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PangenomeCOLN315NCTC8325NewmanUSA300_FPR375704-0298108BA0217611819-97685071193ECT-R 2ED133ED98HO 5096 0412JH1JH9JKD6008JKD6159JSNZLGA251M013MRSA252MSHR1132MSSA476MW2Mu3Mu50RF122ST398T0131TCH60TW20USA300_TCH1516VC40

NCBI: 03-AUG-2016

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⊟Summary[edit | edit source]

Contents

  • 1 Summary
  • 2 Genome View
  • 3 Gene
    • 3.1 General
    • 3.2 Accession numbers
    • 3.3 Phenotype
    • 3.4 DNA sequence
  • 4 Protein
    • 4.1 General
    • 4.2 Function
    • 4.3 Structure, modifications & cofactors
    • 4.4 Localization
    • 4.5 Accession numbers
    • 4.6 Protein sequence
    • 4.7 Experimental data
  • 5 Expression & Regulation
    • 5.1 Operon
    • 5.2 Regulation
    • 5.3 Transcription pattern
    • 5.4 Protein synthesis (provided by Aureolib)
    • 5.5 Protein stability
  • 6 Biological Material
    • 6.1 Mutants
    • 6.2 Expression vector
    • 6.3 lacZ fusion
    • 6.4 GFP fusion
    • 6.5 two-hybrid system
    • 6.6 FLAG-tag construct
    • 6.7 Antibody
  • 7 Other Information
  • 8 Literature
    • 8.1 References
    • 8.2 Relevant publications
  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01182
  • pan locus tag?: SAUPAN003498000
  • symbol: SAOUHSC_01182
  • 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: SAOUHSC_01182
  • symbol: SAOUHSC_01182
  • product: peptide deformylase
  • replicon: chromosome
  • strand: +
  • coordinates: 1133639..1134127
  • length: 489
  • essential: no DEG other strains

⊟Accession numbers[edit | edit source]

  • Gene ID: 3919315 NCBI
  • RefSeq: YP_499721 NCBI
  • BioCyc: G1I0R-1108 BioCyc
  • MicrobesOnline: 1289635 MicrobesOnline

⊟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
    ACAAGAAGTAAAATGATAGTTGTCGAAAGTTATGACGTCAATGGGAACAAAGTTGAACTA
    ACTGCACATGAAGATGTAGCAAGAATGATTTTGCATATTATAGATCAAATGAACGGTATC
    CCTTTTACAGAACGTGCGGACCGTATTTTAACAGATAAAGAAGTGGAGGCATATTTTATA
    AATGACTAA
    60
    120
    180
    240
    300
    360
    420
    480
    489

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_01182
  • symbol: SAOUHSC_01182
  • description: peptide deformylase
  • length: 162
  • theoretical pI: 4.36649
  • theoretical MW: 18101.7
  • GRAVY: -0.110494

⊟Function[edit | edit source]

  • ⊞reaction:
    EC 3.5.1.31?  ExPASy
    Formylmethionine deformylase N-formyl-L-methionine + H2O = formate + L-methionine
    EC 3.5.1.88?  ExPASy
    Peptide deformylase Formyl-L-methionyl peptide + H2O = formate + methionyl peptide
  • 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: 143)
    and 2 more
    4H_Cytokine (CL0053) CNTF; Ciliary neurotrophic factor (PF01110; HMM-score: 12.8)
    PDDEXK (CL0236) NotI; Restriction endonuclease NotI (PF12183; HMM-score: 11.5)

⊟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
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.9972
    • Cytoplasmic Membrane Score: 0.0004
    • Cell wall & surface Score: 0
    • Extracellular Score: 0.0024
  • ⊞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]

  • GI: 88194921 NCBI
  • RefSeq: YP_499721 NCBI
  • UniProt: Q2G265 UniProt
  • STRING: 93061.SAOUHSC_01182 STRING

⊟Protein sequence[edit | edit source]

  • MAIKKLVPASHPILTKKAQAVKTFDDSLKRLLQDLEDTMYAQEAAGLCAPQINQSLQVAIIDMEMEGLLQLVNPKIISQSNETITDLEGSITLPDVYGEVTRSKMIVVESYDVNGNKVELTAHEDVARMILHIIDQMNGIPFTERADRILTDKEVEAYFIND

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [1] [2]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • ⊟interaction partners:
    SAOUHSC_00743(nrdF)ribonucleotide-diphosphate reductase subunit beta  [3] (data from MRSA252)
    SAOUHSC_00519(rplA)50S ribosomal protein L1  [3] (data from MRSA252)
    SAOUHSC_02505(rplP)50S ribosomal protein L16  [3] (data from MRSA252)
    SAOUHSC_01232(rpsB)30S ribosomal protein S2  [3] (data from MRSA252)
    SAOUHSC_02506(rpsC)30S ribosomal protein S3  [3] (data from MRSA252)
    SAOUHSC_02494(rpsE)30S ribosomal protein S5  [3] (data from MRSA252)
    SAOUHSC_02503(rpsQ)30S ribosomal protein S17  [3] (data from MRSA252)
    SAOUHSC_02353(upp)uracil phosphoribosyltransferase  [3] (data from MRSA252)
    SAOUHSC_00187formate acetyltransferase  [3] (data from MRSA252)
    SAOUHSC_00206L-lactate dehydrogenase  [3] (data from MRSA252)
    SAOUHSC_00488hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_00529elongation factor G  [3] (data from MRSA252)
    SAOUHSC_00530elongation factor Tu  [3] (data from MRSA252)
    SAOUHSC_00679hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_00792hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_00878hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_00947enoyl-(acyl carrier protein) reductase  [3] (data from MRSA252)
    SAOUHSC_01007bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase  [3] (data from MRSA252)
    SAOUHSC_01040pyruvate dehydrogenase complex, E1 component subunit alpha  [3] (data from MRSA252)
    SAOUHSC_01043dihydrolipoamide dehydrogenase  [3] (data from MRSA252)
    SAOUHSC_01451threonine dehydratase  [3] (data from MRSA252)
    SAOUHSC_01794glyceraldehyde 3-phosphate dehydrogenase 2  [3] (data from MRSA252)
    SAOUHSC_01806pyruvate kinase  [3] (data from MRSA252)
    SAOUHSC_01819hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_01820acetate kinase  [3] (data from MRSA252)
    SAOUHSC_01859hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_02000glutamate-1-semialdehyde aminotransferase  [3] (data from MRSA252)
    SAOUHSC_02301  [3] (data from MRSA252)
    SAOUHSC_02337UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [3] (data from MRSA252)
    SAOUHSC_02377pyrimidine-nucleoside phosphorylase  [3] (data from MRSA252)
    SAOUHSC_02574hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_02579hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_02849pyruvate oxidase  [3] (data from MRSA252)
    SAOUHSC_02860HMG-CoA synthase  [3] (data from MRSA252)
    SAOUHSC_02969arginine deiminase  [3] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

  • MicrobesOnline: SAOUHSC_01182 > SAOUHSC_01183 > SAOUHSC_01184 > SAOUHSC_01185 > SAOUHSC_01186 > SAOUHSC_01187
    predicted SigA promoter [4] : SAOUHSC_01182 > SAOUHSC_01183 > SAOUHSC_01184 > SAOUHSC_01185 > SAOUHSC_01186 > SAOUHSC_01187

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

  • S.aureus Expression Data Browser:  [4] 
    Expression Data Browser
    ⊟Multi-gene expression profiles



    Click on any data point to display a description of the corresponding condition!

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

  • Aureolib: no data available

⊟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. ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  2. ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  3. ↑ Jump up to: 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 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)
  4. ↑ Jump up to: 4.0 4.1 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

⊟Relevant publications[edit | edit source]

Retrieved from "http://fungenwikiserver.biologie.uni-greifswald.de/aureowiki/index.php?title=SAOUHSC_01182&oldid=102074"
  • This page was last edited on 11 March 2016, at 13:52.
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