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P62399

- RL5_ECOLI

UniProt

P62399 - RL5_ECOLI

Protein

50S ribosomal protein L5

Gene

rplE

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 112 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.
    In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.2 Publications
    Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.

    GO - Molecular functioni

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

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10868-MONOMER.
    ECOL316407:JW3270-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L5
    Gene namesi
    Name:rplE
    Ordered Locus Names:b3308, JW3270
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10868. rplE.

    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 – 17917850S ribosomal protein L5PRO_0000124925Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP62399.
    PRIDEiP62399.

    Expressioni

    Gene expression databases

    GenevestigatoriP62399.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA; cross-links to the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome, contacting protein S13 and S19.

    Protein-protein interaction databases

    BioGridi852112. 1 interaction.
    DIPiDIP-35914N.
    IntActiP62399. 71 interactions.
    MINTiMINT-1238892.
    STRINGi511145.b3308.

    Structurei

    Secondary structure

    1
    179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Turni10 – 123
    Helixi13 – 208
    Helixi25 – 273
    Beta strandi31 – 377
    Helixi42 – 443
    Helixi48 – 6013
    Beta strandi61 – 633
    Beta strandi66 – 694
    Beta strandi71 – 733
    Turni75 – 784
    Beta strandi81 – 833
    Beta strandi84 – 918
    Helixi93 – 10513
    Turni106 – 1105
    Beta strandi111 – 1133
    Beta strandi124 – 1263
    Beta strandi128 – 1336
    Helixi135 – 1373
    Helixi139 – 1413
    Helixi143 – 1453
    Beta strandi153 – 1597
    Helixi163 – 1719
    Turni172 – 1743

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ML5electron microscopy14.00g2-177[»]
    1P85electron microscopy12.30D2-179[»]
    1P86electron microscopy11.50D2-179[»]
    1VS6X-ray3.46F1-179[»]
    1VS8X-ray3.46F1-179[»]
    1VT2X-ray3.30F1-179[»]
    2AW4X-ray3.46F2-179[»]
    2AWBX-ray3.46F2-179[»]
    2GYAelectron microscopy15.00D3-179[»]
    2GYCelectron microscopy15.00D3-179[»]
    2I2TX-ray3.22F2-179[»]
    2I2VX-ray3.22F2-179[»]
    2J28electron microscopy8.00F2-179[»]
    2QAMX-ray3.21F2-179[»]
    2QAOX-ray3.21F2-179[»]
    2QBAX-ray3.54F2-179[»]
    2QBCX-ray3.54F2-179[»]
    2QBEX-ray3.30F2-179[»]
    2QBGX-ray3.30F2-179[»]
    2QBIX-ray4.00F2-179[»]
    2QBKX-ray4.00F2-179[»]
    2QOVX-ray3.93F2-179[»]
    2QOXX-ray3.93F2-179[»]
    2QOZX-ray3.50F2-179[»]
    2QP1X-ray3.50F2-179[»]
    2RDOelectron microscopy9.10F2-179[»]
    2VHMX-ray3.74F2-179[»]
    2VHNX-ray3.74F2-179[»]
    2WWQelectron microscopy5.80F2-179[»]
    2Z4LX-ray4.45F2-179[»]
    2Z4NX-ray4.45F2-179[»]
    3BBXelectron microscopy10.00F2-179[»]
    3DF2X-ray3.50F2-178[»]
    3DF4X-ray3.50F2-178[»]
    3E1Belectron microscopy-22-179[»]
    3E1Delectron microscopy-22-179[»]
    3FIKelectron microscopy6.70F2-179[»]
    3I1NX-ray3.19F1-179[»]
    3I1PX-ray3.19F1-179[»]
    3I1RX-ray3.81F1-179[»]
    3I1TX-ray3.81F1-179[»]
    3I20X-ray3.71F1-179[»]
    3I22X-ray3.71F1-179[»]
    3IZTelectron microscopy-G1-179[»]
    3IZUelectron microscopy-G1-179[»]
    3J01electron microscopy-F2-179[»]
    3J0Telectron microscopy12.10G2-179[»]
    3J0Welectron microscopy14.70G2-179[»]
    3J0Yelectron microscopy13.50G2-179[»]
    3J11electron microscopy13.10G2-179[»]
    3J12electron microscopy11.50G2-179[»]
    3J14electron microscopy11.50G2-179[»]
    3J19electron microscopy8.30F2-178[»]
    3J37electron microscopy9.80G2-179[»]
    3J4Xelectron microscopy12.00F1-179[»]
    3J50electron microscopy20.00F1-179[»]
    3J51electron microscopy17.00F1-179[»]
    3J52electron microscopy12.00F1-179[»]
    3J54electron microscopy13.00F1-179[»]
    3J56electron microscopy15.00F1-179[»]
    3J58electron microscopy17.00F1-179[»]
    3J5Aelectron microscopy12.00F1-179[»]
    3J5Celectron microscopy17.00F1-179[»]
    3J5Eelectron microscopy17.00F1-179[»]
    3J5Gelectron microscopy20.00F1-179[»]
    3J5Ielectron microscopy15.00F1-179[»]
    3J5Kelectron microscopy9.00F1-179[»]
    3J5Lelectron microscopy6.60F2-178[»]
    3J5Oelectron microscopy6.80F1-179[»]
    3J5Selectron microscopy7.50G2-179[»]
    3J5Uelectron microscopy7.60G2-179[»]
    3J5Welectron microscopy7.60G2-179[»]
    3KCRelectron microscopy-F1-179[»]
    3OASX-ray3.25F2-179[»]
    3OATX-ray3.25F2-178[»]
    3OFCX-ray3.19F2-178[»]
    3OFDX-ray3.19F2-179[»]
    3OFQX-ray3.10F2-179[»]
    3OFRX-ray3.10F2-178[»]
    3OFZX-ray3.29F2-178[»]
    3OG0X-ray3.29F2-179[»]
    3ORBX-ray3.30F1-179[»]
    3R8SX-ray3.00F2-178[»]
    3R8TX-ray3.00F2-178[»]
    3SGFX-ray3.20F1-179[»]
    3UOSX-ray3.70F1-179[»]
    4CSUelectron microscopy5.50F2-179[»]
    4GARX-ray3.30F1-179[»]
    4GAUX-ray3.30F1-179[»]
    4KIXX-ray2.90F1-179[»]
    4KIZX-ray2.90F1-179[»]
    4KJ1X-ray2.90F1-179[»]
    4KJ3X-ray2.90F1-179[»]
    4KJ5X-ray2.90F1-179[»]
    4KJ7X-ray2.90F1-179[»]
    4KJ9X-ray2.90F1-179[»]
    4KJBX-ray2.90F1-179[»]
    ProteinModelPortaliP62399.
    SMRiP62399. Positions 2-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62399.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L5P family.Curated

    Phylogenomic databases

    eggNOGiCOG0094.
    HOGENOMiHOG000231311.
    KOiK02931.
    OMAiTEQLIFP.
    OrthoDBiEOG6M9F1R.
    PhylomeDBiP62399.

    Family and domain databases

    Gene3Di3.30.1440.10. 1 hit.
    HAMAPiMF_01333_B. Ribosomal_L5_B.
    InterProiIPR002132. Ribosomal_L5.
    IPR020930. Ribosomal_L5_bac-type.
    IPR020929. Ribosomal_L5_CS.
    IPR022803. Ribosomal_L5_domain.
    [Graphical view]
    PANTHERiPTHR11994. PTHR11994. 1 hit.
    PfamiPF00281. Ribosomal_L5. 1 hit.
    PF00673. Ribosomal_L5_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
    SUPFAMiSSF55282. SSF55282. 1 hit.
    PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62399-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL    50
    DNAAADLAAI SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF 100
    ERLITIAVPR IRDFRGLSAK SFDGRGNYSM GVREQIIFPE IDYDKVDRVR 150
    GLDITITTTA KSDEEGRALL AAFDFPFRK 179
    Length:179
    Mass (Da):20,302
    Last modified:January 23, 2007 - v2
    Checksum:iB2E95A8BE4B8D2A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941E → Q AA sequence (PubMed:791672)Curated
    Sequence conflicti127 – 1271N → D AA sequence (PubMed:791672)Curated

    Mass spectrometryi

    Molecular mass is 20169.8 Da from positions 2 - 179. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25717.1.
    U18997 Genomic DNA. Translation: AAA58105.1.
    U00096 Genomic DNA. Translation: AAC76333.1.
    AP009048 Genomic DNA. Translation: BAE77983.1.
    M10195 Genomic DNA. Translation: AAA24051.1.
    PIRiG65123. R5EC5.
    RefSeqiNP_417767.1. NC_000913.3.
    YP_492124.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76333; AAC76333; b3308.
    BAE77983; BAE77983; BAE77983.
    GeneIDi12934390.
    947800.
    KEGGiecj:Y75_p3868.
    eco:b3308.
    PATRICi32122048. VBIEscCol129921_3401.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25717.1 .
    U18997 Genomic DNA. Translation: AAA58105.1 .
    U00096 Genomic DNA. Translation: AAC76333.1 .
    AP009048 Genomic DNA. Translation: BAE77983.1 .
    M10195 Genomic DNA. Translation: AAA24051.1 .
    PIRi G65123. R5EC5.
    RefSeqi NP_417767.1. NC_000913.3.
    YP_492124.1. 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 g 2-177 [» ]
    1P85 electron microscopy 12.30 D 2-179 [» ]
    1P86 electron microscopy 11.50 D 2-179 [» ]
    1VS6 X-ray 3.46 F 1-179 [» ]
    1VS8 X-ray 3.46 F 1-179 [» ]
    1VT2 X-ray 3.30 F 1-179 [» ]
    2AW4 X-ray 3.46 F 2-179 [» ]
    2AWB X-ray 3.46 F 2-179 [» ]
    2GYA electron microscopy 15.00 D 3-179 [» ]
    2GYC electron microscopy 15.00 D 3-179 [» ]
    2I2T X-ray 3.22 F 2-179 [» ]
    2I2V X-ray 3.22 F 2-179 [» ]
    2J28 electron microscopy 8.00 F 2-179 [» ]
    2QAM X-ray 3.21 F 2-179 [» ]
    2QAO X-ray 3.21 F 2-179 [» ]
    2QBA X-ray 3.54 F 2-179 [» ]
    2QBC X-ray 3.54 F 2-179 [» ]
    2QBE X-ray 3.30 F 2-179 [» ]
    2QBG X-ray 3.30 F 2-179 [» ]
    2QBI X-ray 4.00 F 2-179 [» ]
    2QBK X-ray 4.00 F 2-179 [» ]
    2QOV X-ray 3.93 F 2-179 [» ]
    2QOX X-ray 3.93 F 2-179 [» ]
    2QOZ X-ray 3.50 F 2-179 [» ]
    2QP1 X-ray 3.50 F 2-179 [» ]
    2RDO electron microscopy 9.10 F 2-179 [» ]
    2VHM X-ray 3.74 F 2-179 [» ]
    2VHN X-ray 3.74 F 2-179 [» ]
    2WWQ electron microscopy 5.80 F 2-179 [» ]
    2Z4L X-ray 4.45 F 2-179 [» ]
    2Z4N X-ray 4.45 F 2-179 [» ]
    3BBX electron microscopy 10.00 F 2-179 [» ]
    3DF2 X-ray 3.50 F 2-178 [» ]
    3DF4 X-ray 3.50 F 2-178 [» ]
    3E1B electron microscopy - 2 2-179 [» ]
    3E1D electron microscopy - 2 2-179 [» ]
    3FIK electron microscopy 6.70 F 2-179 [» ]
    3I1N X-ray 3.19 F 1-179 [» ]
    3I1P X-ray 3.19 F 1-179 [» ]
    3I1R X-ray 3.81 F 1-179 [» ]
    3I1T X-ray 3.81 F 1-179 [» ]
    3I20 X-ray 3.71 F 1-179 [» ]
    3I22 X-ray 3.71 F 1-179 [» ]
    3IZT electron microscopy - G 1-179 [» ]
    3IZU electron microscopy - G 1-179 [» ]
    3J01 electron microscopy - F 2-179 [» ]
    3J0T electron microscopy 12.10 G 2-179 [» ]
    3J0W electron microscopy 14.70 G 2-179 [» ]
    3J0Y electron microscopy 13.50 G 2-179 [» ]
    3J11 electron microscopy 13.10 G 2-179 [» ]
    3J12 electron microscopy 11.50 G 2-179 [» ]
    3J14 electron microscopy 11.50 G 2-179 [» ]
    3J19 electron microscopy 8.30 F 2-178 [» ]
    3J37 electron microscopy 9.80 G 2-179 [» ]
    3J4X electron microscopy 12.00 F 1-179 [» ]
    3J50 electron microscopy 20.00 F 1-179 [» ]
    3J51 electron microscopy 17.00 F 1-179 [» ]
    3J52 electron microscopy 12.00 F 1-179 [» ]
    3J54 electron microscopy 13.00 F 1-179 [» ]
    3J56 electron microscopy 15.00 F 1-179 [» ]
    3J58 electron microscopy 17.00 F 1-179 [» ]
    3J5A electron microscopy 12.00 F 1-179 [» ]
    3J5C electron microscopy 17.00 F 1-179 [» ]
    3J5E electron microscopy 17.00 F 1-179 [» ]
    3J5G electron microscopy 20.00 F 1-179 [» ]
    3J5I electron microscopy 15.00 F 1-179 [» ]
    3J5K electron microscopy 9.00 F 1-179 [» ]
    3J5L electron microscopy 6.60 F 2-178 [» ]
    3J5O electron microscopy 6.80 F 1-179 [» ]
    3J5S electron microscopy 7.50 G 2-179 [» ]
    3J5U electron microscopy 7.60 G 2-179 [» ]
    3J5W electron microscopy 7.60 G 2-179 [» ]
    3KCR electron microscopy - F 1-179 [» ]
    3OAS X-ray 3.25 F 2-179 [» ]
    3OAT X-ray 3.25 F 2-178 [» ]
    3OFC X-ray 3.19 F 2-178 [» ]
    3OFD X-ray 3.19 F 2-179 [» ]
    3OFQ X-ray 3.10 F 2-179 [» ]
    3OFR X-ray 3.10 F 2-178 [» ]
    3OFZ X-ray 3.29 F 2-178 [» ]
    3OG0 X-ray 3.29 F 2-179 [» ]
    3ORB X-ray 3.30 F 1-179 [» ]
    3R8S X-ray 3.00 F 2-178 [» ]
    3R8T X-ray 3.00 F 2-178 [» ]
    3SGF X-ray 3.20 F 1-179 [» ]
    3UOS X-ray 3.70 F 1-179 [» ]
    4CSU electron microscopy 5.50 F 2-179 [» ]
    4GAR X-ray 3.30 F 1-179 [» ]
    4GAU X-ray 3.30 F 1-179 [» ]
    4KIX X-ray 2.90 F 1-179 [» ]
    4KIZ X-ray 2.90 F 1-179 [» ]
    4KJ1 X-ray 2.90 F 1-179 [» ]
    4KJ3 X-ray 2.90 F 1-179 [» ]
    4KJ5 X-ray 2.90 F 1-179 [» ]
    4KJ7 X-ray 2.90 F 1-179 [» ]
    4KJ9 X-ray 2.90 F 1-179 [» ]
    4KJB X-ray 2.90 F 1-179 [» ]
    ProteinModelPortali P62399.
    SMRi P62399. Positions 2-178.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852112. 1 interaction.
    DIPi DIP-35914N.
    IntActi P62399. 71 interactions.
    MINTi MINT-1238892.
    STRINGi 511145.b3308.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P62399.
    PRIDEi P62399.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76333 ; AAC76333 ; b3308 .
    BAE77983 ; BAE77983 ; BAE77983 .
    GeneIDi 12934390.
    947800.
    KEGGi ecj:Y75_p3868.
    eco:b3308.
    PATRICi 32122048. VBIEscCol129921_3401.

    Organism-specific databases

    EchoBASEi EB0861.
    EcoGenei EG10868. rplE.

    Phylogenomic databases

    eggNOGi COG0094.
    HOGENOMi HOG000231311.
    KOi K02931.
    OMAi TEQLIFP.
    OrthoDBi EOG6M9F1R.
    PhylomeDBi P62399.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10868-MONOMER.
    ECOL316407:JW3270-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P62399.
    PROi P62399.

    Gene expression databases

    Genevestigatori P62399.

    Family and domain databases

    Gene3Di 3.30.1440.10. 1 hit.
    HAMAPi MF_01333_B. Ribosomal_L5_B.
    InterProi IPR002132. Ribosomal_L5.
    IPR020930. Ribosomal_L5_bac-type.
    IPR020929. Ribosomal_L5_CS.
    IPR022803. Ribosomal_L5_domain.
    [Graphical view ]
    PANTHERi PTHR11994. PTHR11994. 1 hit.
    Pfami PF00281. Ribosomal_L5. 1 hit.
    PF00673. Ribosomal_L5_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002161. Ribosomal_L5. 1 hit.
    SUPFAMi SSF55282. SSF55282. 1 hit.
    PROSITEi PS00358. RIBOSOMAL_L5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "The primary structure of the 5 S RNA binding protein L5 of Escherichia coli ribosomes."
      Chen R., Ehrke G.
      FEBS Lett. 69:240-245(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-179.
      Strain: K.
    5. "Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA."
      Olins P.O., Nomura M.
      Nucleic Acids Res. 9:1757-1764(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
      Strain: K12 / JM105 / ATCC 47016.
    6. "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.
      Strain: MRE-600.
    7. "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.
    8. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
      Osswald M., Doering T., Brimacombe R.
      Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
      Strain: MRE-600.
    9. "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.
    10. "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.
    11. "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.
    12. "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-3, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    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), INTERSUBUNIT BRIDGE FORMATION.
      Strain: MRE-600.
    14. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON TRANSLOCATION.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING 2 CONFORMATIONS OF INTERSUBUNIT BRIDGE B1B.

    Entry informationi

    Entry nameiRL5_ECOLI
    AccessioniPrimary (citable) accession number: P62399
    Secondary accession number(s): P02389, Q2M6X3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 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