Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P68679

- RS21_ECOLI

UniProt

P68679 - RS21_ECOLI

Protein

30S ribosomal protein S21

Gene

rpsU

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10920-MONOMER.
    ECOL316407:JW3037-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    30S ribosomal protein S21
    Gene namesi
    Name:rpsU
    Ordered Locus Names:b3065, JW3037
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10920. rpsU.

    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 – 717030S ribosomal protein S21PRO_0000178332Add
    BLAST

    Proteomic databases

    PaxDbiP68679.
    PRIDEiP68679.

    Expressioni

    Gene expression databases

    GenevestigatoriP68679.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-47839N.
    IntActiP68679. 23 interactions.
    MINTiMINT-1281887.
    STRINGi511145.b3065.

    Structurei

    Secondary structure

    1
    71
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Turni17 – 193
    Helixi20 – 223
    Turni25 – 273
    Helixi28 – 314
    Beta strandi32 – 354
    Beta strandi38 – 403
    Helixi41 – 5010
    Turni51 – 533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VS5X-ray3.46U1-71[»]
    1VS7X-ray3.46U1-71[»]
    2AVYX-ray3.46U1-71[»]
    2AW7X-ray3.46U1-71[»]
    2I2PX-ray3.22U2-71[»]
    2I2UX-ray3.22U2-71[»]
    2QALX-ray3.21U2-71[»]
    2QANX-ray3.21U2-71[»]
    2QB9X-ray3.54U2-71[»]
    2QBBX-ray3.54U2-71[»]
    2QBDX-ray3.30U2-71[»]
    2QBFX-ray3.30U2-71[»]
    2QBHX-ray4.00U2-71[»]
    2QBJX-ray4.00U2-71[»]
    2QOUX-ray3.93U2-71[»]
    2QOWX-ray3.93U2-71[»]
    2QOYX-ray3.50U2-71[»]
    2QP0X-ray3.50U2-71[»]
    2VHOX-ray3.74U1-71[»]
    2VHPX-ray3.74U1-71[»]
    2WWLelectron microscopy5.80U4-54[»]
    2YKRelectron microscopy9.80U4-54[»]
    2Z4KX-ray4.45U2-71[»]
    2Z4MX-ray4.45U2-71[»]
    3DF1X-ray3.50U1-71[»]
    3DF3X-ray3.50U1-71[»]
    3E1Aelectron microscopy-Q1-71[»]
    3E1Celectron microscopy-Q1-71[»]
    3FIHelectron microscopy6.70U4-54[»]
    3I1MX-ray3.19U1-71[»]
    3I1OX-ray3.19U1-71[»]
    3I1QX-ray3.81U1-71[»]
    3I1SX-ray3.81U1-71[»]
    3I1ZX-ray3.71U1-71[»]
    3I21X-ray3.71U1-71[»]
    3IZVelectron microscopy-Y1-71[»]
    3IZWelectron microscopy-Y1-71[»]
    3J00electron microscopy-U2-71[»]
    3J0Uelectron microscopy12.10X2-71[»]
    3J0Velectron microscopy14.70X2-71[»]
    3J0Xelectron microscopy13.50X2-71[»]
    3J0Zelectron microscopy11.50X2-71[»]
    3J10electron microscopy11.50X2-71[»]
    3J13electron microscopy13.10W2-71[»]
    3J18electron microscopy8.30U4-54[»]
    3J36electron microscopy9.80U2-71[»]
    3J4Velectron microscopy12.00U4-54[»]
    3J4Welectron microscopy12.00U4-54[»]
    3J4Yelectron microscopy17.00U4-54[»]
    3J4Zelectron microscopy20.00U4-54[»]
    3J53electron microscopy13.00U4-54[»]
    3J55electron microscopy15.00U4-54[»]
    3J57electron microscopy17.00U4-54[»]
    3J59electron microscopy12.00U4-54[»]
    3J5Belectron microscopy17.00U4-54[»]
    3J5Delectron microscopy17.00U4-54[»]
    3J5Felectron microscopy20.00U4-54[»]
    3J5Helectron microscopy15.00U4-54[»]
    3J5Jelectron microscopy9.00U4-54[»]
    3J5Nelectron microscopy6.80U1-71[»]
    3J5Telectron microscopy7.60U2-71[»]
    3J5Xelectron microscopy7.60U2-71[»]
    3KC4electron microscopy-U1-71[»]
    3OAQX-ray3.25U4-54[»]
    3OARX-ray3.25U4-54[»]
    3OFAX-ray3.19U4-54[»]
    3OFBX-ray3.19U4-54[»]
    3OFOX-ray3.10U4-54[»]
    3OFPX-ray3.10U4-54[»]
    3OFXX-ray3.29U4-54[»]
    3OFYX-ray3.29U4-54[»]
    3OR9X-ray3.30U1-71[»]
    3ORAX-ray3.30U1-71[»]
    3SFSX-ray3.20U1-71[»]
    3UOQX-ray3.70U1-71[»]
    4A2Ielectron microscopy16.50U4-54[»]
    4ADVelectron microscopy13.50U1-71[»]
    4GAQX-ray3.30U1-71[»]
    4GASX-ray3.30U1-71[»]
    4GD1X-ray3.00U4-54[»]
    4GD2X-ray3.00U4-54[»]
    4KIYX-ray2.90U1-71[»]
    4KJ0X-ray2.90U1-71[»]
    4KJ2X-ray2.90U1-71[»]
    4KJ4X-ray2.90U1-71[»]
    4KJ6X-ray2.90U1-71[»]
    4KJ8X-ray2.90U1-71[»]
    4KJAX-ray2.90U1-71[»]
    4KJCX-ray2.90U1-71[»]
    ProteinModelPortaliP68679.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68679.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S21P family.Curated

    Phylogenomic databases

    eggNOGiCOG0828.
    HOGENOMiHOG000157460.
    KOiK02970.
    OMAiRNCAKAG.
    OrthoDBiEOG6FBX3Z.
    PhylomeDBiP68679.

    Family and domain databases

    HAMAPiMF_00358. Ribosomal_S21.
    InterProiIPR001911. Ribosomal_S21.
    IPR018278. Ribosomal_S21_CS.
    [Graphical view]
    PfamiPF01165. Ribosomal_S21. 1 hit.
    [Graphical view]
    PRINTSiPR00976. RIBOSOMALS21.
    ProDomiPD005521. Ribosomal_S21. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    TIGRFAMsiTIGR00030. S21p. 1 hit.
    PROSITEiPS01181. RIBOSOMAL_S21. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P68679-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVIKVRENE PFDVALRRFK RSCEKAGVLA EVRRREFYEK PTTERKRAKA   50
    SAVKRHAKKL ARENARRTRL Y 71
    Length:71
    Mass (Da):8,500
    Last modified:January 23, 2007 - v2
    Checksum:iB2E8A18BFBB2F685
    GO

    Mass spectrometryi

    Molecular mass is 8368.8 Da from positions 2 - 71. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01687 Genomic DNA. Translation: AAA24599.1.
    V00346 Genomic DNA. Translation: CAA23635.1.
    U28379 Genomic DNA. Translation: AAA89145.1.
    U00096 Genomic DNA. Translation: AAC76101.1.
    AP009048 Genomic DNA. Translation: BAE77116.1.
    PIRiA02749. R3EC21.
    RefSeqiNP_417537.1. NC_000913.3.
    YP_491257.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76101; AAC76101; b3065.
    BAE77116; BAE77116; BAE77116.
    GeneIDi12933220.
    947577.
    KEGGiecj:Y75_p2991.
    eco:b3065.
    PATRICi32121544. VBIEscCol129921_3159.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01687 Genomic DNA. Translation: AAA24599.1 .
    V00346 Genomic DNA. Translation: CAA23635.1 .
    U28379 Genomic DNA. Translation: AAA89145.1 .
    U00096 Genomic DNA. Translation: AAC76101.1 .
    AP009048 Genomic DNA. Translation: BAE77116.1 .
    PIRi A02749. R3EC21.
    RefSeqi NP_417537.1. NC_000913.3.
    YP_491257.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VS5 X-ray 3.46 U 1-71 [» ]
    1VS7 X-ray 3.46 U 1-71 [» ]
    2AVY X-ray 3.46 U 1-71 [» ]
    2AW7 X-ray 3.46 U 1-71 [» ]
    2I2P X-ray 3.22 U 2-71 [» ]
    2I2U X-ray 3.22 U 2-71 [» ]
    2QAL X-ray 3.21 U 2-71 [» ]
    2QAN X-ray 3.21 U 2-71 [» ]
    2QB9 X-ray 3.54 U 2-71 [» ]
    2QBB X-ray 3.54 U 2-71 [» ]
    2QBD X-ray 3.30 U 2-71 [» ]
    2QBF X-ray 3.30 U 2-71 [» ]
    2QBH X-ray 4.00 U 2-71 [» ]
    2QBJ X-ray 4.00 U 2-71 [» ]
    2QOU X-ray 3.93 U 2-71 [» ]
    2QOW X-ray 3.93 U 2-71 [» ]
    2QOY X-ray 3.50 U 2-71 [» ]
    2QP0 X-ray 3.50 U 2-71 [» ]
    2VHO X-ray 3.74 U 1-71 [» ]
    2VHP X-ray 3.74 U 1-71 [» ]
    2WWL electron microscopy 5.80 U 4-54 [» ]
    2YKR electron microscopy 9.80 U 4-54 [» ]
    2Z4K X-ray 4.45 U 2-71 [» ]
    2Z4M X-ray 4.45 U 2-71 [» ]
    3DF1 X-ray 3.50 U 1-71 [» ]
    3DF3 X-ray 3.50 U 1-71 [» ]
    3E1A electron microscopy - Q 1-71 [» ]
    3E1C electron microscopy - Q 1-71 [» ]
    3FIH electron microscopy 6.70 U 4-54 [» ]
    3I1M X-ray 3.19 U 1-71 [» ]
    3I1O X-ray 3.19 U 1-71 [» ]
    3I1Q X-ray 3.81 U 1-71 [» ]
    3I1S X-ray 3.81 U 1-71 [» ]
    3I1Z X-ray 3.71 U 1-71 [» ]
    3I21 X-ray 3.71 U 1-71 [» ]
    3IZV electron microscopy - Y 1-71 [» ]
    3IZW electron microscopy - Y 1-71 [» ]
    3J00 electron microscopy - U 2-71 [» ]
    3J0U electron microscopy 12.10 X 2-71 [» ]
    3J0V electron microscopy 14.70 X 2-71 [» ]
    3J0X electron microscopy 13.50 X 2-71 [» ]
    3J0Z electron microscopy 11.50 X 2-71 [» ]
    3J10 electron microscopy 11.50 X 2-71 [» ]
    3J13 electron microscopy 13.10 W 2-71 [» ]
    3J18 electron microscopy 8.30 U 4-54 [» ]
    3J36 electron microscopy 9.80 U 2-71 [» ]
    3J4V electron microscopy 12.00 U 4-54 [» ]
    3J4W electron microscopy 12.00 U 4-54 [» ]
    3J4Y electron microscopy 17.00 U 4-54 [» ]
    3J4Z electron microscopy 20.00 U 4-54 [» ]
    3J53 electron microscopy 13.00 U 4-54 [» ]
    3J55 electron microscopy 15.00 U 4-54 [» ]
    3J57 electron microscopy 17.00 U 4-54 [» ]
    3J59 electron microscopy 12.00 U 4-54 [» ]
    3J5B electron microscopy 17.00 U 4-54 [» ]
    3J5D electron microscopy 17.00 U 4-54 [» ]
    3J5F electron microscopy 20.00 U 4-54 [» ]
    3J5H electron microscopy 15.00 U 4-54 [» ]
    3J5J electron microscopy 9.00 U 4-54 [» ]
    3J5N electron microscopy 6.80 U 1-71 [» ]
    3J5T electron microscopy 7.60 U 2-71 [» ]
    3J5X electron microscopy 7.60 U 2-71 [» ]
    3KC4 electron microscopy - U 1-71 [» ]
    3OAQ X-ray 3.25 U 4-54 [» ]
    3OAR X-ray 3.25 U 4-54 [» ]
    3OFA X-ray 3.19 U 4-54 [» ]
    3OFB X-ray 3.19 U 4-54 [» ]
    3OFO X-ray 3.10 U 4-54 [» ]
    3OFP X-ray 3.10 U 4-54 [» ]
    3OFX X-ray 3.29 U 4-54 [» ]
    3OFY X-ray 3.29 U 4-54 [» ]
    3OR9 X-ray 3.30 U 1-71 [» ]
    3ORA X-ray 3.30 U 1-71 [» ]
    3SFS X-ray 3.20 U 1-71 [» ]
    3UOQ X-ray 3.70 U 1-71 [» ]
    4A2I electron microscopy 16.50 U 4-54 [» ]
    4ADV electron microscopy 13.50 U 1-71 [» ]
    4GAQ X-ray 3.30 U 1-71 [» ]
    4GAS X-ray 3.30 U 1-71 [» ]
    4GD1 X-ray 3.00 U 4-54 [» ]
    4GD2 X-ray 3.00 U 4-54 [» ]
    4KIY X-ray 2.90 U 1-71 [» ]
    4KJ0 X-ray 2.90 U 1-71 [» ]
    4KJ2 X-ray 2.90 U 1-71 [» ]
    4KJ4 X-ray 2.90 U 1-71 [» ]
    4KJ6 X-ray 2.90 U 1-71 [» ]
    4KJ8 X-ray 2.90 U 1-71 [» ]
    4KJA X-ray 2.90 U 1-71 [» ]
    4KJC X-ray 2.90 U 1-71 [» ]
    ProteinModelPortali P68679.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47839N.
    IntActi P68679. 23 interactions.
    MINTi MINT-1281887.
    STRINGi 511145.b3065.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P68679.
    PRIDEi P68679.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76101 ; AAC76101 ; b3065 .
    BAE77116 ; BAE77116 ; BAE77116 .
    GeneIDi 12933220.
    947577.
    KEGGi ecj:Y75_p2991.
    eco:b3065.
    PATRICi 32121544. VBIEscCol129921_3159.

    Organism-specific databases

    EchoBASEi EB0913.
    EcoGenei EG10920. rpsU.

    Phylogenomic databases

    eggNOGi COG0828.
    HOGENOMi HOG000157460.
    KOi K02970.
    OMAi RNCAKAG.
    OrthoDBi EOG6FBX3Z.
    PhylomeDBi P68679.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10920-MONOMER.
    ECOL316407:JW3037-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P68679.
    PROi P68679.

    Gene expression databases

    Genevestigatori P68679.

    Family and domain databases

    HAMAPi MF_00358. Ribosomal_S21.
    InterProi IPR001911. Ribosomal_S21.
    IPR018278. Ribosomal_S21_CS.
    [Graphical view ]
    Pfami PF01165. Ribosomal_S21. 1 hit.
    [Graphical view ]
    PRINTSi PR00976. RIBOSOMALS21.
    ProDomi PD005521. Ribosomal_S21. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    TIGRFAMsi TIGR00030. S21p. 1 hit.
    PROSITEi PS01181. RIBOSOMAL_S21. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The operon that encodes the sigma subunit of RNA polymerase also encodes ribosomal protein S21 and DNA primase in E. coli K12."
      Burton Z.F., Gross C.A., Watanabe K.K., Burgess R.R.
      Cell 32:335-349(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Regulation of the rpsU-dnaG-rpoD macromolecular synthesis operon and the initiation of DNA replication in Escherichia coli K-12."
      Lupski J.R., Smiley B.L., Godson G.N.
      Mol. Gen. Genet. 189:48-57(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    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. "Determination of the complete amino acid sequence of protein S21 from Escherichia coli ribosomes."
      Vandekerckhove J., Rombauts W., Peeters B., Wittmann-Liebold B.
      Hoppe-Seyler's Z. Physiol. Chem. 356:1955-1976(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-71.
      Strain: K.
    6. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
      Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
      EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-35, CROSS-LINKING TO RRNA.
      Strain: MRE-600.
    7. "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.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRS21_ECOLI
    AccessioniPrimary (citable) accession number: P68679
    Secondary accession number(s): P02379, Q2M9E0, Q8ZI69
    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