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P0A7J7

- RL11_ECOLI

UniProt

P0A7J7 - RL11_ECOLI

Protein

50S ribosomal protein L11

Gene

rplK

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

    Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.

    GO - Molecular functioni

    1. large ribosomal subunit rRNA binding Source: UniProtKB-HAMAP
    2. protein binding Source: IntAct
    3. rRNA binding Source: EcoCyc
    4. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. stringent response Source: EcoCyc
    2. translational termination Source: EcoCyc

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10872-MONOMER.
    ECOL316407:JW3946-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L11UniRule annotation
    Gene namesi
    Name:rplKUniRule annotation
    Synonyms:relC
    Ordered Locus Names:b3983, JW3946
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10872. rplK.

    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 – 14214150S ribosomal protein L11PRO_0000104283Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N,N,N-trimethylalanine
    Modified residuei4 – 41N6,N6,N6-trimethyllysine
    Modified residuei40 – 401N6,N6,N6-trimethyllysine
    Modified residuei72 – 721N6-succinyllysine1 Publication
    Modified residuei81 – 811N6-succinyllysine1 Publication

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP0A7J7.
    PRIDEiP0A7J7.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7J7.

    Interactioni

    Subunit structurei

    Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    prmAP0A8T13EBI-547288,EBI-556300

    Protein-protein interaction databases

    BioGridi852778. 1 interaction.
    DIPiDIP-35882N.
    IntActiP0A7J7. 46 interactions.
    MINTiMINT-1232893.
    STRINGi511145.b3983.

    Structurei

    Secondary structure

    1
    142
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Beta strandi9 – 135
    Beta strandi15 – 195
    Beta strandi21 – 244
    Helixi25 – 284
    Beta strandi29 – 324
    Helixi35 – 373
    Turni38 – 403
    Helixi42 – 443
    Turni45 – 495
    Beta strandi51 – 533
    Beta strandi55 – 617
    Beta strandi62 – 665
    Beta strandi67 – 715
    Turni76 – 849
    Beta strandi87 – 893
    Beta strandi94 – 963
    Beta strandi100 – 1045
    Turni105 – 1073
    Helixi108 – 1114
    Helixi112 – 1165
    Beta strandi120 – 1223
    Helixi124 – 1329
    Beta strandi134 – 1363
    Beta strandi139 – 1413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG0electron microscopy11.50K1-140[»]
    1MJ1electron microscopy13.00L1-141[»]
    1ML5electron microscopy14.00l1-141[»]
    1P85electron microscopy12.30G2-142[»]
    1P86electron microscopy11.50G2-142[»]
    1VS6X-ray3.46I1-142[»]
    1VS8X-ray3.46I1-142[»]
    1VT2X-ray3.30I1-142[»]
    2AW4X-ray3.46I2-142[»]
    2AWBX-ray3.46I2-142[»]
    2GYAelectron microscopy15.00G3-141[»]
    2GYCelectron microscopy15.00G3-141[»]
    2I2TX-ray3.22I2-142[»]
    2I2VX-ray3.22I2-142[»]
    2J28electron microscopy8.00I2-142[»]
    2QAMX-ray3.21I2-142[»]
    2QAOX-ray3.21I2-142[»]
    2QBAX-ray3.54I2-142[»]
    2QBCX-ray3.54I2-142[»]
    2QBEX-ray3.30I2-142[»]
    2QBGX-ray3.30I2-142[»]
    2QBIX-ray4.00I2-142[»]
    2QBKX-ray4.00I2-142[»]
    2QOVX-ray3.93I2-142[»]
    2QOXX-ray3.93I2-142[»]
    2QOZX-ray3.50I2-142[»]
    2QP1X-ray3.50I2-142[»]
    2RDOelectron microscopy9.10I2-142[»]
    2VHMX-ray3.74I2-142[»]
    2VHNX-ray3.74I2-142[»]
    2WWQelectron microscopy5.80I2-142[»]
    2Z4LX-ray4.45I2-142[»]
    2Z4NX-ray4.45I2-142[»]
    3DEGelectron microscopy-H2-142[»]
    3DF2X-ray3.50I2-141[»]
    3DF4X-ray3.50I2-141[»]
    3E1Belectron microscopy-51-142[»]
    3E1Delectron microscopy-51-142[»]
    3EP2electron microscopy-I2-142[»]
    3EQ3electron microscopy-I2-142[»]
    3EQ4electron microscopy-I2-142[»]
    3FIKelectron microscopy6.70I2-142[»]
    3I1NX-ray3.19I1-142[»]
    3I1PX-ray3.19I1-142[»]
    3I1RX-ray3.81I1-142[»]
    3I1TX-ray3.81I1-142[»]
    3I20X-ray3.71I1-142[»]
    3I22X-ray3.71I1-142[»]
    3IZTelectron microscopy-J1-142[»]
    3IZUelectron microscopy-J1-142[»]
    3J01electron microscopy-I2-142[»]
    3J0Delectron microscopy11.10G2-142[»]
    3J0Telectron microscopy12.10K2-142[»]
    3J0Welectron microscopy14.70K2-142[»]
    3J0Yelectron microscopy13.50K2-142[»]
    3J11electron microscopy13.10K2-142[»]
    3J12electron microscopy11.50K2-142[»]
    3J14electron microscopy11.50K2-142[»]
    3J19electron microscopy8.30I2-142[»]
    3J37electron microscopy9.80K2-142[»]
    3J4Xelectron microscopy12.00I1-142[»]
    3J50electron microscopy20.00I1-142[»]
    3J51electron microscopy17.00I1-142[»]
    3J52electron microscopy12.00I1-142[»]
    3J54electron microscopy13.00I1-142[»]
    3J56electron microscopy15.00I1-142[»]
    3J58electron microscopy17.00I1-142[»]
    3J5Aelectron microscopy12.00I1-142[»]
    3J5Celectron microscopy17.00I1-142[»]
    3J5Eelectron microscopy17.00I1-142[»]
    3J5Gelectron microscopy20.00I1-142[»]
    3J5Ielectron microscopy15.00I1-142[»]
    3J5Kelectron microscopy9.00I1-142[»]
    3J5Lelectron microscopy6.60I2-142[»]
    3J5Oelectron microscopy6.80I1-142[»]
    3J5Uelectron microscopy7.60K2-142[»]
    3J5Welectron microscopy7.60K2-142[»]
    3KCRelectron microscopy-I1-142[»]
    3OASX-ray3.25I2-142[»]
    3OATX-ray3.25I2-142[»]
    3OFCX-ray3.19I2-142[»]
    3OFDX-ray3.19I2-142[»]
    3OFQX-ray3.10I2-142[»]
    3OFRX-ray3.10I2-142[»]
    3OFZX-ray3.29I2-142[»]
    3OG0X-ray3.29I2-142[»]
    3ORBX-ray3.30I1-142[»]
    3R8SX-ray3.00I2-142[»]
    3R8TX-ray3.00I2-142[»]
    3SGFX-ray3.20I1-142[»]
    3UOSX-ray3.70I1-142[»]
    487Delectron microscopy7.50L10-86[»]
    4CSUelectron microscopy5.50I2-142[»]
    4GARX-ray3.30I1-142[»]
    4GAUX-ray3.30I1-142[»]
    4KIXX-ray2.90I1-142[»]
    4KIZX-ray2.90I1-142[»]
    4KJ1X-ray2.90I1-142[»]
    4KJ3X-ray2.90I1-142[»]
    4KJ5X-ray2.90I1-142[»]
    4KJ7X-ray2.90I1-142[»]
    4KJ9X-ray2.90I1-142[»]
    4KJBX-ray2.90I1-142[»]
    ProteinModelPortaliP0A7J7.
    SMRiP0A7J7. Positions 3-141.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7J7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L11P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0080.
    HOGENOMiHOG000082123.
    KOiK02867.
    OMAiIEAYIKL.
    OrthoDBiEOG69PQ9D.
    PhylomeDBiP0A7J7.

    Family and domain databases

    Gene3Di1.10.10.250. 1 hit.
    3.30.1550.10. 1 hit.
    HAMAPiMF_00736. Ribosomal_L11.
    InterProiIPR000911. Ribosomal_L11/L12.
    IPR006519. Ribosomal_L11_bac-typ.
    IPR020783. Ribosomal_L11_C.
    IPR020785. Ribosomal_L11_CS.
    IPR020784. Ribosomal_L11_N.
    [Graphical view]
    PANTHERiPTHR11661. PTHR11661. 1 hit.
    PfamiPF00298. Ribosomal_L11. 1 hit.
    PF03946. Ribosomal_L11_N. 1 hit.
    [Graphical view]
    SMARTiSM00649. RL11. 1 hit.
    [Graphical view]
    SUPFAMiSSF46906. SSF46906. 1 hit.
    SSF54747. SSF54747. 1 hit.
    TIGRFAMsiTIGR01632. L11_bact. 1 hit.
    PROSITEiPS00359. RIBOSOMAL_L11. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7J7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE    50
    KGLPIPVVIT VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK 100
    ISRAQLQEIA QTKAADMTGA DIEAMTRSIE GTARSMGLVV ED 142
    Length:142
    Mass (Da):14,875
    Last modified:January 23, 2007 - v2
    Checksum:iC49226BB2462BE0F
    GO

    Mass spectrometryi

    Molecular mass is 14870.2 Da from positions 2 - 142. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23621.1. Sequence problems.
    M30610 Genomic DNA. Translation: AAA24623.1.
    U00006 Genomic DNA. Translation: AAC43081.1.
    U00096 Genomic DNA. Translation: AAC76957.1.
    AP009048 Genomic DNA. Translation: BAE77337.1.
    PIRiS12572. R5EC11.
    RefSeqiNP_418410.1. NC_000913.3.
    YP_491478.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76957; AAC76957; b3983.
    BAE77337; BAE77337; BAE77337.
    GeneIDi12930523.
    948484.
    KEGGiecj:Y75_p3214.
    eco:b3983.
    PATRICi32123487. VBIEscCol129921_4096.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23621.1 . Sequence problems.
    M30610 Genomic DNA. Translation: AAA24623.1 .
    U00006 Genomic DNA. Translation: AAC43081.1 .
    U00096 Genomic DNA. Translation: AAC76957.1 .
    AP009048 Genomic DNA. Translation: BAE77337.1 .
    PIRi S12572. R5EC11.
    RefSeqi NP_418410.1. NC_000913.3.
    YP_491478.1. 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 K 1-140 [» ]
    1MJ1 electron microscopy 13.00 L 1-141 [» ]
    1ML5 electron microscopy 14.00 l 1-141 [» ]
    1P85 electron microscopy 12.30 G 2-142 [» ]
    1P86 electron microscopy 11.50 G 2-142 [» ]
    1VS6 X-ray 3.46 I 1-142 [» ]
    1VS8 X-ray 3.46 I 1-142 [» ]
    1VT2 X-ray 3.30 I 1-142 [» ]
    2AW4 X-ray 3.46 I 2-142 [» ]
    2AWB X-ray 3.46 I 2-142 [» ]
    2GYA electron microscopy 15.00 G 3-141 [» ]
    2GYC electron microscopy 15.00 G 3-141 [» ]
    2I2T X-ray 3.22 I 2-142 [» ]
    2I2V X-ray 3.22 I 2-142 [» ]
    2J28 electron microscopy 8.00 I 2-142 [» ]
    2QAM X-ray 3.21 I 2-142 [» ]
    2QAO X-ray 3.21 I 2-142 [» ]
    2QBA X-ray 3.54 I 2-142 [» ]
    2QBC X-ray 3.54 I 2-142 [» ]
    2QBE X-ray 3.30 I 2-142 [» ]
    2QBG X-ray 3.30 I 2-142 [» ]
    2QBI X-ray 4.00 I 2-142 [» ]
    2QBK X-ray 4.00 I 2-142 [» ]
    2QOV X-ray 3.93 I 2-142 [» ]
    2QOX X-ray 3.93 I 2-142 [» ]
    2QOZ X-ray 3.50 I 2-142 [» ]
    2QP1 X-ray 3.50 I 2-142 [» ]
    2RDO electron microscopy 9.10 I 2-142 [» ]
    2VHM X-ray 3.74 I 2-142 [» ]
    2VHN X-ray 3.74 I 2-142 [» ]
    2WWQ electron microscopy 5.80 I 2-142 [» ]
    2Z4L X-ray 4.45 I 2-142 [» ]
    2Z4N X-ray 4.45 I 2-142 [» ]
    3DEG electron microscopy - H 2-142 [» ]
    3DF2 X-ray 3.50 I 2-141 [» ]
    3DF4 X-ray 3.50 I 2-141 [» ]
    3E1B electron microscopy - 5 1-142 [» ]
    3E1D electron microscopy - 5 1-142 [» ]
    3EP2 electron microscopy - I 2-142 [» ]
    3EQ3 electron microscopy - I 2-142 [» ]
    3EQ4 electron microscopy - I 2-142 [» ]
    3FIK electron microscopy 6.70 I 2-142 [» ]
    3I1N X-ray 3.19 I 1-142 [» ]
    3I1P X-ray 3.19 I 1-142 [» ]
    3I1R X-ray 3.81 I 1-142 [» ]
    3I1T X-ray 3.81 I 1-142 [» ]
    3I20 X-ray 3.71 I 1-142 [» ]
    3I22 X-ray 3.71 I 1-142 [» ]
    3IZT electron microscopy - J 1-142 [» ]
    3IZU electron microscopy - J 1-142 [» ]
    3J01 electron microscopy - I 2-142 [» ]
    3J0D electron microscopy 11.10 G 2-142 [» ]
    3J0T electron microscopy 12.10 K 2-142 [» ]
    3J0W electron microscopy 14.70 K 2-142 [» ]
    3J0Y electron microscopy 13.50 K 2-142 [» ]
    3J11 electron microscopy 13.10 K 2-142 [» ]
    3J12 electron microscopy 11.50 K 2-142 [» ]
    3J14 electron microscopy 11.50 K 2-142 [» ]
    3J19 electron microscopy 8.30 I 2-142 [» ]
    3J37 electron microscopy 9.80 K 2-142 [» ]
    3J4X electron microscopy 12.00 I 1-142 [» ]
    3J50 electron microscopy 20.00 I 1-142 [» ]
    3J51 electron microscopy 17.00 I 1-142 [» ]
    3J52 electron microscopy 12.00 I 1-142 [» ]
    3J54 electron microscopy 13.00 I 1-142 [» ]
    3J56 electron microscopy 15.00 I 1-142 [» ]
    3J58 electron microscopy 17.00 I 1-142 [» ]
    3J5A electron microscopy 12.00 I 1-142 [» ]
    3J5C electron microscopy 17.00 I 1-142 [» ]
    3J5E electron microscopy 17.00 I 1-142 [» ]
    3J5G electron microscopy 20.00 I 1-142 [» ]
    3J5I electron microscopy 15.00 I 1-142 [» ]
    3J5K electron microscopy 9.00 I 1-142 [» ]
    3J5L electron microscopy 6.60 I 2-142 [» ]
    3J5O electron microscopy 6.80 I 1-142 [» ]
    3J5U electron microscopy 7.60 K 2-142 [» ]
    3J5W electron microscopy 7.60 K 2-142 [» ]
    3KCR electron microscopy - I 1-142 [» ]
    3OAS X-ray 3.25 I 2-142 [» ]
    3OAT X-ray 3.25 I 2-142 [» ]
    3OFC X-ray 3.19 I 2-142 [» ]
    3OFD X-ray 3.19 I 2-142 [» ]
    3OFQ X-ray 3.10 I 2-142 [» ]
    3OFR X-ray 3.10 I 2-142 [» ]
    3OFZ X-ray 3.29 I 2-142 [» ]
    3OG0 X-ray 3.29 I 2-142 [» ]
    3ORB X-ray 3.30 I 1-142 [» ]
    3R8S X-ray 3.00 I 2-142 [» ]
    3R8T X-ray 3.00 I 2-142 [» ]
    3SGF X-ray 3.20 I 1-142 [» ]
    3UOS X-ray 3.70 I 1-142 [» ]
    487D electron microscopy 7.50 L 10-86 [» ]
    4CSU electron microscopy 5.50 I 2-142 [» ]
    4GAR X-ray 3.30 I 1-142 [» ]
    4GAU X-ray 3.30 I 1-142 [» ]
    4KIX X-ray 2.90 I 1-142 [» ]
    4KIZ X-ray 2.90 I 1-142 [» ]
    4KJ1 X-ray 2.90 I 1-142 [» ]
    4KJ3 X-ray 2.90 I 1-142 [» ]
    4KJ5 X-ray 2.90 I 1-142 [» ]
    4KJ7 X-ray 2.90 I 1-142 [» ]
    4KJ9 X-ray 2.90 I 1-142 [» ]
    4KJB X-ray 2.90 I 1-142 [» ]
    ProteinModelPortali P0A7J7.
    SMRi P0A7J7. Positions 3-141.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852778. 1 interaction.
    DIPi DIP-35882N.
    IntActi P0A7J7. 46 interactions.
    MINTi MINT-1232893.
    STRINGi 511145.b3983.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7J7.
    PRIDEi P0A7J7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76957 ; AAC76957 ; b3983 .
    BAE77337 ; BAE77337 ; BAE77337 .
    GeneIDi 12930523.
    948484.
    KEGGi ecj:Y75_p3214.
    eco:b3983.
    PATRICi 32123487. VBIEscCol129921_4096.

    Organism-specific databases

    EchoBASEi EB0865.
    EcoGenei EG10872. rplK.

    Phylogenomic databases

    eggNOGi COG0080.
    HOGENOMi HOG000082123.
    KOi K02867.
    OMAi IEAYIKL.
    OrthoDBi EOG69PQ9D.
    PhylomeDBi P0A7J7.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10872-MONOMER.
    ECOL316407:JW3946-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7J7.
    PROi P0A7J7.

    Gene expression databases

    Genevestigatori P0A7J7.

    Family and domain databases

    Gene3Di 1.10.10.250. 1 hit.
    3.30.1550.10. 1 hit.
    HAMAPi MF_00736. Ribosomal_L11.
    InterProi IPR000911. Ribosomal_L11/L12.
    IPR006519. Ribosomal_L11_bac-typ.
    IPR020783. Ribosomal_L11_C.
    IPR020785. Ribosomal_L11_CS.
    IPR020784. Ribosomal_L11_N.
    [Graphical view ]
    PANTHERi PTHR11661. PTHR11661. 1 hit.
    Pfami PF00298. Ribosomal_L11. 1 hit.
    PF03946. Ribosomal_L11_N. 1 hit.
    [Graphical view ]
    SMARTi SM00649. RL11. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46906. SSF46906. 1 hit.
    SSF54747. SSF54747. 1 hit.
    TIGRFAMsi TIGR01632. L11_bact. 1 hit.
    PROSITEi PS00359. RIBOSOMAL_L11. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
      Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
      Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes."
      Dognin M.J., Wittmann-Liebold B.
      Eur. J. Biochem. 112:131-151(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-142.
      Strain: K12.
    6. "Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon."
      Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.
      J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
    7. "Structural properties of ribosomal protein L11 from Escherichia coli."
      Choli T.
      Biochem. Int. 19:1323-1338(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURAL STUDIES.
    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. "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.
    10. "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.
    11. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-72 AND LYS-81.
      Strain: K12.
    12. "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.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL11_ECOLI
    AccessioniPrimary (citable) accession number: P0A7J7
    Secondary accession number(s): P02409, P76778, Q2M8R9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 99 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