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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00903
  • pan locus tag?: SAUPAN003074000
  • symbol: SAOUHSC_00903
  • pan gene symbol?: spsB
  • synonym:
  • product: signal peptidase IB

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_00903
  • symbol: SAOUHSC_00903
  • product: signal peptidase IB
  • replicon: chromosome
  • strand: +
  • coordinates: 867744..868211
  • length: 468
  • essential: yes [1] 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
    ATGGATCCAACTTTGAAAGATGGCGAGCGAGTAGCTGTAAACATTGTTGGATATAAAACA
    GGTGGTTTGGAAAAAGGTAATGTAGTTGTCTTCCATGCAAACAAAAATGATGACTATGTT
    AAACGTGTCATCGGTGTTCCTGGTGATAAAGTAGAATACAAAAATGATACATTATATGTC
    AATGGTAAAAAACAAGATGAACCATATTTAAACTACAATTTAAAACATAAACAAGGTGAT
    TACATTACTGGGACTTTCCAAGTTAAAGATTTACCGAATGCGAATCCTAAATCAAATGTC
    ATTCCAAAAGGTAAATATTTAGTGCTTGGAGATAATCGTGAAGTAAGTAAAGATAGCCGT
    GCGTTTGGCCTCATTGATGAAGACCAAATTGTTGGTAAAGTTTCATTTAGGTTCTGGCCA
    TTTAGTGAATTTAAACATAATTTCAATCCTGAAAATACTAAAAATTAA
    60
    120
    180
    240
    300
    360
    420
    468

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_00903
  • symbol: SAOUHSC_00903
  • description: signal peptidase IB
  • length: 155
  • theoretical pI: 9.41739
  • theoretical MW: 17597.7
  • GRAVY: -0.796774

⊟Function[edit | edit source]

  • reaction:
    EC 3.4.21.89?  ExPASy
    Signal peptidase I Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins
  • TIGRFAM:
    Genetic information processing Protein fate Protein and peptide secretion and trafficking signal peptidase I (TIGR02227; EC 3.4.21.89; HMM-score: 148.9)
    and 4 more
    Cellular processes Cellular processes Detoxification nickel-type superoxide dismutase maturation protease (TIGR02754; EC 3.4.21.-; HMM-score: 40.6)
    Genetic information processing Protein fate Protein modification and repair nickel-type superoxide dismutase maturation protease (TIGR02754; EC 3.4.21.-; HMM-score: 40.6)
    conjugative transfer signal peptidase TraF (TIGR02771; HMM-score: 37.3)
    signal peptidase I (TIGR02228; EC 3.4.21.89; HMM-score: 18)
  • TheSEED  :
    • Signal peptidase I (EC 3.4.21.89)
    Protein Metabolism Protein processing and modification Signal peptidase  Signal peptidase I (EC 3.4.21.89)
  • PFAM:
    Peptidase_SF (CL0299) Peptidase_S24; Peptidase S24-like (PF00717; HMM-score: 60.5)
    and 1 more
    Peptidase_S26; Signal peptidase, peptidase S26 (PF10502; HMM-score: 37)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cellwall
    • Cytoplasmic Score: 0.01
    • Cytoplasmic Membrane Score: 0.53
    • Cellwall Score: 8.75
    • Extracellular Score: 0.7
    • 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): 0.020827
    • TAT(Tat/SPI): 0.000743
    • LIPO(Sec/SPII): 0.003513
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MDPTLKDGERVAVNIVGYKTGGLEKGNVVVFHANKNDDYVKRVIGVPGDKVEYKNDTLYVNGKKQDEPYLNYNLKHKQGDYITGTFQVKDLPNANPKSNVIPKGKYLVLGDNREVSKDSRAFGLIDEDQIVGKVSFRFWPFSEFKHNFNPENTKN

⊟Experimental data[edit | edit source]

⊟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. ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
    Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
    BMC Genomics: 2009, 10;291
    [PubMed:19570206] [WorldCat.org] [DOI] (I e)
  2. ↑ 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)
  3. ↑ 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)
  4. ↑ 4.000 4.001 4.002 4.003 4.004 4.005 4.006 4.007 4.008 4.009 4.010 4.011 4.012 4.013 4.014 4.015 4.016 4.017 4.018 4.019 4.020 4.021 4.022 4.023 4.024 4.025 4.026 4.027 4.028 4.029 4.030 4.031 4.032 4.033 4.034 4.035 4.036 4.037 4.038 4.039 4.040 4.041 4.042 4.043 4.044 4.045 4.046 4.047 4.048 4.049 4.050 4.051 4.052 4.053 4.054 4.055 4.056 4.057 4.058 4.059 4.060 4.061 4.062 4.063 4.064 4.065 4.066 4.067 4.068 4.069 4.070 4.071 4.072 4.073 4.074 4.075 4.076 4.077 4.078 4.079 4.080 4.081 4.082 4.083 4.084 4.085 4.086 4.087 4.088 4.089 4.090 4.091 4.092 4.093 4.094 4.095 4.096 4.097 4.098 4.099 4.100 4.101 4.102 4.103 4.104 4.105 4.106 4.107 4.108 4.109 4.110 4.111 4.112 4.113 4.114 4.115 4.116 4.117 4.118 4.119 4.120 4.121 4.122 4.123 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)
  5. ↑ 5.0 5.1 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]

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