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P60723

- RL4_ECOLI

UniProt

P60723 - RL4_ECOLI

Protein

50S ribosomal protein L4

Gene

rplD

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 123 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.1 Publication
    Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).1 Publication
    Forms part of the polypeptide exit tunnel.1 Publication
    Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.1 Publication

    GO - Molecular functioni

    1. rRNA binding Source: UniProtKB-HAMAP
    2. structural constituent of ribosome Source: InterPro
    3. translation repressor activity Source: EcoliWiki

    GO - Biological processi

    1. DNA-templated transcription, termination Source: UniProtKB-KW
    2. negative regulation of translation Source: GOC
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. response to antibiotic Source: UniProtKB-KW
    5. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Antibiotic resistance, Transcription, Transcription regulation, Transcription termination, Translation regulation

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10867-MONOMER.
    ECOL316407:JW3281-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L4
    Gene namesi
    Name:rplD
    Synonyms:eryA
    Ordered Locus Names:b3319, JW3281
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10867. rplD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 8849Missing: Regulates the S10 operon normally. Assembles into ribosomes in vivo. 1 PublicationAdd
    BLAST
    Mutagenesisi67 – 10337Missing: Regulates the S10 operon normally. Does not assemble into ribosomes in vivo. 1 PublicationAdd
    BLAST
    Mutagenesisi93 – 1019Missing: Regulates the S10 operon normally. Not stably associated with the ribosome in vivo. 1 Publication
    Mutagenesisi131 – 1311T → I: Does not regulate the S10 operon; assembles into ribosomes in vivo. 1 Publication
    Mutagenesisi134 – 1341L → P: Does not regulate the S10 operon in vivo. 1 Publication
    Mutagenesisi160 – 1601A → V: Does not regulate the S10 operon; assembles into ribosomes in vivo. 1 Publication
    Mutagenesisi167 – 1671V → D: Does not regulate the S10 operon in vivo. 1 Publication
    Mutagenesisi171 – 20131DATGI…EEMLA → RRSK: Loss of S10 operon regulation. Assembles into ribosomes in vivo. 1 PublicationAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20120150S ribosomal protein L4PRO_0000129215Add
    BLAST

    Proteomic databases

    PaxDbiP60723.
    PRIDEiP60723.

    Expressioni

    Gene expression databases

    GenevestigatoriP60723.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit.

    Protein-protein interaction databases

    DIPiDIP-35791N.
    IntActiP60723. 214 interactions.
    MINTiMINT-1219709.
    STRINGi511145.b3319.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Helixi16 – 194
    Beta strandi22 – 243
    Helixi25 – 3612
    Turni37 – 393
    Turni49 – 513
    Beta strandi52 – 543
    Beta strandi62 – 676
    Beta strandi78 – 814
    Beta strandi83 – 853
    Helixi98 – 11215
    Turni113 – 1164
    Beta strandi118 – 1203
    Beta strandi121 – 1233
    Beta strandi127 – 1293
    Helixi131 – 14111
    Beta strandi144 – 1463
    Beta strandi149 – 1524
    Helixi155 – 1595
    Beta strandi160 – 1634
    Beta strandi165 – 1673
    Helixi172 – 1743
    Helixi177 – 1826
    Beta strandi183 – 1864
    Helixi190 – 19910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P85electron microscopy12.30C1-201[»]
    1P86electron microscopy11.50C1-201[»]
    1VS6X-ray3.46E1-201[»]
    1VS8X-ray3.46E1-201[»]
    1VT2X-ray3.30E1-201[»]
    2AW4X-ray3.46E1-201[»]
    2AWBX-ray3.46E1-201[»]
    2GYAelectron microscopy15.00C1-198[»]
    2GYCelectron microscopy15.00C1-198[»]
    2I2TX-ray3.22E1-201[»]
    2I2VX-ray3.22E1-201[»]
    2J28electron microscopy8.00E1-201[»]
    2QAMX-ray3.21E1-201[»]
    2QAOX-ray3.21E1-201[»]
    2QBAX-ray3.54E1-201[»]
    2QBCX-ray3.54E1-201[»]
    2QBEX-ray3.30E1-201[»]
    2QBGX-ray3.30E1-201[»]
    2QBIX-ray4.00E1-201[»]
    2QBKX-ray4.00E1-201[»]
    2QOVX-ray3.93E1-201[»]
    2QOXX-ray3.93E1-201[»]
    2QOZX-ray3.50E1-201[»]
    2QP1X-ray3.50E1-201[»]
    2RDOelectron microscopy9.10E1-201[»]
    2VHMX-ray3.74E1-201[»]
    2VHNX-ray3.74E1-201[»]
    2WWQelectron microscopy5.80E1-201[»]
    2Z4LX-ray4.45E1-201[»]
    2Z4NX-ray4.45E1-201[»]
    3BBXelectron microscopy10.00E1-201[»]
    3DF2X-ray3.50E1-201[»]
    3DF4X-ray3.50E1-201[»]
    3E1Belectron microscopy-11-201[»]
    3E1Delectron microscopy-11-201[»]
    3FIKelectron microscopy6.70E1-201[»]
    3I1NX-ray3.19E1-201[»]
    3I1PX-ray3.19E1-201[»]
    3I1RX-ray3.81E1-201[»]
    3I1TX-ray3.81E1-201[»]
    3I20X-ray3.71E1-201[»]
    3I22X-ray3.71E1-201[»]
    3IZTelectron microscopy-F1-201[»]
    3IZUelectron microscopy-F1-201[»]
    3J01electron microscopy-E1-201[»]
    3J0Telectron microscopy12.10F1-201[»]
    3J0Welectron microscopy14.70F1-201[»]
    3J0Yelectron microscopy13.50F1-201[»]
    3J11electron microscopy13.10F1-201[»]
    3J12electron microscopy11.50F1-201[»]
    3J14electron microscopy11.50F1-201[»]
    3J19electron microscopy8.30E1-201[»]
    3J37electron microscopy9.80F1-201[»]
    3J4Xelectron microscopy12.00E1-201[»]
    3J50electron microscopy20.00E1-201[»]
    3J51electron microscopy17.00E1-201[»]
    3J52electron microscopy12.00E1-201[»]
    3J54electron microscopy13.00E1-201[»]
    3J56electron microscopy15.00E1-201[»]
    3J58electron microscopy17.00E1-201[»]
    3J5Aelectron microscopy12.00E1-201[»]
    3J5Celectron microscopy17.00E1-201[»]
    3J5Eelectron microscopy17.00E1-201[»]
    3J5Gelectron microscopy20.00E1-201[»]
    3J5Ielectron microscopy15.00E1-201[»]
    3J5Kelectron microscopy9.00E1-201[»]
    3J5Lelectron microscopy6.60E1-201[»]
    3J5Oelectron microscopy6.80E1-201[»]
    3J5Uelectron microscopy7.60F1-201[»]
    3J5Welectron microscopy7.60F1-201[»]
    3KCRelectron microscopy-E1-201[»]
    3OASX-ray3.25E1-201[»]
    3OATX-ray3.25E1-201[»]
    3OFCX-ray3.19E1-201[»]
    3OFDX-ray3.19E1-201[»]
    3OFQX-ray3.10E1-201[»]
    3OFRX-ray3.10E1-201[»]
    3OFZX-ray3.29E1-201[»]
    3OG0X-ray3.29E1-201[»]
    3ORBX-ray3.30E1-201[»]
    3R8SX-ray3.00E1-201[»]
    3R8TX-ray3.00E1-201[»]
    3SGFX-ray3.20E1-201[»]
    3UOSX-ray3.70E1-201[»]
    4CSUelectron microscopy5.50E1-201[»]
    4GARX-ray3.30E1-201[»]
    4GAUX-ray3.30E1-201[»]
    4KIXX-ray2.90E1-201[»]
    4KIZX-ray2.90E1-201[»]
    4KJ1X-ray2.90E1-201[»]
    4KJ3X-ray2.90E1-201[»]
    4KJ5X-ray2.90E1-201[»]
    4KJ7X-ray2.90E1-201[»]
    4KJ9X-ray2.90E1-201[»]
    4KJBX-ray2.90E1-201[»]
    DisProtiDP00600.
    ProteinModelPortaliP60723.
    SMRiP60723. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60723.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L4P family.Curated

    Phylogenomic databases

    eggNOGiCOG0088.
    HOGENOMiHOG000248766.
    KOiK02926.
    OMAiFDEYLYL.
    OrthoDBiEOG6M0T9G.
    PhylomeDBiP60723.

    Family and domain databases

    Gene3Di3.40.1370.10. 1 hit.
    HAMAPiMF_01328_B. Ribosomal_L4_B.
    InterProiIPR002136. Ribosomal_L4/L1e.
    IPR013005. Ribosomal_L4/L1e_bac-type.
    IPR023574. Ribosomal_L4_dom.
    [Graphical view]
    PANTHERiPTHR10746. PTHR10746. 1 hit.
    PfamiPF00573. Ribosomal_L4. 1 hit.
    [Graphical view]
    SUPFAMiSSF52166. SSF52166. 1 hit.
    TIGRFAMsiTIGR03953. rplD_bact. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P60723-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA    50
    EVTGSGKKPW RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM 100
    YRGALKSILS ELVRQDRLIV VEKFSVEAPK TKLLAQKLKD MALEDVLIIT 150
    GELDENLFLA ARNLHKVDVR DATGIDPVSL IAFDKVVMTA DAVKQVEEML 200
    A 201
    Length:201
    Mass (Da):22,087
    Last modified:July 21, 1986 - v1
    Checksum:i3A953206B0F083B5
    GO

    Mass spectrometryi

    Molecular mass is 22086.2 Da from positions 1 - 201. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631K → E in strain: N282; confers erythromycin resistance. Ribosomes bind erythromycin poorly and have reduced peptidyltransferase activity. 50S subunits assemble normally, even in the presence of drug, but assembly is cold-sensitive at 20 degrees Celsius.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26461.1.
    U18997 Genomic DNA. Translation: AAA58116.1.
    U00096 Genomic DNA. Translation: AAC76344.1.
    AP009048 Genomic DNA. Translation: BAE77972.1.
    PIRiC23129. R5EC4.
    RefSeqiNP_417778.1. NC_000913.3.
    YP_492113.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76344; AAC76344; b3319.
    BAE77972; BAE77972; BAE77972.
    GeneIDi12932297.
    947818.
    KEGGiecj:Y75_p3857.
    eco:b3319.
    PATRICi32122070. VBIEscCol129921_3412.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26461.1 .
    U18997 Genomic DNA. Translation: AAA58116.1 .
    U00096 Genomic DNA. Translation: AAC76344.1 .
    AP009048 Genomic DNA. Translation: BAE77972.1 .
    PIRi C23129. R5EC4.
    RefSeqi NP_417778.1. NC_000913.3.
    YP_492113.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P85 electron microscopy 12.30 C 1-201 [» ]
    1P86 electron microscopy 11.50 C 1-201 [» ]
    1VS6 X-ray 3.46 E 1-201 [» ]
    1VS8 X-ray 3.46 E 1-201 [» ]
    1VT2 X-ray 3.30 E 1-201 [» ]
    2AW4 X-ray 3.46 E 1-201 [» ]
    2AWB X-ray 3.46 E 1-201 [» ]
    2GYA electron microscopy 15.00 C 1-198 [» ]
    2GYC electron microscopy 15.00 C 1-198 [» ]
    2I2T X-ray 3.22 E 1-201 [» ]
    2I2V X-ray 3.22 E 1-201 [» ]
    2J28 electron microscopy 8.00 E 1-201 [» ]
    2QAM X-ray 3.21 E 1-201 [» ]
    2QAO X-ray 3.21 E 1-201 [» ]
    2QBA X-ray 3.54 E 1-201 [» ]
    2QBC X-ray 3.54 E 1-201 [» ]
    2QBE X-ray 3.30 E 1-201 [» ]
    2QBG X-ray 3.30 E 1-201 [» ]
    2QBI X-ray 4.00 E 1-201 [» ]
    2QBK X-ray 4.00 E 1-201 [» ]
    2QOV X-ray 3.93 E 1-201 [» ]
    2QOX X-ray 3.93 E 1-201 [» ]
    2QOZ X-ray 3.50 E 1-201 [» ]
    2QP1 X-ray 3.50 E 1-201 [» ]
    2RDO electron microscopy 9.10 E 1-201 [» ]
    2VHM X-ray 3.74 E 1-201 [» ]
    2VHN X-ray 3.74 E 1-201 [» ]
    2WWQ electron microscopy 5.80 E 1-201 [» ]
    2Z4L X-ray 4.45 E 1-201 [» ]
    2Z4N X-ray 4.45 E 1-201 [» ]
    3BBX electron microscopy 10.00 E 1-201 [» ]
    3DF2 X-ray 3.50 E 1-201 [» ]
    3DF4 X-ray 3.50 E 1-201 [» ]
    3E1B electron microscopy - 1 1-201 [» ]
    3E1D electron microscopy - 1 1-201 [» ]
    3FIK electron microscopy 6.70 E 1-201 [» ]
    3I1N X-ray 3.19 E 1-201 [» ]
    3I1P X-ray 3.19 E 1-201 [» ]
    3I1R X-ray 3.81 E 1-201 [» ]
    3I1T X-ray 3.81 E 1-201 [» ]
    3I20 X-ray 3.71 E 1-201 [» ]
    3I22 X-ray 3.71 E 1-201 [» ]
    3IZT electron microscopy - F 1-201 [» ]
    3IZU electron microscopy - F 1-201 [» ]
    3J01 electron microscopy - E 1-201 [» ]
    3J0T electron microscopy 12.10 F 1-201 [» ]
    3J0W electron microscopy 14.70 F 1-201 [» ]
    3J0Y electron microscopy 13.50 F 1-201 [» ]
    3J11 electron microscopy 13.10 F 1-201 [» ]
    3J12 electron microscopy 11.50 F 1-201 [» ]
    3J14 electron microscopy 11.50 F 1-201 [» ]
    3J19 electron microscopy 8.30 E 1-201 [» ]
    3J37 electron microscopy 9.80 F 1-201 [» ]
    3J4X electron microscopy 12.00 E 1-201 [» ]
    3J50 electron microscopy 20.00 E 1-201 [» ]
    3J51 electron microscopy 17.00 E 1-201 [» ]
    3J52 electron microscopy 12.00 E 1-201 [» ]
    3J54 electron microscopy 13.00 E 1-201 [» ]
    3J56 electron microscopy 15.00 E 1-201 [» ]
    3J58 electron microscopy 17.00 E 1-201 [» ]
    3J5A electron microscopy 12.00 E 1-201 [» ]
    3J5C electron microscopy 17.00 E 1-201 [» ]
    3J5E electron microscopy 17.00 E 1-201 [» ]
    3J5G electron microscopy 20.00 E 1-201 [» ]
    3J5I electron microscopy 15.00 E 1-201 [» ]
    3J5K electron microscopy 9.00 E 1-201 [» ]
    3J5L electron microscopy 6.60 E 1-201 [» ]
    3J5O electron microscopy 6.80 E 1-201 [» ]
    3J5U electron microscopy 7.60 F 1-201 [» ]
    3J5W electron microscopy 7.60 F 1-201 [» ]
    3KCR electron microscopy - E 1-201 [» ]
    3OAS X-ray 3.25 E 1-201 [» ]
    3OAT X-ray 3.25 E 1-201 [» ]
    3OFC X-ray 3.19 E 1-201 [» ]
    3OFD X-ray 3.19 E 1-201 [» ]
    3OFQ X-ray 3.10 E 1-201 [» ]
    3OFR X-ray 3.10 E 1-201 [» ]
    3OFZ X-ray 3.29 E 1-201 [» ]
    3OG0 X-ray 3.29 E 1-201 [» ]
    3ORB X-ray 3.30 E 1-201 [» ]
    3R8S X-ray 3.00 E 1-201 [» ]
    3R8T X-ray 3.00 E 1-201 [» ]
    3SGF X-ray 3.20 E 1-201 [» ]
    3UOS X-ray 3.70 E 1-201 [» ]
    4CSU electron microscopy 5.50 E 1-201 [» ]
    4GAR X-ray 3.30 E 1-201 [» ]
    4GAU X-ray 3.30 E 1-201 [» ]
    4KIX X-ray 2.90 E 1-201 [» ]
    4KIZ X-ray 2.90 E 1-201 [» ]
    4KJ1 X-ray 2.90 E 1-201 [» ]
    4KJ3 X-ray 2.90 E 1-201 [» ]
    4KJ5 X-ray 2.90 E 1-201 [» ]
    4KJ7 X-ray 2.90 E 1-201 [» ]
    4KJ9 X-ray 2.90 E 1-201 [» ]
    4KJB X-ray 2.90 E 1-201 [» ]
    DisProti DP00600.
    ProteinModelPortali P60723.
    SMRi P60723. Positions 1-201.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35791N.
    IntActi P60723. 214 interactions.
    MINTi MINT-1219709.
    STRINGi 511145.b3319.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P60723.
    PRIDEi P60723.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76344 ; AAC76344 ; b3319 .
    BAE77972 ; BAE77972 ; BAE77972 .
    GeneIDi 12932297.
    947818.
    KEGGi ecj:Y75_p3857.
    eco:b3319.
    PATRICi 32122070. VBIEscCol129921_3412.

    Organism-specific databases

    EchoBASEi EB0860.
    EcoGenei EG10867. rplD.

    Phylogenomic databases

    eggNOGi COG0088.
    HOGENOMi HOG000248766.
    KOi K02926.
    OMAi FDEYLYL.
    OrthoDBi EOG6M0T9G.
    PhylomeDBi P60723.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10867-MONOMER.
    ECOL316407:JW3281-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P60723.
    PROi P60723.

    Gene expression databases

    Genevestigatori P60723.

    Family and domain databases

    Gene3Di 3.40.1370.10. 1 hit.
    HAMAPi MF_01328_B. Ribosomal_L4_B.
    InterProi IPR002136. Ribosomal_L4/L1e.
    IPR013005. Ribosomal_L4/L1e_bac-type.
    IPR023574. Ribosomal_L4_dom.
    [Graphical view ]
    PANTHERi PTHR10746. PTHR10746. 1 hit.
    Pfami PF00573. Ribosomal_L4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52166. SSF52166. 1 hit.
    TIGRFAMsi TIGR03953. rplD_bact. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of protein L4 from the large subunit of the Escherichia coli ribosome."
      Kimura M., Wittmann-Liebold B.
      FEBS Lett. 121:317-322(1980)
      Cited for: PROTEIN SEQUENCE.
    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. "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 1-12.
      Strain: K12 / EMG2.
    6. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
      Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
      EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-50, CROSS-LINKING TO RRNA.
      Strain: MRE-600.
    7. "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.
    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. "Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins."
      Wittmann H.G., Stoffler G., Apirion D., Rosen L., Tanaka K., Tamaki M., Takata R., Dekio S., Otaka E.
      Mol. Gen. Genet. 127:175-189(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOCHEMICAL CHARACTERIZATION OF AN ERYTHROMYCIN-RESISTANT VARIANT.
      Strain: N282.
    10. "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.
    11. "Autogenous control of the S10 ribosomal protein operon of Escherichia coli: genetic dissection of transcriptional and posttranscriptional regulation."
      Freedman L.P., Zengel J.M., Archer R.H., Lindahl L.
      Proc. Natl. Acad. Sci. U.S.A. 84:6516-6520(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION/TRANSLATION REGULATION.
      Strain: K12 / LL308.
    12. "Escherichia coli ribosomal protein L4 stimulates transcription termination at a specific site in the leader of the S10 operon independent of L4-mediated inhibition of translation."
      Zengel J.M., Lindahl L.
      J. Mol. Biol. 213:67-78(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSCRIPTIONAL REGULATION.
      Strain: K12 / LL308.
    13. "Ribosomal protein L4 stimulates in vitro termination of transcription at a NusA-dependent terminator in the S10 operon leader."
      Zengel J.M., Lindahl L.
      Proc. Natl. Acad. Sci. U.S.A. 87:2675-2679(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: REQUIREMENT FOR NUSA IN TRANSCRIPTION TERMINATION CONTROL.
    14. "Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli."
      Chittum H.S., Champney W.S.
      J. Bacteriol. 176:6192-6198(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF CHANGES IN AN ERYTHROMYCIN-RESISTANT VARIANT.
      Strain: N282.
    15. "Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia coli cells."
      Chittum H.S., Champney W.S.
      Curr. Microbiol. 30:273-279(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ERYTHROMYCIN AND RIBOSOME ASSEMBLY.
      Strain: N282 and SK901.
    16. "Ribosomal protein L4 from Escherichia coli utilizes nonidentical determinants for its structural and regulatory functions."
      Li X., Lindahl L., Zengel J.M.
      RNA 2:24-37(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REQUIREMENT FOR RNA-BINDING, MUTAGENESIS, REGULATION-DEFECTIVE MUTANTS.
      Strain: K12 / LL308.
    17. "Phylogenetic analysis of L4-mediated autogenous control of the S10 ribosomal protein operon."
      Allen T., Shen P., Samsel L., Liu R., Lindahl L., Zengel J.M.
      J. Bacteriol. 181:6124-6132(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABILITY TO REGULATE S10 OPERON EXPRESSION IN OTHER BACTERIA.
      Strain: K12 / LL308.
    18. "The extended loops of ribosomal proteins L4 and L22 are not required for ribosome assembly or L4-mediated autogenous control."
      Zengel J.M., Jerauld A., Walker A., Wahl M.C., Lindahl L.
      RNA 9:1188-1197(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REQUIREMENT FOR RIBOSOME ASSEMBLY, S10 OPERON REGULATION.
      Strain: K12 / LL308.
    19. "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.
    20. "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.
    21. "The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22."
      Gabashvili I.S., Gregory S.T., Valle M., Grassucci R., Worbs M., Wahl M.C., Dahlberg A.E., Frank J.
      Mol. Cell 8:181-188(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (17.8 ANGSTROMS), EFFECT OF THE ERYTHROMYCIN-RESISTANT VARIANT ON THE POLYPEPTIDE EXIT TUNNEL.
      Strain: N282.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL4_ECOLI
    AccessioniPrimary (citable) accession number: P60723
    Secondary accession number(s): P02388, Q2M6Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The erythromycin sensitive allele is dominant over the resistant allele.

    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