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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2263 [new locus tag: SACOL_RS11900 ]
  • pan locus tag?: SAUPAN005731000
  • symbol: moaD
  • pan gene symbol?: moaD
  • synonym:
  • product: molybdopterin converting factor subunit 1

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2263 [new locus tag: SACOL_RS11900 ]
  • symbol: moaD
  • product: molybdopterin converting factor subunit 1
  • replicon: chromosome
  • strand: -
  • coordinates: 2327039..2327272
  • length: 234
  • 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
    ATGAAGGTACTTTACTTCGCAGAAATTAAAGATATATTACAAAAAGCACAGGAAGATATT
    GTGCTTGAACAAGCATTGACTGTACAACAATTTGAAGATTTATTGTTTGAACGTTATCCG
    CAAATCAATAATAAAAAGTTTCAAGTTGCTGTAAATGAGGAATTTGTACAAAAATCGGAT
    TTCATTCAACCTAATGATACTGTTGCATTAATTCCACCGGTTAGTGGAGGTTAA
    60
    120
    180
    234

⊟Protein[edit | edit source]

Protein Data Bank: 2Q5W
Protein Data Bank: 2QIE

⊟General[edit | edit source]

  • locus tag: SACOL2263 [new locus tag: SACOL_RS11900 ]
  • symbol: MoaD
  • description: molybdopterin converting factor subunit 1
  • length: 77
  • theoretical pI: 4.19545
  • theoretical MW: 8871.09
  • GRAVY: -0.172727

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdopterin converting factor, subunit 1 (TIGR01682; HMM-score: 76.7)
    and 2 more
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin MoaD family protein (TIGR01687; HMM-score: 40.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiamine biosynthesis protein ThiS (TIGR01683; HMM-score: 16.2)
  • TheSEED  :
    • Molybdopterin synthase sulfur carrier subunit
    Cofactors, Vitamins, Prosthetic Groups, Pigments Folate and pterines Molybdenum cofactor biosynthesis  Molybdenum cofactor biosynthesis protein MoaD
  • PFAM:
    Ubiquitin (CL0072) ThiS; ThiS family (PF02597; HMM-score: 62.4)
    and 1 more
    NADP_Rossmann (CL0063) UDPG_MGDP_dh_N; UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain (PF03721; HMM-score: 11.9)

⊟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): 0.00173
    • TAT(Tat/SPI): 0.00019
    • LIPO(Sec/SPII): 0.000286
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKVLYFAEIKDILQKAQEDIVLEQALTVQQFEDLLFERYPQINNKKFQVAVNEEFVQKSDFIQPNDTVALIPPVSGG

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1]
  • quantitative data / protein copy number per cell: 81 [2]
  • interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [3] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [3] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [3] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [3] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [3] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [3] (data from MRSA252)
    SACOL1477(ilvA1)threonine dehydratase  [3] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [3] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [3] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [3] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [3] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [3] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [3] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [3] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [3] (data from MRSA252)
    SACOL0015(rplI)50S ribosomal protein L9  [3] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [3] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [3] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [3] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [3] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [3] (data from MRSA252)
    SACOL2228(rplX)50S ribosomal protein L24  [3] (data from MRSA252)
    SACOL2112(rpmE2)50S ribosomal protein L31  [3] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [3] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [3] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [3] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [3] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [3] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [3] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [3] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [3] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [3] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [3] (data from MRSA252)
    SACOL0688ABC transporter substrate-binding protein  [3] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [3] (data from MRSA252)
    SACOL1759universal stress protein  [3] (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. ↑ 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)
  2. ↑ 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)
  3. ↑ 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 3.35 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)

⊟Relevant publications[edit | edit source]

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