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P0A7U7

- RS20_ECOLI

UniProt

P0A7U7 - RS20_ECOLI

Protein

30S ribosomal protein S20

Gene

rpsT

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

    Binds directly to 16S ribosomal RNA.

    GO - Molecular functioni

    1. ornithine decarboxylase inhibitor activity Source: EcoCyc
    2. small ribosomal subunit rRNA binding Source: EcoCyc
    3. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. negative regulation of catalytic activity Source: GOC
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10919-MONOMER.
    ECOL316407:JW0022-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S20
    Gene namesi
    Name:rpsT
    Ordered Locus Names:b0023, JW0022
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10919. rpsT.

    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 – 878630S ribosomal protein S20PRO_0000167958Add
    BLAST

    Proteomic databases

    PaxDbiP0A7U7.
    PRIDEiP0A7U7.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7U7.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-35857N.
    IntActiP0A7U7. 57 interactions.
    STRINGi511145.b0023.

    Structurei

    Secondary structure

    1
    87
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Helixi9 – 4133
    Helixi44 – 6421
    Turni66 – 694
    Helixi70 – 8314
    Turni84 – 863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M5Gmodel-T3-87[»]
    1P6Gelectron microscopy12.30T2-87[»]
    1P87electron microscopy11.50T2-87[»]
    1VS5X-ray3.46T1-87[»]
    1VS7X-ray3.46T1-87[»]
    2AVYX-ray3.46T2-87[»]
    2AW7X-ray3.46T2-87[»]
    2GY9electron microscopy15.00T5-87[»]
    2GYBelectron microscopy15.00T5-87[»]
    2I2PX-ray3.22T2-87[»]
    2I2UX-ray3.22T2-87[»]
    2QALX-ray3.21T2-87[»]
    2QANX-ray3.21T2-87[»]
    2QB9X-ray3.54T2-87[»]
    2QBBX-ray3.54T2-87[»]
    2QBDX-ray3.30T2-87[»]
    2QBFX-ray3.30T2-87[»]
    2QBHX-ray4.00T2-87[»]
    2QBJX-ray4.00T2-87[»]
    2QOUX-ray3.93T2-87[»]
    2QOWX-ray3.93T2-87[»]
    2QOYX-ray3.50T2-87[»]
    2QP0X-ray3.50T2-87[»]
    2VHPX-ray3.74T2-87[»]
    2WWLelectron microscopy5.80T3-87[»]
    2YKRelectron microscopy9.80T3-87[»]
    2Z4KX-ray4.45T2-87[»]
    2Z4MX-ray4.45T2-87[»]
    3DF1X-ray3.50T2-87[»]
    3DF3X-ray3.50T2-86[»]
    3E1Aelectron microscopy-N1-87[»]
    3E1Celectron microscopy-N1-87[»]
    3FIHelectron microscopy6.70T3-87[»]
    3I1MX-ray3.19T1-87[»]
    3I1OX-ray3.19T1-87[»]
    3I1QX-ray3.81T1-87[»]
    3I1SX-ray3.81T1-87[»]
    3I1ZX-ray3.71T1-87[»]
    3I21X-ray3.71T1-87[»]
    3IZVelectron microscopy-X1-87[»]
    3IZWelectron microscopy-X1-87[»]
    3J00electron microscopy-T2-87[»]
    3J0Uelectron microscopy12.10W2-87[»]
    3J0Velectron microscopy14.70W2-87[»]
    3J0Xelectron microscopy13.50W2-87[»]
    3J0Zelectron microscopy11.50W2-87[»]
    3J10electron microscopy11.50W2-87[»]
    3J13electron microscopy13.10V2-87[»]
    3J18electron microscopy8.30T3-87[»]
    3J36electron microscopy9.80T2-87[»]
    3J4Velectron microscopy12.00T3-87[»]
    3J4Welectron microscopy12.00T3-87[»]
    3J4Yelectron microscopy17.00T3-87[»]
    3J4Zelectron microscopy20.00T3-87[»]
    3J53electron microscopy13.00T3-87[»]
    3J55electron microscopy15.00T3-87[»]
    3J57electron microscopy17.00T3-87[»]
    3J59electron microscopy12.00T3-87[»]
    3J5Belectron microscopy17.00T3-87[»]
    3J5Delectron microscopy17.00T3-87[»]
    3J5Felectron microscopy20.00T3-87[»]
    3J5Helectron microscopy15.00T3-87[»]
    3J5Jelectron microscopy9.00T3-87[»]
    3J5Nelectron microscopy6.80T1-87[»]
    3J5Telectron microscopy7.60T2-87[»]
    3J5Xelectron microscopy7.60T2-87[»]
    3KC4electron microscopy-T1-87[»]
    3OAQX-ray3.25T3-87[»]
    3OARX-ray3.25T3-87[»]
    3OFAX-ray3.19T3-87[»]
    3OFBX-ray3.19T3-87[»]
    3OFOX-ray3.10T3-87[»]
    3OFPX-ray3.10T3-87[»]
    3OFXX-ray3.29T3-87[»]
    3OFYX-ray3.29T3-87[»]
    3OR9X-ray3.30T1-87[»]
    3ORAX-ray3.30T1-87[»]
    3SFSX-ray3.20T1-87[»]
    3UOQX-ray3.70T1-87[»]
    4A2Ielectron microscopy16.50T3-87[»]
    4ADVelectron microscopy13.50T2-87[»]
    4GAQX-ray3.30T1-87[»]
    4GASX-ray3.30T1-87[»]
    4GD1X-ray3.00T3-87[»]
    4GD2X-ray3.00T3-87[»]
    4KIYX-ray2.90T1-87[»]
    4KJ0X-ray2.90T1-87[»]
    4KJ2X-ray2.90T1-87[»]
    4KJ4X-ray2.90T1-87[»]
    4KJ6X-ray2.90T1-87[»]
    4KJ8X-ray2.90T1-87[»]
    4KJAX-ray2.90T1-87[»]
    4KJCX-ray2.90T1-87[»]
    ProteinModelPortaliP0A7U7.
    SMRiP0A7U7. Positions 3-87.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7U7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S20P family.Curated

    Phylogenomic databases

    eggNOGiCOG0268.
    HOGENOMiHOG000097048.
    KOiK02968.
    OMAiRHKSNLT.
    OrthoDBiEOG6HMXNQ.
    PhylomeDBiP0A7U7.

    Family and domain databases

    Gene3Di1.20.58.110. 1 hit.
    HAMAPiMF_00500. Ribosomal_S20.
    InterProiIPR002583. Ribosomal_S20.
    [Graphical view]
    PfamiPF01649. Ribosomal_S20p. 1 hit.
    [Graphical view]
    ProDomiPD004231. Ribosomal_S20. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF46992. SSF46992. 1 hit.
    TIGRFAMsiTIGR00029. S20. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P0A7U7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANIKSAKKR AIQSEKARKH NASRRSMMRT FIKKVYAAIE AGDKAAAQKA   50
    FNEMQPIVDR QAAKGLIHKN KAARHKANLT AQINKLA 87
    Length:87
    Mass (Da):9,684
    Last modified:January 23, 2007 - v2
    Checksum:iF02154BE2D1E22D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381A → R in AAA24604. (PubMed:2985604)Curated

    Mass spectrometryi

    Molecular mass is 9553.6 Da from positions 2 - 87. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10428 Genomic DNA. Translation: AAA24604.1.
    X04382 Genomic DNA. Translation: CAA27968.1.
    U00096 Genomic DNA. Translation: AAC73134.1.
    AP009048 Genomic DNA. Translation: BAB96593.1.
    PIRiA30425. R3EC20.
    RefSeqiNP_414564.1. NC_000913.3.
    YP_488329.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73134; AAC73134; b0023.
    BAB96593; BAB96593; BAB96593.
    GeneIDi12931850.
    944759.
    KEGGiecj:Y75_p0023.
    eco:b0023.
    PATRICi32115137. VBIEscCol129921_0020.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10428 Genomic DNA. Translation: AAA24604.1 .
    X04382 Genomic DNA. Translation: CAA27968.1 .
    U00096 Genomic DNA. Translation: AAC73134.1 .
    AP009048 Genomic DNA. Translation: BAB96593.1 .
    PIRi A30425. R3EC20.
    RefSeqi NP_414564.1. NC_000913.3.
    YP_488329.1. 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 - T 3-87 [» ]
    1P6G electron microscopy 12.30 T 2-87 [» ]
    1P87 electron microscopy 11.50 T 2-87 [» ]
    1VS5 X-ray 3.46 T 1-87 [» ]
    1VS7 X-ray 3.46 T 1-87 [» ]
    2AVY X-ray 3.46 T 2-87 [» ]
    2AW7 X-ray 3.46 T 2-87 [» ]
    2GY9 electron microscopy 15.00 T 5-87 [» ]
    2GYB electron microscopy 15.00 T 5-87 [» ]
    2I2P X-ray 3.22 T 2-87 [» ]
    2I2U X-ray 3.22 T 2-87 [» ]
    2QAL X-ray 3.21 T 2-87 [» ]
    2QAN X-ray 3.21 T 2-87 [» ]
    2QB9 X-ray 3.54 T 2-87 [» ]
    2QBB X-ray 3.54 T 2-87 [» ]
    2QBD X-ray 3.30 T 2-87 [» ]
    2QBF X-ray 3.30 T 2-87 [» ]
    2QBH X-ray 4.00 T 2-87 [» ]
    2QBJ X-ray 4.00 T 2-87 [» ]
    2QOU X-ray 3.93 T 2-87 [» ]
    2QOW X-ray 3.93 T 2-87 [» ]
    2QOY X-ray 3.50 T 2-87 [» ]
    2QP0 X-ray 3.50 T 2-87 [» ]
    2VHP X-ray 3.74 T 2-87 [» ]
    2WWL electron microscopy 5.80 T 3-87 [» ]
    2YKR electron microscopy 9.80 T 3-87 [» ]
    2Z4K X-ray 4.45 T 2-87 [» ]
    2Z4M X-ray 4.45 T 2-87 [» ]
    3DF1 X-ray 3.50 T 2-87 [» ]
    3DF3 X-ray 3.50 T 2-86 [» ]
    3E1A electron microscopy - N 1-87 [» ]
    3E1C electron microscopy - N 1-87 [» ]
    3FIH electron microscopy 6.70 T 3-87 [» ]
    3I1M X-ray 3.19 T 1-87 [» ]
    3I1O X-ray 3.19 T 1-87 [» ]
    3I1Q X-ray 3.81 T 1-87 [» ]
    3I1S X-ray 3.81 T 1-87 [» ]
    3I1Z X-ray 3.71 T 1-87 [» ]
    3I21 X-ray 3.71 T 1-87 [» ]
    3IZV electron microscopy - X 1-87 [» ]
    3IZW electron microscopy - X 1-87 [» ]
    3J00 electron microscopy - T 2-87 [» ]
    3J0U electron microscopy 12.10 W 2-87 [» ]
    3J0V electron microscopy 14.70 W 2-87 [» ]
    3J0X electron microscopy 13.50 W 2-87 [» ]
    3J0Z electron microscopy 11.50 W 2-87 [» ]
    3J10 electron microscopy 11.50 W 2-87 [» ]
    3J13 electron microscopy 13.10 V 2-87 [» ]
    3J18 electron microscopy 8.30 T 3-87 [» ]
    3J36 electron microscopy 9.80 T 2-87 [» ]
    3J4V electron microscopy 12.00 T 3-87 [» ]
    3J4W electron microscopy 12.00 T 3-87 [» ]
    3J4Y electron microscopy 17.00 T 3-87 [» ]
    3J4Z electron microscopy 20.00 T 3-87 [» ]
    3J53 electron microscopy 13.00 T 3-87 [» ]
    3J55 electron microscopy 15.00 T 3-87 [» ]
    3J57 electron microscopy 17.00 T 3-87 [» ]
    3J59 electron microscopy 12.00 T 3-87 [» ]
    3J5B electron microscopy 17.00 T 3-87 [» ]
    3J5D electron microscopy 17.00 T 3-87 [» ]
    3J5F electron microscopy 20.00 T 3-87 [» ]
    3J5H electron microscopy 15.00 T 3-87 [» ]
    3J5J electron microscopy 9.00 T 3-87 [» ]
    3J5N electron microscopy 6.80 T 1-87 [» ]
    3J5T electron microscopy 7.60 T 2-87 [» ]
    3J5X electron microscopy 7.60 T 2-87 [» ]
    3KC4 electron microscopy - T 1-87 [» ]
    3OAQ X-ray 3.25 T 3-87 [» ]
    3OAR X-ray 3.25 T 3-87 [» ]
    3OFA X-ray 3.19 T 3-87 [» ]
    3OFB X-ray 3.19 T 3-87 [» ]
    3OFO X-ray 3.10 T 3-87 [» ]
    3OFP X-ray 3.10 T 3-87 [» ]
    3OFX X-ray 3.29 T 3-87 [» ]
    3OFY X-ray 3.29 T 3-87 [» ]
    3OR9 X-ray 3.30 T 1-87 [» ]
    3ORA X-ray 3.30 T 1-87 [» ]
    3SFS X-ray 3.20 T 1-87 [» ]
    3UOQ X-ray 3.70 T 1-87 [» ]
    4A2I electron microscopy 16.50 T 3-87 [» ]
    4ADV electron microscopy 13.50 T 2-87 [» ]
    4GAQ X-ray 3.30 T 1-87 [» ]
    4GAS X-ray 3.30 T 1-87 [» ]
    4GD1 X-ray 3.00 T 3-87 [» ]
    4GD2 X-ray 3.00 T 3-87 [» ]
    4KIY X-ray 2.90 T 1-87 [» ]
    4KJ0 X-ray 2.90 T 1-87 [» ]
    4KJ2 X-ray 2.90 T 1-87 [» ]
    4KJ4 X-ray 2.90 T 1-87 [» ]
    4KJ6 X-ray 2.90 T 1-87 [» ]
    4KJ8 X-ray 2.90 T 1-87 [» ]
    4KJA X-ray 2.90 T 1-87 [» ]
    4KJC X-ray 2.90 T 1-87 [» ]
    ProteinModelPortali P0A7U7.
    SMRi P0A7U7. Positions 3-87.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35857N.
    IntActi P0A7U7. 57 interactions.
    STRINGi 511145.b0023.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7U7.
    PRIDEi P0A7U7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73134 ; AAC73134 ; b0023 .
    BAB96593 ; BAB96593 ; BAB96593 .
    GeneIDi 12931850.
    944759.
    KEGGi ecj:Y75_p0023.
    eco:b0023.
    PATRICi 32115137. VBIEscCol129921_0020.

    Organism-specific databases

    EchoBASEi EB0912.
    EcoGenei EG10919. rpsT.

    Phylogenomic databases

    eggNOGi COG0268.
    HOGENOMi HOG000097048.
    KOi K02968.
    OMAi RHKSNLT.
    OrthoDBi EOG6HMXNQ.
    PhylomeDBi P0A7U7.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10919-MONOMER.
    ECOL316407:JW0022-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7U7.
    PROi P0A7U7.

    Gene expression databases

    Genevestigatori P0A7U7.

    Family and domain databases

    Gene3Di 1.20.58.110. 1 hit.
    HAMAPi MF_00500. Ribosomal_S20.
    InterProi IPR002583. Ribosomal_S20.
    [Graphical view ]
    Pfami PF01649. Ribosomal_S20p. 1 hit.
    [Graphical view ]
    ProDomi PD004231. Ribosomal_S20. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF46992. SSF46992. 1 hit.
    TIGRFAMsi TIGR00029. S20. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the gene for ribosomal protein S20 and its flanking regions."
      Mackie G.A.
      J. Biol. Chem. 256:8177-8182(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon."
      Kamio Y., Lin C.-K., Regue M., Wu H.C.
      J. Biol. Chem. 260:5616-5620(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Structure of the DNA distal to the gene for ribosomal protein S20 in Escherichia coli K12: presence of a strong terminator and an IS1 element."
      Mackie G.A.
      Nucleic Acids Res. 14:6965-6981(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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.
    7. "Primary structure of protein S20 from the small ribosomal subunit of Escherichia coli."
      Wittmann-Liebold B., Marzinzig E., Lehmann A.
      FEBS Lett. 68:110-114(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-87.
      Strain: K.
    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. "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.
    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 nameiRS20_ECOLI
    AccessioniPrimary (citable) accession number: P0A7U7
    Secondary accession number(s): P02378
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 97 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