. NC_000913.3.
    YP_492114.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76343; AAC76343; b3318.
    BAE77973; BAE77973; BAE77973.
    GeneIDi12932296.
    947819.
    KEGGiecj:Y75_p3858.
    eco:b3318.
    PATRICi32122068. VBIEscCol129921_3411.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26462.1 .
    U18997 Genomic DNA. Translation: AAA58115.1 .
    U00096 Genomic DNA. Translation: AAC76343.1 .
    AP009048 Genomic DNA. Translation: BAE77973.1 .
    PIRi A65125. R5EC23.
    RefSeqi NP_417777.1. NC_000913.3.
    YP_492114.1. 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 t 2-85 [» ]
    1P85 electron microscopy 12.30 R 1-100 [» ]
    1P86 electron microscopy 11.50 R 1-100 [» ]
    1VS6 X-ray 3.46 T 1-100 [» ]
    1VS8 X-ray 3.46 T 1-100 [» ]
    1VT2 X-ray 3.30 T 1-100 [» ]
    2AW4 X-ray 3.46 T 1-100 [» ]
    2AWB X-ray 3.46 T 1-100 [» ]
    2GYA electron microscopy 15.00 R 7-98 [» ]
    2GYC electron microscopy 15.00 R 7-98 [» ]
    2I2T X-ray 3.22 T 1-100 [» ]
    2I2V X-ray 3.22 T 1-100 [» ]
    2J28 electron microscopy 8.00 T 1-99 [» ]
    2QAM X-ray 3.21 T 1-100 [» ]
    2QAO X-ray 3.21 T 1-100 [» ]
    2QBA X-ray 3.54 T 1-100 [» ]
    2QBC X-ray 3.54 T 1-100 [» ]
    2QBE X-ray 3.30 T 1-100 [» ]
    2QBG X-ray 3.30 T 1-100 [» ]
    2QBI X-ray 4.00 T 1-100 [» ]
    2QBK X-ray 4.00 T 1-100 [» ]
    2QOV X-ray 3.93 T 1-100 [» ]
    2QOX X-ray 3.93 T 1-100 [» ]
    2QOZ X-ray 3.50 T 1-100 [» ]
    2QP1 X-ray 3.50 T 1-100 [» ]
    2RDO electron microscopy 9.10 T 1-100 [» ]
    2VRH electron microscopy 19.00 B 1-100 [» ]
    2WWQ electron microscopy 5.80 T 1-93 [» ]
    2Z4L X-ray 4.45 T 1-100 [» ]
    2Z4N X-ray 4.45 T 1-100 [» ]
    3BBX electron microscopy 10.00 T 1-100 [» ]
    3E1B electron microscopy - M 1-99 [» ]
    3E1D electron microscopy - M 1-99 [» ]
    3FIK electron microscopy 6.70 T 1-93 [» ]
    3I1N X-ray 3.19 T 1-100 [» ]
    3I1P X-ray 3.19 T 1-100 [» ]
    3I1R X-ray 3.81 T 1-100 [» ]
    3I1T X-ray 3.81 T 1-100 [» ]
    3I20 X-ray 3.71 T 1-100 [» ]
    3I22 X-ray 3.71 T 1-100 [» ]
    3IY9 electron microscopy 14.10 T 1-99 [» ]
    3IZT electron microscopy - U 1-100 [» ]
    3IZU electron microscopy - U 1-100 [» ]
    3J01 electron microscopy - T 1-100 [» ]
    3J0T electron microscopy 12.10 V 1-100 [» ]
    3J0W electron microscopy 14.70 V 1-100 [» ]
    3J0Y electron microscopy 13.50 V 1-100 [» ]
    3J11 electron microscopy 13.10 V 1-100 [» ]
    3J12 electron microscopy 11.50 V 1-100 [» ]
    3J14 electron microscopy 11.50 V 1-100 [» ]
    3J19 electron microscopy 8.30 T 1-93 [» ]
    3J37 electron microscopy 9.80 X 1-100 [» ]
    3J45 electron microscopy 9.50 T 1-100 [» ]
    3J46 electron microscopy 10.10 T 1-100 [» ]
    3J4X electron microscopy 12.00 T 1-93 [» ]
    3J50 electron microscopy 20.00 T 1-93 [» ]
    3J51 electron microscopy 17.00 T 1-93 [» ]
    3J52 electron microscopy 12.00 T 1-93 [» ]
    3J54 electron microscopy 13.00 T 1-93 [» ]
    3J56 electron microscopy 15.00 T 1-93 [» ]
    3J58 electron microscopy 17.00 T 1-93 [» ]
    3J5A electron microscopy 12.00 T 1-93 [» ]
    3J5C electron microscopy 17.00 T 1-93 [» ]
    3J5E electron microscopy 17.00 T 1-93 [» ]
    3J5G electron microscopy 20.00 T 1-93 [» ]
    3J5I electron microscopy 15.00 T 1-93 [» ]
    3J5K electron microscopy 9.00 T 1-93 [» ]
    3J5L electron microscopy 6.60 T 1-93 [» ]
    3J5O electron microscopy 6.80 T 1-100 [» ]
    3J5U electron microscopy 7.60 V 1-100 [» ]
    3J5W electron microscopy 7.60 W 1-100 [» ]
    3KCR electron microscopy - T 1-100 [» ]
    3OAS X-ray 3.25 T 1-93 [» ]
    3OAT X-ray 3.25 T 1-93 [» ]
    3OFC X-ray 3.19 T 1-93 [» ]
    3OFD X-ray 3.19 T 1-93 [» ]
    3OFQ X-ray 3.10 T 1-93 [» ]
    3OFR X-ray 3.10 T 1-93 [» ]
    3OFZ X-ray 3.29 T 1-93 [» ]
    3OG0 X-ray 3.29 T 1-93 [» ]
    3ORB X-ray 3.30 T 1-100 [» ]
    3R8S X-ray 3.00 T 1-93 [» ]
    3R8T X-ray 3.00 T 1-93 [» ]
    3SGF X-ray 3.20 X 1-100 [» ]
    3UOS X-ray 3.70 X 1-100 [» ]
    4CSU electron microscopy 5.50 T 1-100 [» ]
    4GAR X-ray 3.30 T 1-100 [» ]
    4GAU X-ray 3.30 T 1-100 [» ]
    4KIX X-ray 2.90 T 1-100 [» ]
    4KIZ X-ray 2.90 T 1-100 [» ]
    4KJ1 X-ray 2.90 T 1-100 [» ]
    4KJ3 X-ray 2.90 T 1-100 [» ]
    4KJ5 X-ray 2.90 T 1-100 [» ]
    4KJ7 X-ray 2.90 T 1-100 [» ]
    4KJ9 X-ray 2.90 T 1-100 [» ]
    4KJB X-ray 2.90 T 1-100 [» ]
    ProteinModelPortali P0ADZ0.
    SMRi P0ADZ0. Positions 7-98.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35972N.
    IntActi P0ADZ0. 73 interactions.
    MINTi MINT-1225825.
    STRINGi 511145.b3318.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0ADZ0.
    PRIDEi P0ADZ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76343 ; AAC76343 ; b3318 .
    BAE77973 ; BAE77973 ; BAE77973 .
    GeneIDi 12932296.
    947819.
    KEGGi ecj:Y75_p3858.
    eco:b3318.
    PATRICi 32122068. VBIEscCol129921_3411.

    Organism-specific databases

    EchoBASEi EB0876.
    EcoGenei EG10883. rplW.

    Phylogenomic databases

    eggNOGi COG0089.
    HOGENOMi HOG000231364.
    KOi K02892.
    OMAi FGRRSDW.
    OrthoDBi EOG6HTP4P.
    PhylomeDBi P0ADZ0.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10883-MONOMER.
    ECOL316407:JW3280-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ADZ0.
    PROi P0ADZ0.

    Gene expression databases

    Genevestigatori P0ADZ0.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    HAMAPi MF_01369_B. Ribosomal_L23_B.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR012678. Ribosomal_L23/L15e_core_dom.
    IPR001014. Ribosomal_L23/L25_CS.
    IPR013025. Ribosomal_L25/23.
    [Graphical view ]
    Pfami PF00276. Ribosomal_L23. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54189. SSF54189. 1 hit.
    PROSITEi PS00050. RIBOSOMAL_L23. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of protein L23 from the Escherichia coli ribosome."
      Wittmann-Liebold B., Greuer B.
      FEBS Lett. 108:69-74(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: K12.
    2. "Structure of the Escherichia coli S10 ribosomal protein operon."
      Zurawski G., Zurawski S.M.
      Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29."
      Wower I., Wower J., Meinke M., Brimacombe R.
      Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO 23S RRNA.
      Strain: MRE-600.
    6. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
      Herold M., Nierhaus K.H.
      J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
      Strain: K12.
    7. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
      Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
      Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO L29.
    8. "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.
    9. Cited for: BINDING TO TRIGGER FACTOR, MUTAGENESIS OF 16-VAL--GLU-18; GLU-18; 51-PHE--VAL-53 AND GLU-52.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    10. "Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
      Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
      J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKS TO FFH (SRP54); TRIGGER FACTOR AND TO NASCENT PROTEIN CHAINS.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    11. "The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome."
      Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.
      RNA 9:566-573(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RECOGNITION PARTICLE.
      Strain: MRE-600.
    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. "Structure of the E. coli protein-conducting channel bound to a translating ribosome."
      Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
      Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX.
      Strain: MRE-600.
    14. "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.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.
    16. Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A NASCENT POLYPEPTIDE CHAIN.

    Entry informationi

    Entry nameiRL23_ECOLI
    AccessioniPrimary (citable) accession number: P0ADZ0
    Secondary accession number(s): P02424, Q2M6Y3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 90 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