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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2262 [new locus tag: SACOL_RS11895 ]
  • pan locus tag?: SAUPAN005730000
  • symbol: mobA
  • pan gene symbol?: mobA
  • synonym:
  • product: molybdopterin-guanine dinucleotide biosynthesis protein MobA

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2262 [new locus tag: SACOL_RS11895 ]
  • symbol: mobA
  • product: molybdopterin-guanine dinucleotide biosynthesis protein MobA
  • replicon: chromosome
  • strand: -
  • coordinates: 2326433..2327032
  • length: 600
  • 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
    421
    481
    541
    ATGAAAGCAATAATTCTTGCAGGTGGTCATTCAGTGCGATTTGGTAAGCCCAAAGCTTTT
    GCGGAAGTGAACGGTGAGACCTTTTATAGTAGAGTAATTAAGACATTAGAATCAACAAAT
    ATGTTCAATGAAATTATTATTAGTACAAATGCGCAATTGGCAACGCAATTTAAATATCCA
    AATGTTGTTATAGATGATGAGAATCATAATGATAAAGGTCCATTAGCAGGAATTTATACA
    ATCATGAAGCAACATCCTGAAGAAGAATTGTTTTTTGTCGTTTCTGTTGATACACCAATG
    ATTACTGGTAAAGCTGTAAGCACGTTGTATCAGTTTTTAGTTTCTCATCTTATTGAAAAT
    CATTTAGATGTCGCAGCTTTTAAAGAAGATGGACGTTTTATTCCAACAATTGCATTTTAT
    AGTCCGAATGCATTAGGCGCTATAACTAAAGCACTACATTCTGATAATTACAGTTTTAAA
    AATGTATATCATGAATTATCAACGGATTATTTGGATGTAAGGGATGTAGATGCGCCCTCA
    TATTGGTACAAAAATATAAATTATCAGCATGATTTGGACGCTTTAATTCAAAAATTGTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2262 [new locus tag: SACOL_RS11895 ]
  • symbol: MobA
  • description: molybdopterin-guanine dinucleotide biosynthesis protein MobA
  • length: 199
  • theoretical pI: 5.81455
  • theoretical MW: 22541.4
  • GRAVY: -0.164824

⊟Function[edit | edit source]

  • reaction:
    EC 2.7.7.77?  ExPASy
    Molybdenum cofactor guanylyltransferase GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor
  • TIGRFAM:
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdenum cofactor guanylyltransferase (TIGR02665; EC 2.7.7.77; HMM-score: 88.2)
    and 9 more
    molybdenum cofactor cytidylyltransferase (TIGR03310; EC 2.7.7.76; HMM-score: 32.4)
    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: 28.1)
    Hypothetical proteins Conserved TIGR00454 family protein (TIGR00454; HMM-score: 22.5)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR01173; EC 2.3.1.157,2.7.7.23; HMM-score: 19.3)
    Cell structure Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR01173; EC 2.3.1.157,2.7.7.23; HMM-score: 19.3)
    Metabolism Central intermediary metabolism Amino sugars UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR01173; EC 2.3.1.157,2.7.7.23; HMM-score: 19.3)
    xanthine dehydrogenase accessory protein pucB (TIGR03202; HMM-score: 16.2)
    pseudaminic acid cytidylyltransferase (TIGR03584; EC 2.7.7.81; HMM-score: 12.4)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other 2-phospho-L-lactate guanylyltransferase (TIGR03552; EC 2.7.7.68; HMM-score: 12.1)
  • TheSEED  :
    • Molybdenum cofactor guanylyltransferase (EC 2.7.7.77)
    Cofactors, Vitamins, Prosthetic Groups, Pigments Folate and pterines Molybdenum cofactor biosynthesis  Molybdopterin-guanine dinucleotide biosynthesis protein MobA
  • PFAM:
    GT-A (CL0110) NTP_transf_3; MobA-like NTP transferase domain (PF12804; HMM-score: 91.5)
    and 4 more
    IspD; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (PF01128; HMM-score: 16.6)
    CTP_transf_3; Cytidylyltransferase (PF02348; HMM-score: 14.9)
    Metallo-HOrase (CL0381) Lactamase_B_6; Metallo-beta-lactamase superfamily domain (PF16661; HMM-score: 14.6)
    CheY (CL0304) RcsC; RcsC Alpha-Beta-Loop (ABL) (PF09456; HMM-score: 14.3)

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

  • domains:
  • modifications:
  • cofactors: Mg2+
  • 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): 0.051389
    • TAT(Tat/SPI): 0.000857
    • LIPO(Sec/SPII): 0.002827
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKAIILAGGHSVRFGKPKAFAEVNGETFYSRVIKTLESTNMFNEIIISTNAQLATQFKYPNVVIDDENHNDKGPLAGIYTIMKQHPEEELFFVVSVDTPMITGKAVSTLYQFLVSHLIENHLDVAAFKEDGRFIPTIAFYSPNALGAITKALHSDNYSFKNVYHELSTDYLDVRDVDAPSYWYKNINYQHDLDALIQKL

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell:
  • interaction partners:

⊟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. ↑ 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)

⊟Relevant publications[edit | edit source]

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