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P0A7L3

- RL20_ECOLI

UniProt

P0A7L3 - RL20_ECOLI

Protein

50S ribosomal protein L20

Gene

rplT

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

    One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.

    GO - Molecular functioni

    1. rRNA binding Source: UniProtKB-KW
    2. structural constituent of ribosome Source: EcoCyc
    3. translation repressor activity, nucleic acid binding Source: EcoCyc

    GO - Biological processi

    1. negative regulation of translation Source: GOC
    2. ribosomal large subunit assembly Source: EcoCyc
    3. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10881-MONOMER.
    ECOL316407:JW1706-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L20
    Gene namesi
    Name:rplT
    Synonyms:pdzA
    Ordered Locus Names:b1716, JW1706
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10881. rplT.

    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 – 11811750S ribosomal protein L20PRO_0000177156Add
    BLAST

    Proteomic databases

    PaxDbiP0A7L3.
    PRIDEiP0A7L3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7L3.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Contacts L21 (PubMed:2665813).1 Publication

    Protein-protein interaction databases

    DIPiDIP-47941N.
    IntActiP0A7L3. 35 interactions.
    MINTiMINT-1321645.
    STRINGi511145.b1716.

    Structurei

    Secondary structure

    1
    118
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2013
    Turni21 – 233
    Helixi27 – 304
    Helixi32 – 7140
    Beta strandi72 – 743
    Helixi76 – 8510
    Beta strandi86 – 883
    Turni92 – 943
    Helixi95 – 973
    Helixi98 – 1014
    Helixi103 – 11715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P85electron microscopy12.30O2-118[»]
    1P86electron microscopy11.50O2-118[»]
    1VS6X-ray3.46Q1-118[»]
    1VS8X-ray3.46Q1-118[»]
    1VT2X-ray3.30Q1-118[»]
    2AW4X-ray3.46Q2-118[»]
    2AWBX-ray3.46Q2-118[»]
    2GYAelectron microscopy15.00O3-117[»]
    2GYCelectron microscopy15.00O3-117[»]
    2I2TX-ray3.22Q2-118[»]
    2I2VX-ray3.22Q2-118[»]
    2J28electron microscopy8.00Q2-118[»]
    2QAMX-ray3.21Q2-118[»]
    2QAOX-ray3.21Q2-118[»]
    2QBAX-ray3.54Q2-118[»]
    2QBCX-ray3.54Q2-118[»]
    2QBEX-ray3.30Q2-118[»]
    2QBGX-ray3.30Q2-118[»]
    2QBIX-ray4.00Q2-118[»]
    2QBKX-ray4.00Q2-118[»]
    2QOVX-ray3.93Q2-118[»]
    2QOXX-ray3.93Q2-118[»]
    2QOZX-ray3.50Q2-118[»]
    2QP1X-ray3.50Q2-118[»]
    2RDOelectron microscopy9.10Q2-118[»]
    2VHMX-ray3.74Q2-118[»]
    2VHNX-ray3.74Q2-118[»]
    2WWQelectron microscopy5.80Q2-118[»]
    2Z4LX-ray4.45Q2-118[»]
    2Z4NX-ray4.45Q2-118[»]
    3BBXelectron microscopy10.00Q2-118[»]
    3DF2X-ray3.50Q2-117[»]
    3DF4X-ray3.50Q2-117[»]
    3E1Belectron microscopy-J1-118[»]
    3E1Delectron microscopy-J1-118[»]
    3FIKelectron microscopy6.70Q2-118[»]
    3I1NX-ray3.19Q1-118[»]
    3I1PX-ray3.19Q1-118[»]
    3I1RX-ray3.81Q1-118[»]
    3I1TX-ray3.81Q1-118[»]
    3I20X-ray3.71Q1-118[»]
    3I22X-ray3.71Q1-118[»]
    3IZTelectron microscopy-R1-118[»]
    3IZUelectron microscopy-R1-118[»]
    3J01electron microscopy-Q2-118[»]
    3J0Telectron microscopy12.10S2-118[»]
    3J0Welectron microscopy14.70S2-118[»]
    3J0Yelectron microscopy13.50S2-118[»]
    3J11electron microscopy13.10S2-118[»]
    3J12electron microscopy11.50S2-118[»]
    3J14electron microscopy11.50S2-118[»]
    3J19electron microscopy8.30Q2-118[»]
    3J37electron microscopy9.80U2-118[»]
    3J4Xelectron microscopy12.00Q1-118[»]
    3J50electron microscopy20.00Q1-118[»]
    3J51electron microscopy17.00Q1-118[»]
    3J52electron microscopy12.00Q1-118[»]
    3J54electron microscopy13.00Q1-118[»]
    3J56electron microscopy15.00Q1-118[»]
    3J58electron microscopy17.00Q1-118[»]
    3J5Aelectron microscopy12.00Q1-118[»]
    3J5Celectron microscopy17.00Q1-118[»]
    3J5Eelectron microscopy17.00Q1-118[»]
    3J5Gelectron microscopy20.00Q1-118[»]
    3J5Ielectron microscopy15.00Q1-118[»]
    3J5Kelectron microscopy9.00Q1-118[»]
    3J5Lelectron microscopy6.60Q2-118[»]
    3J5Oelectron microscopy6.80Q1-118[»]
    3J5Uelectron microscopy7.60S2-118[»]
    3J5Welectron microscopy7.60T2-118[»]
    3KCRelectron microscopy-Q1-118[»]
    3OASX-ray3.25Q2-118[»]
    3OATX-ray3.25Q2-118[»]
    3OFCX-ray3.19Q2-118[»]
    3OFDX-ray3.19Q2-118[»]
    3OFQX-ray3.10Q2-118[»]
    3OFRX-ray3.10Q2-118[»]
    3OFZX-ray3.29Q2-118[»]
    3OG0X-ray3.29Q2-118[»]
    3ORBX-ray3.30Q1-118[»]
    3R8SX-ray3.00Q2-118[»]
    3R8TX-ray3.00Q2-118[»]
    3SGFX-ray3.20U1-118[»]
    3UOSX-ray3.70U1-118[»]
    4CSUelectron microscopy5.50Q2-118[»]
    4GARX-ray3.30Q1-118[»]
    4GAUX-ray3.30Q1-118[»]
    4KIXX-ray2.90Q1-118[»]
    4KIZX-ray2.90Q1-118[»]
    4KJ1X-ray2.90Q1-118[»]
    4KJ3X-ray2.90Q1-118[»]
    4KJ5X-ray2.90Q1-118[»]
    4KJ7X-ray2.90Q1-118[»]
    4KJ9X-ray2.90Q1-118[»]
    4KJBX-ray2.90Q1-118[»]
    ProteinModelPortaliP0A7L3.
    SMRiP0A7L3. Positions 2-118.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7L3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L20P family.Curated

    Phylogenomic databases

    eggNOGiCOG0292.
    HOGENOMiHOG000035046.
    KOiK02887.
    OMAiFISEPIN.
    OrthoDBiEOG6CGCMB.
    PhylomeDBiP0A7L3.

    Family and domain databases

    HAMAPiMF_00382. Ribosomal_L20.
    InterProiIPR005813. Ribosomal_L20.
    [Graphical view]
    PANTHERiPTHR10986. PTHR10986. 1 hit.
    PfamiPF00453. Ribosomal_L20. 1 hit.
    [Graphical view]
    PRINTSiPR00062. RIBOSOMALL20.
    TIGRFAMsiTIGR01032. rplT_bact. 1 hit.
    PROSITEiPS00937. RIBOSOMAL_L20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7L3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARVKRGVIA RARHKKILKQ AKGYYGARSR VYRVAFQAVI KAGQYAYRDR    50
    RQRKRQFRQL WIARINAAAR QNGISYSKFI NGLKKASVEI DRKILADIAV 100
    FDKVAFTALV EKAKAALA 118
    Length:118
    Mass (Da):13,497
    Last modified:January 23, 2007 - v2
    Checksum:iE60AFDBB6F05DFB3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331R → A in CAA23562. (PubMed:6317865)Curated
    Sequence conflicti33 – 331R → A in AAA51468. (PubMed:6317865)Curated

    Mass spectrometryi

    Molecular mass is 13366.9 Da from positions 2 - 118. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. Translation: CAA23562.1.
    K02844 Genomic DNA. Translation: AAA51468.1.
    U00096 Genomic DNA. Translation: AAC74786.1.
    AP009048 Genomic DNA. Translation: BAA15483.1.
    M10423 Genomic DNA. Translation: AAA23960.1.
    PIRiD64930. R5EC20.
    RefSeqiNP_416231.1. NC_000913.3.
    YP_489978.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74786; AAC74786; b1716.
    BAA15483; BAA15483; BAA15483.
    GeneIDi12931309.
    945152.
    KEGGiecj:Y75_p1691.
    eco:b1716.
    PATRICi32118736. VBIEscCol129921_1786.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. Translation: CAA23562.1 .
    K02844 Genomic DNA. Translation: AAA51468.1 .
    U00096 Genomic DNA. Translation: AAC74786.1 .
    AP009048 Genomic DNA. Translation: BAA15483.1 .
    M10423 Genomic DNA. Translation: AAA23960.1 .
    PIRi D64930. R5EC20.
    RefSeqi NP_416231.1. NC_000913.3.
    YP_489978.1. 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 O 2-118 [» ]
    1P86 electron microscopy 11.50 O 2-118 [» ]
    1VS6 X-ray 3.46 Q 1-118 [» ]
    1VS8 X-ray 3.46 Q 1-118 [» ]
    1VT2 X-ray 3.30 Q 1-118 [» ]
    2AW4 X-ray 3.46 Q 2-118 [» ]
    2AWB X-ray 3.46 Q 2-118 [» ]
    2GYA electron microscopy 15.00 O 3-117 [» ]
    2GYC electron microscopy 15.00 O 3-117 [» ]
    2I2T X-ray 3.22 Q 2-118 [» ]
    2I2V X-ray 3.22 Q 2-118 [» ]
    2J28 electron microscopy 8.00 Q 2-118 [» ]
    2QAM X-ray 3.21 Q 2-118 [» ]
    2QAO X-ray 3.21 Q 2-118 [» ]
    2QBA X-ray 3.54 Q 2-118 [» ]
    2QBC X-ray 3.54 Q 2-118 [» ]
    2QBE X-ray 3.30 Q 2-118 [» ]
    2QBG X-ray 3.30 Q 2-118 [» ]
    2QBI X-ray 4.00 Q 2-118 [» ]
    2QBK X-ray 4.00 Q 2-118 [» ]
    2QOV X-ray 3.93 Q 2-118 [» ]
    2QOX X-ray 3.93 Q 2-118 [» ]
    2QOZ X-ray 3.50 Q 2-118 [» ]
    2QP1 X-ray 3.50 Q 2-118 [» ]
    2RDO electron microscopy 9.10 Q 2-118 [» ]
    2VHM X-ray 3.74 Q 2-118 [» ]
    2VHN X-ray 3.74 Q 2-118 [» ]
    2WWQ electron microscopy 5.80 Q 2-118 [» ]
    2Z4L X-ray 4.45 Q 2-118 [» ]
    2Z4N X-ray 4.45 Q 2-118 [» ]
    3BBX electron microscopy 10.00 Q 2-118 [» ]
    3DF2 X-ray 3.50 Q 2-117 [» ]
    3DF4 X-ray 3.50 Q 2-117 [» ]
    3E1B electron microscopy - J 1-118 [» ]
    3E1D electron microscopy - J 1-118 [» ]
    3FIK electron microscopy 6.70 Q 2-118 [» ]
    3I1N X-ray 3.19 Q 1-118 [» ]
    3I1P X-ray 3.19 Q 1-118 [» ]
    3I1R X-ray 3.81 Q 1-118 [» ]
    3I1T X-ray 3.81 Q 1-118 [» ]
    3I20 X-ray 3.71 Q 1-118 [» ]
    3I22 X-ray 3.71 Q 1-118 [» ]
    3IZT electron microscopy - R 1-118 [» ]
    3IZU electron microscopy - R 1-118 [» ]
    3J01 electron microscopy - Q 2-118 [» ]
    3J0T electron microscopy 12.10 S 2-118 [» ]
    3J0W electron microscopy 14.70 S 2-118 [» ]
    3J0Y electron microscopy 13.50 S 2-118 [» ]
    3J11 electron microscopy 13.10 S 2-118 [» ]
    3J12 electron microscopy 11.50 S 2-118 [» ]
    3J14 electron microscopy 11.50 S 2-118 [» ]
    3J19 electron microscopy 8.30 Q 2-118 [» ]
    3J37 electron microscopy 9.80 U 2-118 [» ]
    3J4X electron microscopy 12.00 Q 1-118 [» ]
    3J50 electron microscopy 20.00 Q 1-118 [» ]
    3J51 electron microscopy 17.00 Q 1-118 [» ]
    3J52 electron microscopy 12.00 Q 1-118 [» ]
    3J54 electron microscopy 13.00 Q 1-118 [» ]
    3J56 electron microscopy 15.00 Q 1-118 [» ]
    3J58 electron microscopy 17.00 Q 1-118 [» ]
    3J5A electron microscopy 12.00 Q 1-118 [» ]
    3J5C electron microscopy 17.00 Q 1-118 [» ]
    3J5E electron microscopy 17.00 Q 1-118 [» ]
    3J5G electron microscopy 20.00 Q 1-118 [» ]
    3J5I electron microscopy 15.00 Q 1-118 [» ]
    3J5K electron microscopy 9.00 Q 1-118 [» ]
    3J5L electron microscopy 6.60 Q 2-118 [» ]
    3J5O electron microscopy 6.80 Q 1-118 [» ]
    3J5U electron microscopy 7.60 S 2-118 [» ]
    3J5W electron microscopy 7.60 T 2-118 [» ]
    3KCR electron microscopy - Q 1-118 [» ]
    3OAS X-ray 3.25 Q 2-118 [» ]
    3OAT X-ray 3.25 Q 2-118 [» ]
    3OFC X-ray 3.19 Q 2-118 [» ]
    3OFD X-ray 3.19 Q 2-118 [» ]
    3OFQ X-ray 3.10 Q 2-118 [» ]
    3OFR X-ray 3.10 Q 2-118 [» ]
    3OFZ X-ray 3.29 Q 2-118 [» ]
    3OG0 X-ray 3.29 Q 2-118 [» ]
    3ORB X-ray 3.30 Q 1-118 [» ]
    3R8S X-ray 3.00 Q 2-118 [» ]
    3R8T X-ray 3.00 Q 2-118 [» ]
    3SGF X-ray 3.20 U 1-118 [» ]
    3UOS X-ray 3.70 U 1-118 [» ]
    4CSU electron microscopy 5.50 Q 2-118 [» ]
    4GAR X-ray 3.30 Q 1-118 [» ]
    4GAU X-ray 3.30 Q 1-118 [» ]
    4KIX X-ray 2.90 Q 1-118 [» ]
    4KIZ X-ray 2.90 Q 1-118 [» ]
    4KJ1 X-ray 2.90 Q 1-118 [» ]
    4KJ3 X-ray 2.90 Q 1-118 [» ]
    4KJ5 X-ray 2.90 Q 1-118 [» ]
    4KJ7 X-ray 2.90 Q 1-118 [» ]
    4KJ9 X-ray 2.90 Q 1-118 [» ]
    4KJB X-ray 2.90 Q 1-118 [» ]
    ProteinModelPortali P0A7L3.
    SMRi P0A7L3. Positions 2-118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47941N.
    IntActi P0A7L3. 35 interactions.
    MINTi MINT-1321645.
    STRINGi 511145.b1716.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7L3.
    PRIDEi P0A7L3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74786 ; AAC74786 ; b1716 .
    BAA15483 ; BAA15483 ; BAA15483 .
    GeneIDi 12931309.
    945152.
    KEGGi ecj:Y75_p1691.
    eco:b1716.
    PATRICi 32118736. VBIEscCol129921_1786.

    Organism-specific databases

    EchoBASEi EB0874.
    EcoGenei EG10881. rplT.

    Phylogenomic databases

    eggNOGi COG0292.
    HOGENOMi HOG000035046.
    KOi K02887.
    OMAi FISEPIN.
    OrthoDBi EOG6CGCMB.
    PhylomeDBi P0A7L3.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10881-MONOMER.
    ECOL316407:JW1706-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7L3.
    PROi P0A7L3.

    Gene expression databases

    Genevestigatori P0A7L3.

    Family and domain databases

    HAMAPi MF_00382. Ribosomal_L20.
    InterProi IPR005813. Ribosomal_L20.
    [Graphical view ]
    PANTHERi PTHR10986. PTHR10986. 1 hit.
    Pfami PF00453. Ribosomal_L20. 1 hit.
    [Graphical view ]
    PRINTSi PR00062. RIBOSOMALL20.
    TIGRFAMsi TIGR01032. rplT_bact. 1 hit.
    PROSITEi PS00937. RIBOSOMAL_L20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20."
      Fayat G., Mayaux J.-F., Sacerdot C., Fromant M., Springer M., Grunberg-Manago M., Blanquet S.
      J. Mol. Biol. 171:239-261(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Primary structure of the himA gene of Escherichia coli: homology with DNA-binding protein HU and association with the phenylalanyl-tRNA synthetase operon."
      Miller H.I.
      Cold Spring Harb. Symp. Quant. Biol. 49:691-698(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "The primary structure of protein L20 from the large subunit of the Escherichia coli ribosome."
      Wittmann-Liebold B., Seib C.
      FEBS Lett. 103:61-65(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-118.
      Strain: K12.
    7. "Attenuation control of the Escherichia coli phenylalanyl-tRNA synthetase operon."
      Springer M., Mayaux J.-F., Fayat G., Plumbridge J.A., Graffe M., Blanquet S., Grunberg-Manago M.
      J. Mol. Biol. 181:467-478(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-118.
    8. "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.
    9. "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 L21.
    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. "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.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL20_ECOLI
    AccessioniPrimary (citable) accession number: P0A7L3
    Secondary accession number(s): P02421, Q47253
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 98 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