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NCBI: 26-AUG-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA1058 [new locus tag: SA_RS06005 ]
  • pan locus tag?: SAUPAN003498000
  • symbol: SA1058
  • pan gene symbol?: def2
  • synonym:
  • product: peptide deformylase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SA1058 [new locus tag: SA_RS06005 ]
  • symbol: SA1058
  • product: peptide deformylase
  • replicon: chromosome
  • strand: +
  • coordinates: 1197820..1198308
  • length: 489
  • essential: no DEG 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
    ATGGCGATTAAAAAGTTAGTACCAGCATCGCATCCTATTTTAACGAAAAAAGCGCAAGCA
    GTTAAAACATTTGATGATTCGTTAAAAAGATTATTACAAGATTTAGAAGATACAATGTAT
    GCACAAGAAGCTGCTGGCTTATGTGCACCTCAAATTAATCAGTCATTGCAAGTGGCAATT
    ATTGATATGGAAATGGAAGGATTATTACAACTTGTTAATCCGAAAATTATTAGTCAATCA
    AATGAAACAATAACAGACTTAGAAGGTTCAATTACATTGCCAGATGTTTACGGCGAAGTG
    ACAAGAAGTAAAATGATAGTTGTTGAAAGTTATGACGTCAATGGGAACAAAGTTGAACTA
    ACTGCACATGAAGATGTAGCAAGAATGATTTTGCATATTATAGATCAAATGAACGGTATC
    CCTTTTACAGAACGTGCGGACCGTATTTTAACAGATAAAGAAGTGGAGGCATATTTTATA
    AATGACTAA
    60
    120
    180
    240
    300
    360
    420
    480
    489

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SA1058 [new locus tag: SA_RS06005 ]
  • symbol: SA1058
  • description: peptide deformylase
  • length: 162
  • theoretical pI: 4.36649
  • theoretical MW: 18101.7
  • GRAVY: -0.110494

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein fate Protein modification and repair peptide deformylase (TIGR00079; EC 3.5.1.88; HMM-score: 105.4)
  • TheSEED  :
    • Peptide deformylase (EC 3.5.1.88)
    Carbohydrates Central carbohydrate metabolism Dehydrogenase complexes  Peptide deformylase (EC 3.5.1.88)
    and 1 more
    Protein Metabolism Protein biosynthesis Translation termination factors bacterial  Peptide deformylase (EC 3.5.1.88)
  • PFAM:
    no clan defined Pep_deformylase; Polypeptide deformylase (PF01327; HMM-score: 132)
    and 1 more
    4H_Cytokine (CL0053) CNTF; Ciliary neurotrophic factor (PF01110; HMM-score: 12.8)

⊟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): 0.009408
    • TAT(Tat/SPI): 0.000392
    • LIPO(Sec/SPII): 0.000424
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAIKKLVPASHPILTKKAQAVKTFDDSLKRLLQDLEDTMYAQEAAGLCAPQINQSLQVAIIDMEMEGLLQLVNPKIISQSNETITDLEGSITLPDVYGEVTRSKMIVVESYDVNGNKVELTAHEDVARMILHIIDQMNGIPFTERADRILTDKEVEAYFIND

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • interaction partners:
    SA1533(ackA)acetate kinase  [1] (data from MRSA252)
    SA2428(arcA)arginine deiminase  [1] (data from MRSA252)
    SA0471(cysK)hypothetical protein  [1] (data from MRSA252)
    SA0869(fabI)enoyl-ACP reductase  [1] (data from MRSA252)
    SA0915(folD)bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [1] (data from MRSA252)
    SA0505(fus)elongation factor G  [1] (data from MRSA252)
    SA1510(gapB)glyceraldehyde 3-phosphate dehydrogenase 2  [1] (data from MRSA252)
    SA1681(gsaB)glutamate-1-semialdehyde aminotransferase  [1] (data from MRSA252)
    SA0232(lctE)L-lactate dehydrogenase  [1] (data from MRSA252)
    SA1902(murA)UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [1] (data from MRSA252)
    SA2334(mvaS)3-hydroxy-3-methylglutaryl-CoA synthase  [1] (data from MRSA252)
    SA0687(nrdF)ribonucleotide-diphosphate reductase subunit beta  [1] (data from MRSA252)
    SA0943-1(pdhA)pyruvate dehydrogenase E1 component subunit alpha  [1] (data from MRSA252)
    SA0946(pdhD)dihydrolipoamide dehydrogenase  [1] (data from MRSA252)
    SA1938(pdp)pyrimidine-nucleoside phosphorylase  [1] (data from MRSA252)
    SA0218(pflB)formate acetyltransferase  [1] (data from MRSA252)
    SA1520(pykA)pyruvate kinase  [1] (data from MRSA252)
    SA0496(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    SA2040(rplP)50S ribosomal protein L16  [1] (data from MRSA252)
    SA1099(rpsB)30S ribosomal protein S2  [1] (data from MRSA252)
    SA2041(rpsC)30S ribosomal protein S3  [1] (data from MRSA252)
    SA2031(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SA2038(rpsQ)30S ribosomal protein S17  [1] (data from MRSA252)
    SA1872(rsbU)sigmaB regulation protein RsbU  [1] (data from MRSA252)
    SA0506(tuf)elongation factor Tu  [1] (data from MRSA252)
    SA1914(upp)uracil phosphoribosyltransferase  [1] (data from MRSA252)
    SA0627hypothetical protein  [1] (data from MRSA252)
    SA0724hypothetical protein  [1] (data from MRSA252)
    SA0802hypothetical protein  [1] (data from MRSA252)
    SA1271threonine dehydratase  [1] (data from MRSA252)
    SA1532hypothetical protein  [1] (data from MRSA252)
    SA1564hypothetical protein  [1] (data from MRSA252)
    SA2095hypothetical protein  [1] (data from MRSA252)
    SA2099hypothetical protein  [1] (data from MRSA252)
    SA2327pyruvate oxidase  [1] (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. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 1.28 1.29 1.30 1.31 1.32 1.33 1.34 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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