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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00471
  • pan locus tag?: SAUPAN002239000
  • symbol: glmU
  • pan gene symbol?: glmU
  • synonym:
  • product: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_00471
  • symbol: glmU
  • product: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase
  • replicon: chromosome
  • strand: +
  • coordinates: 469575..470927
  • length: 1353
  • 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
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    ATGCGAAGACACGCGATAATTTTGGCAGCAGGTAAAGGCACAAGAATGAAATCTAAAAAG
    TATAAAGTGCTACACGAGGTTGCTGGGAAACCTATGGTCGAACATGTATTGGAAAGTGTG
    AAAGGCTCTGGTGTCGATCAAGTTGTAACCATCGTAGGACATGGTGCTGAAAGTGTAAAA
    GGACATTTAGGCGAGCGTTCTTTATACAGTTTTCAAGAGGAACAACTCGGTACTGCGCAT
    GCAGTGCAAATGGCGAAATCACACTTAGAAGACAAGGAAGGTACGACAATCGTTGTATGT
    GGTGACACACCGCTCATCACAAAGGAAACATTAGTAACATTGATTGCGCATCACGAGGAT
    GCTAATGCTCAAGCAACTGTATTATCTGCATCGATTCAACAACCATATGGATACGGAAGA
    ATCGTTCGAAATGCGTCAGGTCGTTTAGAACGCATAGTTGAAGAGAAAGATGCAACGCAA
    GCTGAAAAGGATATTAATGAAATTAGTTCAGGTATTTTTGCGTTTAATAATAAAACGTTG
    TTTGAAAAATTAACACAAGTGAAAAATGATAATGCGCAAGGTGAATATTACCTCCCTGAT
    GTATTGTCGTTAATTTTAAATGATGGCGGCATCGTAGAAGTCTATCGTACCAATGATGTT
    GAAGAAATCATGGGTGTAAATGATCGTGTAATGCTTAGTCAGGCTGAGAAGGCGATGCAA
    CGTCGTACGAATCATTATCACATGCTAAATGGTGTGACAATCATCGATCCTGACAGCACT
    TATATTGGTCCAGACGTTACAATTGGTAGTGATACAGTCATTGAACCAGGCGTACGAATT
    AATGGTCGTACAGAAATTGGCGAAGATGTTGTTATTGGTCAGTACTCTGAAATTAACAAT
    AGTACGATTGAAAATGGTGCATGTATTCAACAGTCTGTTGTTAATGATGCTAGCGTAGGA
    GCGAATACTAAGGTCGGACCGTTTGCGCAATTGAGACCAGGCGCGCAATTAGGTGCAGAT
    GTTAAGGTTGGAAATTTTGTAGAAATTAAAAAAGCAGATCTTAAAGATGGTGCCAAGGTT
    TCACATTTAAGTTATATTGGCGATGCTGTAATTGGCGAACGTACTAATATTGGTTGCGGA
    ACGATTACAGTTAACTATGATGGTGAAAATAAATTTAAAACTATCGTCGGCAAAGATTCA
    TTTGTAGGTTGCAATGTTAATTTAGTAGCACCTGTAACAATTGGTGATGATGTATTGGTG
    GCAGCTGGTTCCACAATCACAGATGACGTACCAAATGACAGTTTAGCTGTGGCAAGAGCA
    AGACAAACAACAAAAGAAGGATATAGGAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1353

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_00471
  • symbol: GlmU
  • description: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase
  • length: 450
  • theoretical pI: 5.6261
  • theoretical MW: 48502.4
  • GRAVY: -0.248667

⊟Function[edit | edit source]

  • reaction:
    EC 2.7.7.23?  ExPASy
    UDP-N-acetylglucosamine diphosphorylase UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
    EC 2.3.1.157?  ExPASy
    Glucosamine-1-phosphate N-acetyltransferase Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
  • TIGRFAM:
    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: 587.6)
    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: 587.6)
    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: 587.6)
    and 25 more
    UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR03992; EC 2.3.1.157,2.7.7.23; HMM-score: 204.4)
    glucose-1-phosphate thymidylyltransferase (TIGR01208; EC 2.7.7.24; HMM-score: 93)
    sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family (TIGR03570; HMM-score: 62.9)
    molybdenum cofactor cytidylyltransferase (TIGR03310; EC 2.7.7.76; HMM-score: 55.3)
    Metabolism Energy metabolism Biosynthesis and degradation of polysaccharides glucose-1-phosphate adenylyltransferase (TIGR02091; EC 2.7.7.27; HMM-score: 43.7)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase (TIGR01852; EC 2.3.1.129; HMM-score: 41.9)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD (TIGR01853; EC 2.3.1.191; HMM-score: 41.5)
    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: 40.7)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides UTP--glucose-1-phosphate uridylyltransferase (TIGR01099; EC 2.7.7.9; HMM-score: 38.4)
    Hypothetical proteins Conserved TIGR00454 family protein (TIGR00454; HMM-score: 36.3)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides glucose-1-phosphate thymidylyltransferase (TIGR01207; EC 2.7.7.24; HMM-score: 36.2)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides 3-deoxy-D-manno-octulosonate cytidylyltransferase (TIGR00466; EC 2.7.7.38; HMM-score: 35.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdenum cofactor guanylyltransferase (TIGR02665; EC 2.7.7.77; HMM-score: 35.3)
    colanic acid biosynthesis acetyltransferase WcaB (TIGR04016; EC 2.3.1.-; HMM-score: 27.2)
    Cell structure Cell envelope Biosynthesis and degradation of murein sacculus and peptidoglycan UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR03991; EC 2.3.1.157,2.7.7.23; HMM-score: 26.6)
    Metabolism Central intermediary metabolism Amino sugars UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR03991; EC 2.3.1.157,2.7.7.23; HMM-score: 26.6)
    phosphonate metabolim protein, transferase hexapeptide repeat family (TIGR03308; HMM-score: 26.5)
    2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase (TIGR03532; EC 2.3.1.89; HMM-score: 26.1)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides glucose-1-phosphate cytidylyltransferase (TIGR02623; EC 2.7.7.33; HMM-score: 24.1)
    non-ribosomal peptide synthetase terminal domain of unknown function (TIGR02353; HMM-score: 20.9)
    Metabolism Amino acid biosynthesis Serine family serine O-acetyltransferase (TIGR01172; EC 2.3.1.30; HMM-score: 19.7)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other 2-phospho-L-lactate guanylyltransferase (TIGR03552; EC 2.7.7.68; HMM-score: 17.4)
    Metabolism Energy metabolism Other phenylacetic acid degradation protein PaaY (TIGR02287; HMM-score: 17.3)
    xanthine dehydrogenase accessory protein pucB (TIGR03202; HMM-score: 17)
    colanic acid biosynthesis acetyltransferase WcaF (TIGR04008; EC 2.3.1.-; HMM-score: 16.5)
  • TheSEED  :
    • Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)
    • N-acetylglucosamine-1-phosphate uridyltransferase (EC 2.7.7.23)
    Cell Wall and Capsule Capsular and extracellular polysacchrides Sialic Acid Metabolism  Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)
    and 5 more
    Cell Wall and Capsule Capsular and extracellular polysacchrides Sialic Acid Metabolism  N-acetylglucosamine-1-phosphate uridyltransferase (EC 2.7.7.23)
    Cell Wall and Capsule Cell Wall and Capsule - no subcategory Peptidoglycan Biosynthesis  Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)
    Cell Wall and Capsule Cell Wall and Capsule - no subcategory Peptidoglycan Biosynthesis  N-acetylglucosamine-1-phosphate uridyltransferase (EC 2.7.7.23)
    Cell Wall and Capsule Cell Wall and Capsule - no subcategory UDP-N-acetylmuramate from Fructose-6-phosphate Biosynthesis  Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)
    Cell Wall and Capsule Cell Wall and Capsule - no subcategory UDP-N-acetylmuramate from Fructose-6-phosphate Biosynthesis  N-acetylglucosamine-1-phosphate uridyltransferase (EC 2.7.7.23)
  • PFAM:
    HEXAPEP (CL0536) Hexapep; Bacterial transferase hexapeptide (six repeats) (PF00132; HMM-score: 99.8)
    GT-A (CL0110) NTP_transferase; Nucleotidyl transferase (PF00483; HMM-score: 82.3)
    and 5 more
    NTP_transf_3; MobA-like NTP transferase domain (PF12804; HMM-score: 78.1)
    HEXAPEP (CL0536) Hexapep_2; Hexapeptide repeat of succinyl-transferase (PF14602; HMM-score: 38)
    GT-A (CL0110) IspD; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (PF01128; HMM-score: 35.9)
    CTP_transf_3; Cytidylyltransferase (PF02348; HMM-score: 32.1)
    CofC; Guanylyl transferase CofC like (PF01983; HMM-score: 14.9)

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

  • domains:
  • modifications:
  • cofactors: Mg2+
  • 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): 0.01358
    • TAT(Tat/SPI): 0.000791
    • LIPO(Sec/SPII): 0.002605
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MRRHAIILAAGKGTRMKSKKYKVLHEVAGKPMVEHVLESVKGSGVDQVVTIVGHGAESVKGHLGERSLYSFQEEQLGTAHAVQMAKSHLEDKEGTTIVVCGDTPLITKETLVTLIAHHEDANAQATVLSASIQQPYGYGRIVRNASGRLERIVEEKDATQAEKDINEISSGIFAFNNKTLFEKLTQVKNDNAQGEYYLPDVLSLILNDGGIVEVYRTNDVEEIMGVNDRVMLSQAEKAMQRRTNHYHMLNGVTIIDPDSTYIGPDVTIGSDTVIEPGVRINGRTEIGEDVVIGQYSEINNSTIENGACIQQSVVNDASVGANTKVGPFAQLRPGAQLGADVKVGNFVEIKKADLKDGAKVSHLSYIGDAVIGERTNIGCGTITVNYDGENKFKTIVGKDSFVGCNVNLVAPVTIGDDVLVAAGSTITDDVPNDSLAVARARQTTKEGYRK

⊟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. ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 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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