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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2224 [new locus tag: SACOL_RS11705 ]
  • pan locus tag?: SAUPAN005687000
  • symbol: rplF
  • pan gene symbol?: rplF
  • synonym:
  • product: 50S ribosomal protein L6

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2224 [new locus tag: SACOL_RS11705 ]
  • symbol: rplF
  • product: 50S ribosomal protein L6
  • replicon: chromosome
  • strand: -
  • coordinates: 2299852..2300388
  • length: 537
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    ATGAGTCGTGTTGGTAAGAAAATTATTGACATCCCTAGTGACGTAACAGTAACTTTTGAT
    GGAAATCATGTAACTGTTAAAGGTCCTAAAGGTGAATTATCAAGAACTTTAAATGAAAGA
    ATGACATTCAAACAAGAAGAAAACACAATTGAAGTTGTAAGACCATCTGATTCTAAAGAA
    GATAGAACAAACCATGGTACAACTCGTGCTTTATTAAACAATATGGTACAAGGTGTTTCT
    CAAGGATACGTAAAAGTACTTGAACTTGTTGGTGTAGGTTACCGTGCTCAAATGCAAGGT
    AAAGACTTAATCCTTAACGTTGGTTATTCTCACCCAGTAGAAATTAAAGCTGAAGAAAAC
    ATTACTTTCTCAGTTGAGAAAAACACAGTCGTTAAAGTTGAAGGTATTTCAAAAGAACAA
    GTTGGAGCATTAGCATCTAACATCCGTTCAGTAAGACCTCCAGAGCCTTACAAAGGTAAA
    GGTATTCGTTACCAAGGTGAATACGTTCGCCGTAAAGAAGGTAAAACTGGTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    537

⊟Protein[edit | edit source]

Protein Data Bank: 4WCE
Protein Data Bank: 4WF9
Protein Data Bank: 4WFA
Protein Data Bank: 4WFB
Protein Data Bank: 5HKV
Protein Data Bank: 5HL7
Protein Data Bank: 5LI0
Protein Data Bank: 5ND8
Protein Data Bank: 5ND9
Protein Data Bank: 5NRG
Protein Data Bank: 5TCU

⊟General[edit | edit source]

  • locus tag: SACOL2224 [new locus tag: SACOL_RS11705 ]
  • symbol: RplF
  • description: 50S ribosomal protein L6
  • length: 178
  • theoretical pI: 10.1171
  • theoretical MW: 19786.4
  • GRAVY: -0.635955

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL6 (TIGR03654; HMM-score: 247.2)
    and 2 more
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein uL6 (TIGR03653; HMM-score: 79.7)
    Planctomycetes uncharacterized domain TIGR03000 (TIGR03000; HMM-score: 13.3)
  • TheSEED  :
    • LSU ribosomal protein L6p (L9e)
    Protein Metabolism Protein biosynthesis Ribosome LSU bacterial  LSU ribosomal protein L6p (L9e)
  • PFAM:
    no clan defined Ribosomal_L6; Ribosomal protein L6 (PF00347; HMM-score: 147.7)
    and 1 more
    RAB3GAP2_N; Rab3 GTPase-activating protein regulatory subunit N-terminus (PF14655; HMM-score: 11.9)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • Internal Helices: 0
  • LocateP: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: -1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.008363
    • TAT(Tat/SPI): 0.000401
    • LIPO(Sec/SPII): 0.000857
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSRVGKKIIDIPSDVTVTFDGNHVTVKGPKGELSRTLNERMTFKQEENTIEVVRPSDSKEDRTNHGTTRALLNNMVQGVSQGYVKVLELVGVGYRAQMQGKDLILNVGYSHPVEIKAEENITFSVEKNTVVKVEGISKEQVGALASNIRSVRPPEPYKGKGIRYQGEYVRRKEGKTGK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4] [5]
  • quantitative data / protein copy number per cell: 5992 [6]
  • interaction partners:
    SACOL1518(cmk)cytidylate kinase  [7] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [7] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [7] (data from MRSA252)
    SACOL1245(fabG1)3-oxoacyl-ACP reductase  [7] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [7] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [7] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [7] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [7] (data from MRSA252)
    SACOL0961(gluD)glutamate dehydrogenase  [7] (data from MRSA252)
    SACOL1554(gnd)6-phosphogluconate dehydrogenase  [7] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [7] (data from MRSA252)
    SACOL0554(hpt)hypoxanthine phosphoribosyltransferase  [7] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [7] (data from MRSA252)
    SACOL0746(norR)MarR family transcriptional regulator  [7] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [7] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [7] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [7] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [7] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [7] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [7] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [7] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [7] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [7] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [7] (data from MRSA252)
    SACOL2112(rpmE2)50S ribosomal protein L31  [7] (data from MRSA252)
    SACOL1516(rpsA)30S ribosomal protein S1  [7] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [7] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [7] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [7] (data from MRSA252)
    SACOL0521hypothetical protein  [7] (data from MRSA252)
    SACOL0721hypothetical protein  [7] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [7] (data from MRSA252)
    SACOL0815ribosomal subunit interface protein  [7] (data from MRSA252)
    SACOL1020hypothetical protein  [7] (data from MRSA252)
    SACOL1670hypothetical protein  [7] (data from MRSA252)
    SACOL1794thioredoxin  [7] (data from MRSA252)
    SACOL1801dipeptidase PepV  [7] (data from MRSA252)
    SACOL1912hypothetical protein  [7] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [7] (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: 11.67 h [8]

⊟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. ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
    A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
    PLoS One: 2009, 4(12);e8176
    [PubMed:19997597] [WorldCat.org] [DOI] (I e)
  2. ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ Annette Dreisbach, Kristina Hempel, Girbe Buist, Michael Hecker, Dörte Becher, Jan Maarten van Dijl
    Profiling the surfacome of Staphylococcus aureus.
    Proteomics: 2010, 10(17);3082-96
    [PubMed:20662103] [WorldCat.org] [DOI] (I p)
  4. ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
    Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
    J Proteome Res: 2011, 10(4);1657-66
    [PubMed:21323324] [WorldCat.org] [DOI] (I p)
  5. ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
    The Staphylococcus aureus proteome.
    Int J Med Microbiol: 2014, 304(2);110-20
    [PubMed:24439828] [WorldCat.org] [DOI] (I p)
  6. ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
    Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
    Sci Rep: 2016, 6;28172
    [PubMed:27344979] [WorldCat.org] [DOI] (I e)
  7. ↑ 7.00 7.01 7.02 7.03 7.04 7.05 7.06 7.07 7.08 7.09 7.10 7.11 7.12 7.13 7.14 7.15 7.16 7.17 7.18 7.19 7.20 7.21 7.22 7.23 7.24 7.25 7.26 7.27 7.28 7.29 7.30 7.31 7.32 7.33 7.34 7.35 7.36 7.37 7.38 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)
  8. ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
    Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
    Mol Cell Proteomics: 2012, 11(9);558-70
    [PubMed:22556279] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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