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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00225
  • pan locus tag?: SAUPAN001133000
  • symbol: ispD
  • pan gene symbol?: tarI
  • synonym:
  • product: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_00225
  • symbol: ispD
  • product: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
  • replicon: chromosome
  • strand: +
  • coordinates: 245250..245966
  • length: 717
  • 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
    481
    541
    601
    661
    ATGAAATACGCTGGTATTCTAGCTGGAGGTATAGGCTCAAGAATGGGTAACGTACCTTTA
    CCTAAACAATTTTTAGATTTAGACAACAAACCGATTTTAATCCATACATTAGAAAAATTT
    ATTTTAATTAATGATTTTGAAAAAATTATTATCGCGACGCCACAACAATGGATGACGCAT
    ACGAAAGATACACTTAGAAAATTCAAAATTTCTGATGAAAGAATTGAAGTCATTCAAGGT
    GGTAGCGATCGTAACGATACAATTATGAATATCGTTAAACATATTGAATCAACAAATGGT
    ATTAACGATGACGATGTCATTGTGACACATGATGCAGTTAGACCATTTTTAACGCATCGT
    ATTATTAAAGAAAATATTCAAGCTGCTTTAGAGTACGGTGCAGTAGATACAGTGATTGAT
    GCTATAGATACGATTGTTACATCTAAAGATAATCAAACGATTGATGCAATTCCAGTGCGT
    AATGAAATGTACCAAGGTCAAACACCTCAATCGTTTAATATTAATTTATTAAAAGAAAGC
    TATGCACAGTTGAGTGATGAGCAAAAGAGTATTTTATCTGATGCTTGTAAGATTATTGTA
    GAAACAAACAAACCGGTTCGACTTGTAAAAGGTGAGTTATATAACATTAAAGTAACAACA
    CCTTACGATTTAAAAGTAGCGAATGCTATTATTCGAGGTGGTATTGCCGATGATTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    717

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_00225
  • symbol: IspD
  • description: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
  • length: 238
  • theoretical pI: 5.36178
  • theoretical MW: 26656.4
  • GRAVY: -0.215546

⊟Function[edit | edit source]

  • reaction:
    EC 2.7.7.40?  ExPASy
    D-ribitol-5-phosphate cytidylyltransferase CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol
    EC 2.7.7.60?  ExPASy
    2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
  • TIGRFAM:
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (TIGR00453; EC 2.7.7.60; HMM-score: 156.7)
    and 8 more
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdenum cofactor guanylyltransferase (TIGR02665; EC 2.7.7.77; HMM-score: 19.6)
    molybdenum cofactor cytidylyltransferase (TIGR03310; EC 2.7.7.76; HMM-score: 19.2)
    glucose-1-phosphate thymidylyltransferase (TIGR01208; EC 2.7.7.24; HMM-score: 16.8)
    Hypothetical proteins Conserved TIGR00454 family protein (TIGR00454; HMM-score: 14.6)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase (TIGR01479; EC 2.7.7.13,5.3.1.8; HMM-score: 14.5)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides glucose-1-phosphate cytidylyltransferase (TIGR02623; EC 2.7.7.33; HMM-score: 14)
    Cell structure Cell envelope Other rare lipoprotein A (TIGR00413; HMM-score: 13.4)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides glucose-1-phosphate thymidylyltransferase (TIGR01207; EC 2.7.7.24; HMM-score: 13.2)
  • TheSEED  :
    • Sugar-phosphate cytidylyltransferase
    Cell Wall and Capsule Gram-Positive cell wall components Teichoic and lipoteichoic acids biosynthesis  2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60)
    and 2 more
    Cell Wall and Capsule Gram-Positive cell wall components Teichoic and lipoteichoic acids biosynthesis  ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40)
    Fatty Acids, Lipids, and Isoprenoids Isoprenoids Isoprenoid Biosynthesis  2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60)
  • PFAM:
    GT-A (CL0110) IspD; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (PF01128; HMM-score: 145.9)
    and 3 more
    NTP_transf_3; MobA-like NTP transferase domain (PF12804; HMM-score: 31.8)
    CTP_transf_3; Cytidylyltransferase (PF02348; HMM-score: 25)
    NTP_transferase; Nucleotidyl transferase (PF00483; HMM-score: 18.4)

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

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

⊟Localization[edit | edit source]

  • PSORTb: unknown (no significant prediction)
    • Cytoplasmic Score: 2.5
    • Cytoplasmic Membrane Score: 2.5
    • Cellwall Score: 2.5
    • Extracellular Score: 2.5
    • 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): 0.004137
    • TAT(Tat/SPI): 0.000092
    • LIPO(Sec/SPII): 0.000995
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKYAGILAGGIGSRMGNVPLPKQFLDLDNKPILIHTLEKFILINDFEKIIIATPQQWMTHTKDTLRKFKISDERIEVIQGGSDRNDTIMNIVKHIESTNGINDDDVIVTHDAVRPFLTHRIIKENIQAALEYGAVDTVIDAIDTIVTSKDNQTIDAIPVRNEMYQGQTPQSFNINLLKESYAQLSDEQKSILSDACKIIVETNKPVRLVKGELYNIKVTTPYDLKVANAIIRGGIADD

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [2] [3]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SAOUHSC_02494(rpsE)30S ribosomal protein S5  [4] (data from MRSA252)
    SAOUHSC_01040pyruvate dehydrogenase complex, E1 component subunit alpha  [4] (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. ↑ 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. ↑ 4.0 4.1 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 5.2 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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