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P0A7R9

- RS11_ECOLI

UniProt

P0A7R9 - RS11_ECOLI

Protein

30S ribosomal protein S11

Gene

rpsK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome By similarity.By similarity

    GO - Molecular functioni

    1. small ribosomal subunit rRNA binding Source: EcoliWiki
    2. structural constituent of ribosome Source: EcoliWiki

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10910-MONOMER.
    ECOL316407:JW3259-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S11
    Gene namesi
    Name:rpsK
    Ordered Locus Names:b3297, JW3259
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10910. rpsK.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 12912830S ribosomal protein S11PRO_0000123144Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-methylalanine

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP0A7R9.
    PRIDEiP0A7R9.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7R9.

    Interactioni

    Subunit structurei

    Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18 By similarity. Cross-links to IF-3.By similarity

    Protein-protein interaction databases

    BioGridi852104. 1 interaction.
    DIPiDIP-47838N.
    IntActiP0A7R9. 14 interactions.
    MINTiMINT-1232137.
    STRINGi511145.b3297.

    Structurei

    Secondary structure

    1
    129
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 259
    Beta strandi27 – 293
    Beta strandi30 – 367
    Turni37 – 393
    Beta strandi43 – 475
    Helixi48 – 503
    Beta strandi54 – 563
    Beta strandi57 – 593
    Helixi60 – 7112
    Turni72 – 743
    Helixi75 – 773
    Beta strandi79 – 9012
    Helixi93 – 1019
    Turni102 – 1043
    Beta strandi106 – 1127

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M5Gmodel-K13-129[»]
    1P6Gelectron microscopy12.30K2-129[»]
    1P87electron microscopy11.50K2-129[»]
    1VS5X-ray3.46K1-129[»]
    1VS7X-ray3.46K1-129[»]
    2AVYX-ray3.46K2-129[»]
    2AW7X-ray3.46K2-129[»]
    2GY9electron microscopy15.00K13-128[»]
    2GYBelectron microscopy15.00K13-128[»]
    2I2PX-ray3.22K2-129[»]
    2I2UX-ray3.22K2-129[»]
    2QALX-ray3.21K2-129[»]
    2QANX-ray3.21K2-129[»]
    2QB9X-ray3.54K2-129[»]
    2QBBX-ray3.54K2-129[»]
    2QBDX-ray3.30K2-129[»]
    2QBFX-ray3.30K2-129[»]
    2QBHX-ray4.00K2-129[»]
    2QBJX-ray4.00K2-129[»]
    2QOUX-ray3.93K2-129[»]
    2QOWX-ray3.93K2-129[»]
    2QOYX-ray3.50K2-129[»]
    2QP0X-ray3.50K2-129[»]
    2VHOX-ray3.74K2-129[»]
    2VHPX-ray3.74K2-129[»]
    2WWLelectron microscopy5.80K13-129[»]
    2YKRelectron microscopy9.80K13-129[»]
    2Z4KX-ray4.45K2-129[»]
    2Z4MX-ray4.45K2-129[»]
    3DF1X-ray3.50K2-128[»]
    3DF3X-ray3.50K2-129[»]
    3E1Aelectron microscopy-C1-129[»]
    3E1Celectron microscopy-C1-129[»]
    3FIHelectron microscopy6.70K13-129[»]
    3I1MX-ray3.19K1-129[»]
    3I1OX-ray3.19K1-129[»]
    3I1QX-ray3.81K1-129[»]
    3I1SX-ray3.81K1-129[»]
    3I1ZX-ray3.71K1-129[»]
    3I21X-ray3.71K1-129[»]
    3IZVelectron microscopy-O1-129[»]
    3IZWelectron microscopy-O1-129[»]
    3J00electron microscopy-K2-129[»]
    3J0Uelectron microscopy12.10N2-129[»]
    3J0Velectron microscopy14.70N2-129[»]
    3J0Xelectron microscopy13.50N2-129[»]
    3J0Zelectron microscopy11.50N2-129[»]
    3J10electron microscopy11.50N2-129[»]
    3J13electron microscopy13.10M2-129[»]
    3J18electron microscopy8.30K13-129[»]
    3J36electron microscopy9.80K2-129[»]
    3J4Velectron microscopy12.00K13-129[»]
    3J4Welectron microscopy12.00K13-129[»]
    3J4Yelectron microscopy17.00K13-129[»]
    3J4Zelectron microscopy20.00K13-129[»]
    3J53electron microscopy13.00K13-129[»]
    3J55electron microscopy15.00K13-129[»]
    3J57electron microscopy17.00K13-129[»]
    3J59electron microscopy12.00K13-129[»]
    3J5Belectron microscopy17.00K13-129[»]
    3J5Delectron microscopy17.00K13-129[»]
    3J5Felectron microscopy20.00K13-129[»]
    3J5Helectron microscopy15.00K13-129[»]
    3J5Jelectron microscopy9.00K13-129[»]
    3J5Nelectron microscopy6.80K1-129[»]
    3J5Telectron microscopy7.60K2-129[»]
    3J5Xelectron microscopy7.60K2-129[»]
    3KC4electron microscopy-K1-129[»]
    3OAQX-ray3.25K13-129[»]
    3OARX-ray3.25K13-129[»]
    3OFAX-ray3.19K13-129[»]
    3OFBX-ray3.19K13-129[»]
    3OFOX-ray3.10K13-129[»]
    3OFPX-ray3.10K13-129[»]
    3OFXX-ray3.29K13-129[»]
    3OFYX-ray3.29K13-129[»]
    3OR9X-ray3.30K1-129[»]
    3ORAX-ray3.30K1-129[»]
    3SFSX-ray3.20K1-129[»]
    3UOQX-ray3.70K1-129[»]
    4A2Ielectron microscopy16.50K13-129[»]
    4ADVelectron microscopy13.50K2-129[»]
    4GAQX-ray3.30K1-129[»]
    4GASX-ray3.30K1-129[»]
    4GD1X-ray3.00K13-129[»]
    4GD2X-ray3.00K13-129[»]
    4KIYX-ray2.90K1-129[»]
    4KJ0X-ray2.90K1-129[»]
    4KJ2X-ray2.90K1-129[»]
    4KJ4X-ray2.90K1-129[»]
    4KJ6X-ray2.90K1-129[»]
    4KJ8X-ray2.90K1-129[»]
    4KJAX-ray2.90K1-129[»]
    4KJCX-ray2.90K1-129[»]
    ProteinModelPortaliP0A7R9.
    SMRiP0A7R9. Positions 2-129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7R9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S11P family.Curated

    Phylogenomic databases

    eggNOGiCOG0100.
    HOGENOMiHOG000111598.
    KOiK02948.
    OMAiHISASFN.
    OrthoDBiEOG6ZSPF3.
    PhylomeDBiP0A7R9.

    Family and domain databases

    Gene3Di3.30.420.80. 1 hit.
    HAMAPiMF_01310. Ribosomal_S11.
    InterProiIPR001971. Ribosomal_S11.
    IPR019981. Ribosomal_S11_bac-type.
    IPR018102. Ribosomal_S11_CS.
    [Graphical view]
    PANTHERiPTHR11759. PTHR11759. 1 hit.
    PfamiPF00411. Ribosomal_S11. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
    TIGRFAMsiTIGR03632. bact_S11. 1 hit.
    PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7R9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKAPIRARK RVRKQVSDGV AHIHASFNNT IVTITDRQGN ALGWATAGGS    50
    GFRGSRKSTP FAAQVAAERC ADAVKEYGIK NLEVMVKGPG PGRESTIRAL 100
    NAAGFRITNI TDVTPIPHNG CRPPKKRRV 129
    Length:129
    Mass (Da):13,845
    Last modified:January 23, 2007 - v2
    Checksum:i0C759DDA60E89C0C
    GO

    Mass spectrometryi

    Molecular mass is 13727.7 Da from positions 2 - 129. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02543 Genomic DNA. Translation: CAA26393.1.
    U18997 Genomic DNA. Translation: AAA58095.1.
    U00096 Genomic DNA. Translation: AAC76322.1.
    AP009048 Genomic DNA. Translation: BAE77994.1.
    PIRiB23807. R3EC11.
    RefSeqiNP_417756.1. NC_000913.3.
    YP_492135.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76322; AAC76322; b3297.
    BAE77994; BAE77994; BAE77994.
    GeneIDi12934439.
    947792.
    KEGGiecj:Y75_p3879.
    eco:b3297.
    PATRICi32122026. VBIEscCol129921_3390.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02543 Genomic DNA. Translation: CAA26393.1 .
    U18997 Genomic DNA. Translation: AAA58095.1 .
    U00096 Genomic DNA. Translation: AAC76322.1 .
    AP009048 Genomic DNA. Translation: BAE77994.1 .
    PIRi B23807. R3EC11.
    RefSeqi NP_417756.1. NC_000913.3.
    YP_492135.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M5G model - K 13-129 [» ]
    1P6G electron microscopy 12.30 K 2-129 [» ]
    1P87 electron microscopy 11.50 K 2-129 [» ]
    1VS5 X-ray 3.46 K 1-129 [» ]
    1VS7 X-ray 3.46 K 1-129 [» ]
    2AVY X-ray 3.46 K 2-129 [» ]
    2AW7 X-ray 3.46 K 2-129 [» ]
    2GY9 electron microscopy 15.00 K 13-128 [» ]
    2GYB electron microscopy 15.00 K 13-128 [» ]
    2I2P X-ray 3.22 K 2-129 [» ]
    2I2U X-ray 3.22 K 2-129 [» ]
    2QAL X-ray 3.21 K 2-129 [» ]
    2QAN X-ray 3.21 K 2-129 [» ]
    2QB9 X-ray 3.54 K 2-129 [» ]
    2QBB X-ray 3.54 K 2-129 [» ]
    2QBD X-ray 3.30 K 2-129 [» ]
    2QBF X-ray 3.30 K 2-129 [» ]
    2QBH X-ray 4.00 K 2-129 [» ]
    2QBJ X-ray 4.00 K 2-129 [» ]
    2QOU X-ray 3.93 K 2-129 [» ]
    2QOW X-ray 3.93 K 2-129 [» ]
    2QOY X-ray 3.50 K 2-129 [» ]
    2QP0 X-ray 3.50 K 2-129 [» ]
    2VHO X-ray 3.74 K 2-129 [» ]
    2VHP X-ray 3.74 K 2-129 [» ]
    2WWL electron microscopy 5.80 K 13-129 [» ]
    2YKR electron microscopy 9.80 K 13-129 [» ]
    2Z4K X-ray 4.45 K 2-129 [» ]
    2Z4M X-ray 4.45 K 2-129 [» ]
    3DF1 X-ray 3.50 K 2-128 [» ]
    3DF3 X-ray 3.50 K 2-129 [» ]
    3E1A electron microscopy - C 1-129 [» ]
    3E1C electron microscopy - C 1-129 [» ]
    3FIH electron microscopy 6.70 K 13-129 [» ]
    3I1M X-ray 3.19 K 1-129 [» ]
    3I1O X-ray 3.19 K 1-129 [» ]
    3I1Q X-ray 3.81 K 1-129 [» ]
    3I1S X-ray 3.81 K 1-129 [» ]
    3I1Z X-ray 3.71 K 1-129 [» ]
    3I21 X-ray 3.71 K 1-129 [» ]
    3IZV electron microscopy - O 1-129 [» ]
    3IZW electron microscopy - O 1-129 [» ]
    3J00 electron microscopy - K 2-129 [» ]
    3J0U electron microscopy 12.10 N 2-129 [» ]
    3J0V electron microscopy 14.70 N 2-129 [» ]
    3J0X electron microscopy 13.50 N 2-129 [» ]
    3J0Z electron microscopy 11.50 N 2-129 [» ]
    3J10 electron microscopy 11.50 N 2-129 [» ]
    3J13 electron microscopy 13.10 M 2-129 [» ]
    3J18 electron microscopy 8.30 K 13-129 [» ]
    3J36 electron microscopy 9.80 K 2-129 [» ]
    3J4V electron microscopy 12.00 K 13-129 [» ]
    3J4W electron microscopy 12.00 K 13-129 [» ]
    3J4Y electron microscopy 17.00 K 13-129 [» ]
    3J4Z electron microscopy 20.00 K 13-129 [» ]
    3J53 electron microscopy 13.00 K 13-129 [» ]
    3J55 electron microscopy 15.00 K 13-129 [» ]
    3J57 electron microscopy 17.00 K 13-129 [» ]
    3J59 electron microscopy 12.00 K 13-129 [» ]
    3J5B electron microscopy 17.00 K 13-129 [» ]
    3J5D electron microscopy 17.00 K 13-129 [» ]
    3J5F electron microscopy 20.00 K 13-129 [» ]
    3J5H electron microscopy 15.00 K 13-129 [» ]
    3J5J electron microscopy 9.00 K 13-129 [» ]
    3J5N electron microscopy 6.80 K 1-129 [» ]
    3J5T electron microscopy 7.60 K 2-129 [» ]
    3J5X electron microscopy 7.60 K 2-129 [» ]
    3KC4 electron microscopy - K 1-129 [» ]
    3OAQ X-ray 3.25 K 13-129 [» ]
    3OAR X-ray 3.25 K 13-129 [» ]
    3OFA X-ray 3.19 K 13-129 [» ]
    3OFB X-ray 3.19 K 13-129 [» ]
    3OFO X-ray 3.10 K 13-129 [» ]
    3OFP X-ray 3.10 K 13-129 [» ]
    3OFX X-ray 3.29 K 13-129 [» ]
    3OFY X-ray 3.29 K 13-129 [» ]
    3OR9 X-ray 3.30 K 1-129 [» ]
    3ORA X-ray 3.30 K 1-129 [» ]
    3SFS X-ray 3.20 K 1-129 [» ]
    3UOQ X-ray 3.70 K 1-129 [» ]
    4A2I electron microscopy 16.50 K 13-129 [» ]
    4ADV electron microscopy 13.50 K 2-129 [» ]
    4GAQ X-ray 3.30 K 1-129 [» ]
    4GAS X-ray 3.30 K 1-129 [» ]
    4GD1 X-ray 3.00 K 13-129 [» ]
    4GD2 X-ray 3.00 K 13-129 [» ]
    4KIY X-ray 2.90 K 1-129 [» ]
    4KJ0 X-ray 2.90 K 1-129 [» ]
    4KJ2 X-ray 2.90 K 1-129 [» ]
    4KJ4 X-ray 2.90 K 1-129 [» ]
    4KJ6 X-ray 2.90 K 1-129 [» ]
    4KJ8 X-ray 2.90 K 1-129 [» ]
    4KJA X-ray 2.90 K 1-129 [» ]
    4KJC X-ray 2.90 K 1-129 [» ]
    ProteinModelPortali P0A7R9.
    SMRi P0A7R9. Positions 2-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852104. 1 interaction.
    DIPi DIP-47838N.
    IntActi P0A7R9. 14 interactions.
    MINTi MINT-1232137.
    STRINGi 511145.b3297.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7R9.
    PRIDEi P0A7R9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76322 ; AAC76322 ; b3297 .
    BAE77994 ; BAE77994 ; BAE77994 .
    GeneIDi 12934439.
    947792.
    KEGGi ecj:Y75_p3879.
    eco:b3297.
    PATRICi 32122026. VBIEscCol129921_3390.

    Organism-specific databases

    EchoBASEi EB0903.
    EcoGenei EG10910. rpsK.

    Phylogenomic databases

    eggNOGi COG0100.
    HOGENOMi HOG000111598.
    KOi K02948.
    OMAi HISASFN.
    OrthoDBi EOG6ZSPF3.
    PhylomeDBi P0A7R9.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10910-MONOMER.
    ECOL316407:JW3259-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7R9.
    PROi P0A7R9.

    Gene expression databases

    Genevestigatori P0A7R9.

    Family and domain databases

    Gene3Di 3.30.420.80. 1 hit.
    HAMAPi MF_01310. Ribosomal_S11.
    InterProi IPR001971. Ribosomal_S11.
    IPR019981. Ribosomal_S11_bac-type.
    IPR018102. Ribosomal_S11_CS.
    [Graphical view ]
    PANTHERi PTHR11759. PTHR11759. 1 hit.
    Pfami PF00411. Ribosomal_S11. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002131. Ribosomal_S11. 1 hit.
    TIGRFAMsi TIGR03632. bact_S11. 1 hit.
    PROSITEi PS00054. RIBOSOMAL_S11. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli."
      Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L.
      Nucleic Acids Res. 13:3891-3903(1985) [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. "Primary structure of protein S11 from Escherichia coli ribosomes."
      Kamp R., Wittmann-Liebold B.
      FEBS Lett. 121:117-122(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-129.
      Strain: K.
    5. "Photochemical cross-linking of initiation factor-3 to Escherichia coli 30 S ribosomal subunits."
      MacKeen L.A., Kahan L., Wahba A.J., Schwartz I.
      J. Biol. Chem. 255:10526-10531(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO IF-3.
      Strain: B.
    6. "IF-3 crosslinking to Escherichia coli ribosomal 30 S subunits by three different light-dependent procedures: identification of 30 S proteins crosslinked to IF-3 -- utilization of a new two-stage crosslinking reagent, p-nitrobenzylmaleimide."
      Cooperman B.S., Expert-Bezancon A., Kahan L., Dondon J., Grunberg-Manago M.
      Arch. Biochem. Biophys. 208:554-562(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO IF-3.
    7. "Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane."
      Boileau G., Butler P., Hershey J.W.B., Traut R.R.
      Biochemistry 22:3162-3170(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO IF-3.
      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. "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. "Interaction of translation initiation factor 3 with the 30S ribosomal subunit."
      Dallas A., Noller H.F.
      Mol. Cell 8:855-864(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MODELING OF IF-3/30S SUBUNIT INTERACTION.
    11. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
      Tung C.-S., Joseph S., Sanbonmatsu K.Y.
      Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    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 nameiRS11_ECOLI
    AccessioniPrimary (citable) accession number: P0A7R9
    Secondary accession number(s): P02366, Q2M6W2
    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

    Miscellaneous

    Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies; exactly how IF-3 interacts with the 30S subunit is controversial.1 Publication

    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