Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0AG55

- RL6_ECOLI

UniProt

P0AG55 - RL6_ECOLI

Protein

50S ribosomal protein L6

Gene

rplF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
    Gentamicin-resistant mutations in this protein affect translation fidelity.

    GO - Molecular functioni

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

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10869-MONOMER.
    ECOL316407:JW3267-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L6UniRule annotation
    Gene namesi
    Name:rplFUniRule annotation
    Ordered Locus Names:b3305, JW3267
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10869. rplF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 17717650S ribosomal protein L6PRO_0000131048Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441N6-acetyllysine1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0AG55.
    PRIDEiP0AG55.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AG55.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit.

    Protein-protein interaction databases

    BioGridi852115. 1 interaction.
    DIPiDIP-35860N.
    IntActiP0AG55. 83 interactions.
    MINTiMINT-1244940.
    STRINGi511145.b3305.

    Structurei

    Secondary structure

    1
    177
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 64
    Beta strandi18 – 203
    Beta strandi21 – 255
    Beta strandi29 – 313
    Beta strandi35 – 373
    Beta strandi39 – 446
    Beta strandi46 – 483
    Beta strandi49 – 546
    Beta strandi55 – 573
    Turni59 – 624
    Helixi63 – 8119
    Beta strandi83 – 853
    Beta strandi87 – 915
    Beta strandi94 – 963
    Beta strandi97 – 993
    Beta strandi100 – 1034
    Beta strandi105 – 1084
    Beta strandi109 – 1113
    Beta strandi113 – 1164
    Beta strandi119 – 1246
    Beta strandi126 – 1294
    Beta strandi130 – 1367
    Helixi138 – 15013
    Turni156 – 1583
    Beta strandi161 – 1666

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG0electron microscopy11.50J1-171[»]
    1ML5electron microscopy14.00h2-177[»]
    1P85electron microscopy12.30E2-177[»]
    1P86electron microscopy11.50E2-177[»]
    1VS6X-ray3.46G1-177[»]
    1VS8X-ray3.46G1-177[»]
    1VT2X-ray3.30G1-177[»]
    2AW4X-ray3.46G2-177[»]
    2AWBX-ray3.46G2-177[»]
    2GYAelectron microscopy15.00E6-172[»]
    2GYCelectron microscopy15.00E6-172[»]
    2I2TX-ray3.22G2-177[»]
    2I2VX-ray3.22G2-177[»]
    2J28electron microscopy8.00G2-177[»]
    2QAMX-ray3.21G2-177[»]
    2QAOX-ray3.21G2-177[»]
    2QBAX-ray3.54G2-177[»]
    2QBCX-ray3.54G2-177[»]
    2QBEX-ray3.30G2-177[»]
    2QBGX-ray3.30G2-177[»]
    2QBIX-ray4.00G2-177[»]
    2QBKX-ray4.00G2-177[»]
    2QOVX-ray3.93G2-177[»]
    2QOXX-ray3.93G2-177[»]
    2QOZX-ray3.50G2-177[»]
    2QP1X-ray3.50G2-177[»]
    2RDOelectron microscopy9.10G2-177[»]
    2VHMX-ray3.74G2-177[»]
    2VHNX-ray3.74G2-177[»]
    2WWQelectron microscopy5.80G2-177[»]
    2Z4LX-ray4.45G2-177[»]
    2Z4NX-ray4.45G2-177[»]
    3BBXelectron microscopy10.00G2-177[»]
    3E1Belectron microscopy-31-177[»]
    3E1Delectron microscopy-31-177[»]
    3FIKelectron microscopy6.70G2-177[»]
    3I1NX-ray3.19G1-177[»]
    3I1PX-ray3.19G1-177[»]
    3I1RX-ray3.81G1-177[»]
    3I1TX-ray3.81G1-177[»]
    3I20X-ray3.71G1-177[»]
    3I22X-ray3.71G1-177[»]
    3IZTelectron microscopy-H1-177[»]
    3IZUelectron microscopy-H1-177[»]
    3J01electron microscopy-G2-177[»]
    3J0Telectron microscopy12.10H2-177[»]
    3J0Welectron microscopy14.70H2-177[»]
    3J0Yelectron microscopy13.50H2-177[»]
    3J11electron microscopy13.10H2-177[»]
    3J12electron microscopy11.50H2-177[»]
    3J14electron microscopy11.50H2-177[»]
    3J19electron microscopy8.30G2-177[»]
    3J37electron microscopy9.80H2-177[»]
    3J4Xelectron microscopy12.00G1-177[»]
    3J50electron microscopy20.00G1-177[»]
    3J51electron microscopy17.00G1-177[»]
    3J52electron microscopy12.00G1-177[»]
    3J54electron microscopy13.00G1-177[»]
    3J56electron microscopy15.00G1-177[»]
    3J58electron microscopy17.00G1-177[»]
    3J5Aelectron microscopy12.00G1-177[»]
    3J5Celectron microscopy17.00G1-177[»]
    3J5Eelectron microscopy17.00G1-177[»]
    3J5Gelectron microscopy20.00G1-177[»]
    3J5Ielectron microscopy15.00G1-177[»]
    3J5Kelectron microscopy9.00G1-177[»]
    3J5Lelectron microscopy6.60G2-177[»]
    3J5Oelectron microscopy6.80G1-177[»]
    3J5Uelectron microscopy7.60H2-177[»]
    3J5Welectron microscopy7.60H2-177[»]
    3KCRelectron microscopy-G1-177[»]
    3OASX-ray3.25G2-177[»]
    3OATX-ray3.25G2-177[»]
    3OFCX-ray3.19G2-177[»]
    3OFDX-ray3.19G2-177[»]
    3OFQX-ray3.10G2-177[»]
    3OFRX-ray3.10G2-177[»]
    3OFZX-ray3.29G2-177[»]
    3OG0X-ray3.29G2-177[»]
    3ORBX-ray3.30G1-177[»]
    3R8SX-ray3.00G2-177[»]
    3R8TX-ray3.00G2-177[»]
    3SGFX-ray3.20G1-177[»]
    3UOSX-ray3.70G1-177[»]
    487Delectron microscopy7.50J31-165[»]
    4CSUelectron microscopy5.50G2-177[»]
    4GARX-ray3.30G1-177[»]
    4GAUX-ray3.30G1-177[»]
    4KIXX-ray2.90G1-177[»]
    4KIZX-ray2.90G1-177[»]
    4KJ1X-ray2.90G1-177[»]
    4KJ3X-ray2.90G1-177[»]
    4KJ5X-ray2.90G1-177[»]
    4KJ7X-ray2.90G1-177[»]
    4KJ9X-ray2.90G1-177[»]
    4KJBX-ray2.90G1-177[»]
    ProteinModelPortaliP0AG55.
    SMRiP0AG55. Positions 2-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG55.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L6P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0097.
    HOGENOMiHOG000039903.
    KOiK02933.
    OMAiSHPINYE.
    OrthoDBiEOG67DPRD.
    PhylomeDBiP0AG55.

    Family and domain databases

    Gene3Di3.90.930.12. 2 hits.
    HAMAPiMF_01365_B. Ribosomal_L6_B.
    InterProiIPR000702. Ribosomal_L6.
    IPR020040. Ribosomal_L6_a/b-dom.
    IPR019906. Ribosomal_L6_bac-type.
    IPR002358. Ribosomal_L6_CS.
    [Graphical view]
    PANTHERiPTHR11655. PTHR11655. 1 hit.
    PfamiPF00347. Ribosomal_L6. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
    PRINTSiPR00059. RIBOSOMALL6.
    SUPFAMiSSF56053. SSF56053. 2 hits.
    TIGRFAMsiTIGR03654. L6_bact. 1 hit.
    PROSITEiPS00525. RIBOSOMAL_L6_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0AG55-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRVAKAPVV VPAGVDVKIN GQVITIKGKN GELTRTLNDA VEVKHADNTL    50
    TFGPRDGYAD GWAQAGTARA LLNSMVIGVT EGFTKKLQLV GVGYRAAVKG 100
    NVINLSLGFS HPVDHQLPAG ITAECPTQTE IVLKGADKQV IGQVAADLRA 150
    YRRPEPYKGK GVRYADEVVR TKEAKKK 177
    Length:177
    Mass (Da):18,904
    Last modified:January 23, 2007 - v2
    Checksum:i946B64E9FA42FE61
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821G → D in CAA25720. (PubMed:6222285)Curated
    Sequence conflicti88 – 881Q → E AA sequence (PubMed:324885)Curated

    Mass spectrometryi

    Molecular mass is 18772.7 Da from positions 2 - 177. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti152 – 17726RRPEP…EAKKK → AL in gentamicin resistant strain: GS50-15.
    Add
    BLAST
    Natural varianti158 – 17720KGKGV…EAKKK → TL in gentamicin resistant strain: GS20-8.
    Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25720.1.
    U18997 Genomic DNA. Translation: AAA58102.1.
    U00096 Genomic DNA. Translation: AAC76330.1.
    AP009048 Genomic DNA. Translation: BAE77986.1.
    PIRiD65123. R5EC6.
    RefSeqiNP_417764.1. NC_000913.3.
    YP_492127.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76330; AAC76330; b3305.
    BAE77986; BAE77986; BAE77986.
    GeneIDi12934434.
    947803.
    KEGGiecj:Y75_p3871.
    eco:b3305.
    PATRICi32122042. VBIEscCol129921_3398.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25720.1 .
    U18997 Genomic DNA. Translation: AAA58102.1 .
    U00096 Genomic DNA. Translation: AAC76330.1 .
    AP009048 Genomic DNA. Translation: BAE77986.1 .
    PIRi D65123. R5EC6.
    RefSeqi NP_417764.1. NC_000913.3.
    YP_492127.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EG0 electron microscopy 11.50 J 1-171 [» ]
    1ML5 electron microscopy 14.00 h 2-177 [» ]
    1P85 electron microscopy 12.30 E 2-177 [» ]
    1P86 electron microscopy 11.50 E 2-177 [» ]
    1VS6 X-ray 3.46 G 1-177 [» ]
    1VS8 X-ray 3.46 G 1-177 [» ]
    1VT2 X-ray 3.30 G 1-177 [» ]
    2AW4 X-ray 3.46 G 2-177 [» ]
    2AWB X-ray 3.46 G 2-177 [» ]
    2GYA electron microscopy 15.00 E 6-172 [» ]
    2GYC electron microscopy 15.00 E 6-172 [» ]
    2I2T X-ray 3.22 G 2-177 [» ]
    2I2V X-ray 3.22 G 2-177 [» ]
    2J28 electron microscopy 8.00 G 2-177 [» ]
    2QAM X-ray 3.21 G 2-177 [» ]
    2QAO X-ray 3.21 G 2-177 [» ]
    2QBA X-ray 3.54 G 2-177 [» ]
    2QBC X-ray 3.54 G 2-177 [» ]
    2QBE X-ray 3.30 G 2-177 [» ]
    2QBG X-ray 3.30 G 2-177 [» ]
    2QBI X-ray 4.00 G 2-177 [» ]
    2QBK X-ray 4.00 G 2-177 [» ]
    2QOV X-ray 3.93 G 2-177 [» ]
    2QOX X-ray 3.93 G 2-177 [» ]
    2QOZ X-ray 3.50 G 2-177 [» ]
    2QP1 X-ray 3.50 G 2-177 [» ]
    2RDO electron microscopy 9.10 G 2-177 [» ]
    2VHM X-ray 3.74 G 2-177 [» ]
    2VHN X-ray 3.74 G 2-177 [» ]
    2WWQ electron microscopy 5.80 G 2-177 [» ]
    2Z4L X-ray 4.45 G 2-177 [» ]
    2Z4N X-ray 4.45 G 2-177 [» ]
    3BBX electron microscopy 10.00 G 2-177 [» ]
    3E1B electron microscopy - 3 1-177 [» ]
    3E1D electron microscopy - 3 1-177 [» ]
    3FIK electron microscopy 6.70 G 2-177 [» ]
    3I1N X-ray 3.19 G 1-177 [» ]
    3I1P X-ray 3.19 G 1-177 [» ]
    3I1R X-ray 3.81 G 1-177 [» ]
    3I1T X-ray 3.81 G 1-177 [» ]
    3I20 X-ray 3.71 G 1-177 [» ]
    3I22 X-ray 3.71 G 1-177 [» ]
    3IZT electron microscopy - H 1-177 [» ]
    3IZU electron microscopy - H 1-177 [» ]
    3J01 electron microscopy - G 2-177 [» ]
    3J0T electron microscopy 12.10 H 2-177 [» ]
    3J0W electron microscopy 14.70 H 2-177 [» ]
    3J0Y electron microscopy 13.50 H 2-177 [» ]
    3J11 electron microscopy 13.10 H 2-177 [» ]
    3J12 electron microscopy 11.50 H 2-177 [» ]
    3J14 electron microscopy 11.50 H 2-177 [» ]
    3J19 electron microscopy 8.30 G 2-177 [» ]
    3J37 electron microscopy 9.80 H 2-177 [» ]
    3J4X electron microscopy 12.00 G 1-177 [» ]
    3J50 electron microscopy 20.00 G 1-177 [» ]
    3J51 electron microscopy 17.00 G 1-177 [» ]
    3J52 electron microscopy 12.00 G 1-177 [» ]
    3J54 electron microscopy 13.00 G 1-177 [» ]
    3J56 electron microscopy 15.00 G 1-177 [» ]
    3J58 electron microscopy 17.00 G 1-177 [» ]
    3J5A electron microscopy 12.00 G 1-177 [» ]
    3J5C electron microscopy 17.00 G 1-177 [» ]
    3J5E electron microscopy 17.00 G 1-177 [» ]
    3J5G electron microscopy 20.00 G 1-177 [» ]
    3J5I electron microscopy 15.00 G 1-177 [» ]
    3J5K electron microscopy 9.00 G 1-177 [» ]
    3J5L electron microscopy 6.60 G 2-177 [» ]
    3J5O electron microscopy 6.80 G 1-177 [» ]
    3J5U electron microscopy 7.60 H 2-177 [» ]
    3J5W electron microscopy 7.60 H 2-177 [» ]
    3KCR electron microscopy - G 1-177 [» ]
    3OAS X-ray 3.25 G 2-177 [» ]
    3OAT X-ray 3.25 G 2-177 [» ]
    3OFC X-ray 3.19 G 2-177 [» ]
    3OFD X-ray 3.19 G 2-177 [» ]
    3OFQ X-ray 3.10 G 2-177 [» ]
    3OFR X-ray 3.10 G 2-177 [» ]
    3OFZ X-ray 3.29 G 2-177 [» ]
    3OG0 X-ray 3.29 G 2-177 [» ]
    3ORB X-ray 3.30 G 1-177 [» ]
    3R8S X-ray 3.00 G 2-177 [» ]
    3R8T X-ray 3.00 G 2-177 [» ]
    3SGF X-ray 3.20 G 1-177 [» ]
    3UOS X-ray 3.70 G 1-177 [» ]
    487D electron microscopy 7.50 J 31-165 [» ]
    4CSU electron microscopy 5.50 G 2-177 [» ]
    4GAR X-ray 3.30 G 1-177 [» ]
    4GAU X-ray 3.30 G 1-177 [» ]
    4KIX X-ray 2.90 G 1-177 [» ]
    4KIZ X-ray 2.90 G 1-177 [» ]
    4KJ1 X-ray 2.90 G 1-177 [» ]
    4KJ3 X-ray 2.90 G 1-177 [» ]
    4KJ5 X-ray 2.90 G 1-177 [» ]
    4KJ7 X-ray 2.90 G 1-177 [» ]
    4KJ9 X-ray 2.90 G 1-177 [» ]
    4KJB X-ray 2.90 G 1-177 [» ]
    ProteinModelPortali P0AG55.
    SMRi P0AG55. Positions 2-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852115. 1 interaction.
    DIPi DIP-35860N.
    IntActi P0AG55. 83 interactions.
    MINTi MINT-1244940.
    STRINGi 511145.b3305.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0AG55.
    PRIDEi P0AG55.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76330 ; AAC76330 ; b3305 .
    BAE77986 ; BAE77986 ; BAE77986 .
    GeneIDi 12934434.
    947803.
    KEGGi ecj:Y75_p3871.
    eco:b3305.
    PATRICi 32122042. VBIEscCol129921_3398.

    Organism-specific databases

    EchoBASEi EB0862.
    EcoGenei EG10869. rplF.

    Phylogenomic databases

    eggNOGi COG0097.
    HOGENOMi HOG000039903.
    KOi K02933.
    OMAi SHPINYE.
    OrthoDBi EOG67DPRD.
    PhylomeDBi P0AG55.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10869-MONOMER.
    ECOL316407:JW3267-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AG55.
    PROi P0AG55.

    Gene expression databases

    Genevestigatori P0AG55.

    Family and domain databases

    Gene3Di 3.90.930.12. 2 hits.
    HAMAPi MF_01365_B. Ribosomal_L6_B.
    InterProi IPR000702. Ribosomal_L6.
    IPR020040. Ribosomal_L6_a/b-dom.
    IPR019906. Ribosomal_L6_bac-type.
    IPR002358. Ribosomal_L6_CS.
    [Graphical view ]
    PANTHERi PTHR11655. PTHR11655. 1 hit.
    Pfami PF00347. Ribosomal_L6. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002162. Ribosomal_L6. 1 hit.
    PRINTSi PR00059. RIBOSOMALL6.
    SUPFAMi SSF56053. SSF56053. 2 hits.
    TIGRFAMsi TIGR03654. L6_bact. 1 hit.
    PROSITEi PS00525. RIBOSOMAL_L6_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of protein L6 from the aminoacyl-tRNA binding site of the Escherichia coli ribosome."
      Chen R., Arfsten U., Chen-Schmeisser U.
      Hoppe-Seyler's Z. Physiol. Chem. 358:531-535(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-177.
      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. "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.
    6. "Alteration of ribosomal protein L6 in gentamicin-resistant strains of Escherichia coli. Effects on fidelity of protein synthesis."
      Kuehberger R., Piepersberg W., Petzet A., Buckel P., Boeck A.
      Biochemistry 18:187-193(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOLATION, CHARACTERIZATION OF VARIANTS GENTAMICIN-RESISTANT GE20-8; GS20-10 AND GS50-15.
      Strain: K12 / A19.
    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. "Ribosomal proteins S5 and L6: high-resolution crystal structures and roles in protein synthesis and antibiotic resistance."
      Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V., White S.W.
      J. Mol. Biol. 279:873-888(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF VARIANTS GENTAMICIN-RESISTANT.
    9. "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.
    10. "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.
    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-44, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    12. "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
      Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
      J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    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 nameiRL6_ECOLI
    AccessioniPrimary (citable) accession number: P0AG55
    Secondary accession number(s): P02390, Q2M6X0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 91 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