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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0594 [new locus tag: SACOL_RS03080 ]
  • pan locus tag?: SAUPAN002320000
  • symbol: tuf
  • pan gene symbol?: tuf
  • synonym:
  • product: elongation factor Tu

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0594 [new locus tag: SACOL_RS03080 ]
  • symbol: tuf
  • product: elongation factor Tu
  • replicon: chromosome
  • strand: +
  • coordinates: 618158..619342
  • length: 1185
  • 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
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    ATGGCAAAAGAAAAATTCGATCGTTCTAAAGAACATGCCAATATCGGTACTATCGGTCAC
    GTTGACCATGGTAAAACAACATTAACAGCAGCAATCGCTACTGTATTAGCAAAAAATGGT
    GACTCAGTTGCACAATCATATGACATGATTGACAACGCTCCAGAAGAAAAAGAACGTGGT
    ATCACAATCAATACTTCTCACATTGAGTACCAAACTGACAAACGTCACTACGCTCACGTT
    GACTGCCCAGGACACGCTGACTACGTTAAAAACATGATCACTGGTGCTGCTCAAATGGAC
    GGCGGTATCTTAGTAGTATCTGCTGCTGACGGTCCAATGCCACAAACTCGTGAACACATT
    CTTTTATCACGTAACGTTGGTGTACCAGCATTAGTAGTATTCTTAAACAAAGTTGACATG
    GTTGACGATGAAGAATTATTAGAATTAGTAGAAATGGAAGTTCGTGACTTATTAAGCGAA
    TATGACTTCCCAGGTGACGATGTACCTGTAATCGCTGGTTCAGCATTAAAAGCTTTAGAA
    GGCGATGCTCAATACGAAGAAAAAATCTTAGAATTAATGGAAGCTGTAGATACTTACATT
    CCAACTCCAGAACGTGATTCTGACAAACCATTCATGATGCCAGTTGAGGACGTATTCTCA
    ATCACTGGTCGTGGTACTGTTGCTACAGGCCGTGTTGAACGTGGTCAAATCAAAGTTGGT
    GAAGAAGTTGAAATCATCGGTTTACATGACACATCTAAAACAACTGTTACAGGTGTTGAA
    ATGTTCCGTAAATTATTAGACTACGCTGAAGCTGGTGACAACATTGGTGCATTATTACGT
    GGTGTTGCTCGTGAAGACGTACAACGTGGTCAAGTATTAGCTGCTCCTGGTTCAATTACA
    CCACATACTGAATTCAAAGCAGAAGTATACGTATTATCAAAAGACGAAGGTGGACGTCAC
    ACTCCATTCTTCTCAAACTATCGTCCACAATTCTATTTCCGTACTACTGACGTAACTGGT
    GTTGTTCACTTACCAGAAGGTACTGAAATGGTAATGCCTGGTGATAACGTTGAAATGACA
    GTAGAATTAATCGCTCCAATCGCGATTGAAGACGGTACTCGTTTCTCAATCCGTGAAGGT
    GGACGTACTGTAGGATCAGGCGTTGTTACTGAAATCATTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1185

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0594 [new locus tag: SACOL_RS03080 ]
  • symbol: Tuf
  • description: elongation factor Tu
  • length: 394
  • theoretical pI: 4.48462
  • theoretical MW: 43103.4
  • GRAVY: -0.250508

⊟Function[edit | edit source]

  • reaction:
    EC 3.6.5.3?  ExPASy
    Protein-synthesizing GTPase GTP + H2O = GDP + phosphate
  • TIGRFAM:
    Genetic information processing Protein synthesis Translation factors translation elongation factor Tu (TIGR00485; HMM-score: 773.7)
    and 18 more
    Genetic information processing Protein synthesis Translation factors translation elongation factor EF-1, subunit alpha (TIGR00483; HMM-score: 216.2)
    Genetic information processing Protein synthesis Translation factors selenocysteine-specific translation elongation factor (TIGR00475; HMM-score: 184.5)
    translation initiation factor 2, gamma subunit (TIGR03680; HMM-score: 129.4)
    Cellular processes Cellular processes Adaptations to atypical conditions GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 122.8)
    Genetic information processing Protein synthesis Translation factors GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 122.8)
    Signal transduction Regulatory functions Other GTP-binding protein TypA/BipA (TIGR01394; HMM-score: 122.8)
    Metabolism Central intermediary metabolism Sulfur metabolism sulfate adenylyltransferase, large subunit (TIGR02034; EC 2.7.7.4; HMM-score: 112.8)
    Unknown function General elongation factor 4 (TIGR01393; EC 3.6.5.-; HMM-score: 82.3)
    Genetic information processing Protein synthesis Translation factors translation elongation factor aEF-2 (TIGR00490; HMM-score: 78.1)
    Genetic information processing Protein synthesis Translation factors translation initiation factor IF-2 (TIGR00487; HMM-score: 68.9)
    Genetic information processing Protein synthesis Translation factors translation elongation factor G (TIGR00484; HMM-score: 53.3)
    Unknown function General small GTP-binding protein domain (TIGR00231; HMM-score: 52)
    Genetic information processing Protein synthesis Translation factors peptide chain release factor 3 (TIGR00503; HMM-score: 44.6)
    Genetic information processing Protein synthesis Translation factors translation initiation factor aIF-2 (TIGR00491; HMM-score: 34.7)
    Metabolism Energy metabolism Amino acids and amines ethanolamine utilization protein, EutP (TIGR02528; HMM-score: 13.4)
    Genetic information processing Protein synthesis Other ribosome-associated GTPase EngA (TIGR03594; HMM-score: 13.4)
    arsenical pump-driving ATPase (TIGR04291; EC 3.6.1.-; HMM-score: 12.5)
    cell division ATPase MinD (TIGR01969; HMM-score: 12.3)
  • TheSEED  :
    • Translation elongation factor Tu
    Protein Metabolism Protein biosynthesis Translation elongation factors bacterial  Translation elongation factor Tu
    and 2 more
    Protein Metabolism Protein biosynthesis Universal GTPases  Translation elongation factor Tu
    Virulence Virulence - no subcategory Mycobacterium virulence operon involved in protein synthesis (SSU ribosomal proteins)  Translation elongation factor Tu
  • PFAM:
    P-loop_NTPase (CL0023) GTP_EFTU; Elongation factor Tu GTP binding domain (PF00009; HMM-score: 204.3)
    and 6 more
    no clan defined GTP_EFTU_D3; Elongation factor Tu C-terminal domain (PF03143; HMM-score: 118.6)
    EFTPs (CL0575) GTP_EFTU_D2; Elongation factor Tu domain 2 (PF03144; HMM-score: 67.6)
    P-loop_NTPase (CL0023) MMR_HSR1; 50S ribosome-binding GTPase (PF01926; HMM-score: 21.7)
    CbiA; CobQ/CobB/MinD/ParA nucleotide binding domain (PF01656; HMM-score: 14.7)
    cobW; CobW/HypB/UreG, nucleotide-binding domain (PF02492; HMM-score: 13.6)
    RsgA_GTPase; RsgA GTPase (PF03193; HMM-score: 12.2)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 10
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0
    • Extracellular Score: 0
    • 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): 0.053712
    • TAT(Tat/SPI): 0.012475
    • LIPO(Sec/SPII): 0.004058
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAKEKFDRSKEHANIGTIGHVDHGKTTLTAAIATVLAKNGDSVAQSYDMIDNAPEEKERGITINTSHIEYQTDKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKALEGDAQYEEKILELMEAVDTYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQIKVGEEVEIIGLHDTSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDVQRGQVLAAPGSITPHTEFKAEVYVLSKDEGGRHTPFFSNYRPQFYFRTTDVTGVVHLPEGTEMVMPGDNVEMTVELIAPIAIEDGTRFSIREGGRTVGSGVVTEIIK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4] [5]
  • quantitative data / protein copy number per cell: 17452 [6]
  • interaction partners:
    SACOL0593(fusA)elongation factor G  [7] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [7] (data from MRSA252)
    SACOL0556(hslO)Hsp33-like chaperonin  [7] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [7] (data from MRSA252)
    SACOL0033(mecA)penicillin-binding protein 2'  [7] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [7] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [7] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [7] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [7] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [7] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [7] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [7] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [7] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [7] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [7] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [7] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [7] (data from MRSA252)
    SACOL1759universal stress protein  [7] (data from MRSA252)
    SACOL2553pyruvate oxidase  [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: 38.21 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 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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