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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0698 [new locus tag: SACOL_RS03590 ]
  • pan locus tag?: SAUPAN002518000
  • symbol: tagD
  • pan gene symbol?: tagD
  • synonym:
  • product: glycerol-3-phosphate cytidylyltransferase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0698 [new locus tag: SACOL_RS03590 ]
  • symbol: tagD
  • product: glycerol-3-phosphate cytidylyltransferase
  • replicon: chromosome
  • strand: +
  • coordinates: 722415..722813
  • length: 399
  • 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
    ATGAAACGTGTAATAACATATGGCACATATGACTTACTTCACTATGGTCATATCGAATTG
    CTTCGTCGTGCAAGAGAGATGGGCGATTATTTAATAGTAGCATTATCAACAGATGAATTT
    AATCAAATTAAACATAAAAAATCTTATTATGATTATGAACAACGAAAAATGATGCTTGAA
    TCAATACGCTATGTCGATTTAGTCATTCCAGAAAAGGGCTGGGGACAAAAAGAAGACGAT
    GTCGAAAAATTTGATGTAGATGTTTTTGTTATGGGACATGACTGGGAAGGTGAATTCGAC
    TTCTTAAAGGATAAATGTGAAGTCATTTATTTAAAACGTACAGAAGGCATTTCGACGACT
    AAAATCAAACAAGAATTATATGGTAAAGATGCTAAATAA
    60
    120
    180
    240
    300
    360
    399

⊟Protein[edit | edit source]

Protein Data Bank: 2B7L

⊟General[edit | edit source]

  • locus tag: SACOL0698 [new locus tag: SACOL_RS03590 ]
  • symbol: TagD
  • description: glycerol-3-phosphate cytidylyltransferase
  • length: 132
  • theoretical pI: 5.69067
  • theoretical MW: 15817
  • GRAVY: -0.660606

⊟Function[edit | edit source]

  • reaction:
    EC 2.7.7.15?  ExPASy
    Choline-phosphate cytidylyltransferase CTP + phosphocholine = diphosphate + CDP-choline
  • TIGRFAM:
    Cell structure Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan glycerol-3-phosphate cytidylyltransferase (TIGR01518; EC 2.7.7.39; HMM-score: 201)
    and 5 more
    cytidyltransferase-like domain (TIGR00125; HMM-score: 77.8)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides bifunctional protein RfaE, domain II (TIGR02199; EC 2.7.7.-; HMM-score: 61.5)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pantothenate and coenzyme A pantetheine-phosphate adenylyltransferase (TIGR01510; EC 2.7.7.3; HMM-score: 29.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides nicotinate (nicotinamide) nucleotide adenylyltransferase (TIGR00482; EC 2.7.7.18; HMM-score: 15.2)
    nicotinamide-nucleotide adenylyltransferase (TIGR01526; EC 2.7.7.1; HMM-score: 13.8)
  • TheSEED  :
    • Glycerol-3-phosphate cytidylyltransferase (EC 2.7.7.39)
    Cell Wall and Capsule Gram-Positive cell wall components Teichoic and lipoteichoic acids biosynthesis  Glycerol-3-phosphate cytidylyltransferase (EC 2.7.7.39)
  • PFAM:
    HUP (CL0039) CTP_transf_like; Cytidylyltransferase-like (PF01467; HMM-score: 83.6)
    and 3 more
    FAD_syn; FAD synthetase (PF06574; HMM-score: 18.2)
    HIGH_NTase1_ass; Cytidyltransferase-related C-terminal region (PF16581; HMM-score: 14.9)
    Pantoate_ligase; Pantoate-beta-alanine ligase (PF02569; HMM-score: 13.8)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • 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): 0.003818
    • TAT(Tat/SPI): 0.00017
    • LIPO(Sec/SPII): 0.000723
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKRVITYGTYDLLHYGHIELLRRAREMGDYLIVALSTDEFNQIKHKKSYYDYEQRKMMLESIRYVDLVIPEKGWGQKEDDVEKFDVDVFVMGHDWEGEFDFLKDKCEVIYLKRTEGISTTKIKQELYGKDAK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 57 [4]
  • interaction partners:
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [5] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [5] (data from MRSA252)
    SACOL1011(ppnK)inorganic polyphosphate/ATP-NAD kinase  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (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: 38.6 h [6]

⊟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, 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 5.0 5.1 5.2 5.3 5.4 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)
  6. ↑ 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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