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NCBI: 02-MAR-2017

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA_RS11770 [old locus tag: SA2048 ]
  • pan locus tag?: SAUPAN005703000
  • symbol: SA_RS11770
  • pan gene symbol?: rpsJ
  • synonym:
  • product: 30S ribosomal protein S10

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SA_RS11770 [old locus tag: SA2048 ]
  • symbol: SA_RS11770
  • product: 30S ribosomal protein S10
  • replicon: chromosome
  • strand: -
  • coordinates: 2308333..2308641
  • length: 309
  • essential: yes [1] DEG

⊟Accession numbers[edit | edit source]

  • Location: NC_002745 (2308333..2308641) NCBI
  • BioCyc: SA_RS11770 BioCyc
  • MicrobesOnline: see SA2048

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    ATGGCAAAACAAAAAATCAGAATCAGATTAAAAGCTTATGATCACCGCGTGATTGATCAA
    TCAGCAGAGAAGATTGTAGAAACAGCGAAACGTTCTGGTGCAGATGTTTCTGGACCAATT
    CCGTTACCAACTGAGAAATCAGTTTACACAATCATCCGTGCCGTGCATAAGTATAAAGAT
    TCACGTGAACAATTCGAACAACGTACACACAAACGTTTAATCGATATTGTAAACCCAACA
    CCAAAAACAGTTGACGCTTTAATGGGCTTAAACTTACCATCTGGTGTAGACATCGAAATC
    AAATTATAA
    60
    120
    180
    240
    300
    309

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SA_RS11770 [old locus tag: SA2048 ]
  • symbol: SA_RS11770
  • description: 30S ribosomal protein S10
  • length: 102
  • theoretical pI: 10.3739
  • theoretical MW: 11576.4
  • GRAVY: -0.492157

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS10 (TIGR01049; HMM-score: 152.5)
    and 1 more
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uS10 (TIGR01046; HMM-score: 65.1)
  • TheSEED: see SA2048
  • PFAM:
    no clan defined Ribosomal_S10; Ribosomal protein S10p/S20e (PF00338; HMM-score: 120.9)
    and 2 more
    DUF384; Domain of unknown function (DUF384) (PF04064; HMM-score: 16.7)
    Phi-29_GP3; Phi-29 DNA terminal protein GP3 (PF05435; HMM-score: 14.2)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • Internal Helices: 0
  • LocateP:
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.005469
    • TAT(Tat/SPI): 0.000491
    • LIPO(Sec/SPII): 0.001485
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAKQKIRIRLKAYDHRVIDQSAEKIVETAKRSGADVSGPIPLPTEKSVYTIIRAVHKYKDSREQFEQRTHKRLIDIVNPTPKTVDALMGLNLPSGVDIEIKL

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for COL
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA_RS11130(deoA)pyrimidine-nucleoside phosphorylase  [2] (data from MRSA252)
    SA_RS00170DNA gyrase subunit A  [2] (data from MRSA252)
    SA_RS01275formate acetyltransferase  [2] (data from MRSA252)
    SA_RS01365L-lactate dehydrogenase  [2] (data from MRSA252)
    SA_RS0290550S ribosomal protein L11  [2] (data from MRSA252)
    SA_RS0291550S ribosomal protein L10  [2] (data from MRSA252)
    SA_RS0292050S ribosomal protein L7/L12  [2] (data from MRSA252)
    SA_RS0294530S ribosomal protein S12  [2] (data from MRSA252)
    SA_RS02955elongation factor G  [2] (data from MRSA252)
    SA_RS02960elongation factor Tu  [2] (data from MRSA252)
    SA_RS02985UDP-glucose 4-epimerase  [2] (data from MRSA252)
    SA_RS04575NADH dehydrogenase  [2] (data from MRSA252)
    SA_RS05350pyruvate dehydrogenase E1 component subunit alpha  [2] (data from MRSA252)
    SA_RS05365dihydrolipoyl dehydrogenase  [2] (data from MRSA252)
    SA_RS0614050S ribosomal protein L19  [2] (data from MRSA252)
    SA_RS0622530S ribosomal protein S2  [2] (data from MRSA252)
    SA_RS06325ribonuclease J 2  [2] (data from MRSA252)
    SA_RS07385DNA-binding protein HU  [2] (data from MRSA252)
    SA_RS07725glycine dehydrogenase  [2] (data from MRSA252)
    SA_RS0829550S ribosomal protein L21  [2] (data from MRSA252)
    SA_RS08470translation initiation factor IF-3  [2] (data from MRSA252)
    SA_RS08505aldehyde dehydrogenase  [2] (data from MRSA252)
    SA_RS08560pyruvate kinase  [2] (data from MRSA252)
    SA_RS08625universal stress protein UspA  [2] (data from MRSA252)
    SA_RS10535molecular chaperone GroEL  [2] (data from MRSA252)
    SA_RS10845DEAD/DEAH box family ATP-dependent RNA helicase  [2] (data from MRSA252)
    SA_RS11010uracil phosphoribosyltransferase  [2] (data from MRSA252)
    SA_RS11070UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [2] (data from MRSA252)
    SA_RS1164030S ribosomal protein S11  [2] (data from MRSA252)
    SA_RS1167050S ribosomal protein L15  [2] (data from MRSA252)
    SA_RS1168030S ribosomal protein S5  [2] (data from MRSA252)
    SA_RS1175050S ribosomal protein L2  [2] (data from MRSA252)
    SA_RS1175550S ribosomal protein L23  [2] (data from MRSA252)
    SA_RS13340pyruvate oxidase  [2] (data from MRSA252)
    SA_RS13735malate:quinone oxidoreductase  [2] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: no data available

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

  1. ↑ R Allyn Forsyth, Robert J Haselbeck, Kari L Ohlsen, Robert T Yamamoto, Howard Xu, John D Trawick, Daniel Wall, Liangsu Wang, Vickie Brown-Driver, Jamie M Froelich, Kedar G C, Paula King, Melissa McCarthy, Cheryl Malone, Brian Misiner, David Robbins, Zehui Tan, Zhan-yang Zhu Zy, Grant Carr, Deborah A Mosca, Carlos Zamudio, J Gordon Foulkes, Judith W Zyskind
    A genome-wide strategy for the identification of essential genes in Staphylococcus aureus.
    Mol Microbiol: 2002, 43(6);1387-400
    [PubMed:11952893] [WorldCat.org] [DOI] (P p)
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 2.21 2.22 2.23 2.24 2.25 2.26 2.27 2.28 2.29 2.30 2.31 2.32 2.33 2.34 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
    Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
    J Proteome Res: 2011, 10(3);1139-50
    [PubMed:21166474] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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