From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0543 [new locus tag: SACOL_RS02775 ]
  • 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: SACOL0543 [new locus tag: SACOL_RS02775 ]
  • symbol: glmU
  • product: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase
  • replicon: chromosome
  • strand: +
  • coordinates: 549902..551254
  • length: 1353
  • 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
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    ATGCGAAGACACGCGATAATTTTGGCAGCAGGTAAAGGCACAAGAATGAAATCTAAAAAG
    TATAAAGTGCTACACGAGGTTGCTGGGAAACCTATGGTCGAACATGTATTGGAAAGTGTG
    AAAGGCTCTGGTGTCGATCAAGTTGTAACCATCGTAGGACATGGTGCTGAAAGTGTAAAA
    GGACATTTAGGCGAGCGTTCTTTATACAGTTTTCAAGAGGAACAACTCGGTACTGCGCAT
    GCAGTGCAAATGGCGAAATCACACTTAGAAGACAAGGAAGGTACGACAATCGTTGTATGT
    GGTGACACACCGCTCATCACAAAGGAAACATTAGAAACATTGATTGCGCATCACGAGGAT
    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: SACOL0543 [new locus tag: SACOL_RS02775 ]
  • symbol: GlmU
  • description: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase
  • length: 450
  • theoretical pI: 5.47401
  • theoretical MW: 48532.4
  • GRAVY: -0.265778

⊟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: 590.2)
    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: 590.2)
    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: 590.2)
    and 25 more
    UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR03992; EC 2.3.1.157,2.7.7.23; HMM-score: 206.4)
    glucose-1-phosphate thymidylyltransferase (TIGR01208; EC 2.7.7.24; HMM-score: 94.2)
    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: 57.5)
    Metabolism Energy metabolism Biosynthesis and degradation of polysaccharides glucose-1-phosphate adenylyltransferase (TIGR02091; EC 2.7.7.27; HMM-score: 46.3)
    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: 42.7)
    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 UTP--glucose-1-phosphate uridylyltransferase (TIGR01099; EC 2.7.7.9; HMM-score: 39.5)
    Hypothetical proteins Conserved TIGR00454 family protein (TIGR00454; HMM-score: 38.6)
    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: 38.2)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides glucose-1-phosphate thymidylyltransferase (TIGR01207; EC 2.7.7.24; HMM-score: 37.1)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdenum cofactor guanylyltransferase (TIGR02665; EC 2.7.7.77; HMM-score: 36.6)
    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: 35.8)
    colanic acid biosynthesis acetyltransferase WcaB (TIGR04016; EC 2.3.1.-; HMM-score: 27.2)
    phosphonate metabolim protein, transferase hexapeptide repeat family (TIGR03308; HMM-score: 26.5)
    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: 26.2)
    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: 26.2)
    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: 25)
    non-ribosomal peptide synthetase terminal domain of unknown function (TIGR02353; HMM-score: 20.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other 2-phospho-L-lactate guanylyltransferase (TIGR03552; EC 2.7.7.68; HMM-score: 19.7)
    Metabolism Amino acid biosynthesis Serine family serine O-acetyltransferase (TIGR01172; EC 2.3.1.30; HMM-score: 19.6)
    xanthine dehydrogenase accessory protein pucB (TIGR03202; HMM-score: 18.7)
    Metabolism Energy metabolism Other phenylacetic acid degradation protein PaaY (TIGR02287; HMM-score: 17.3)
    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: 84.8)
    NTP_transf_3; MobA-like NTP transferase domain (PF12804; HMM-score: 80.8)
    and 5 more
    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: 36.8)
    CTP_transf_3; Cytidylyltransferase (PF02348; HMM-score: 32.9)
    CofC; Guanylyl transferase CofC like (PF01983; HMM-score: 17.1)
    DUF2064; Uncharacterized protein conserved in bacteria (DUF2064) (PF09837; HMM-score: 11.9)

⊟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]

  • MRRHAIILAAGKGTRMKSKKYKVLHEVAGKPMVEHVLESVKGSGVDQVVTIVGHGAESVKGHLGERSLYSFQEEQLGTAHAVQMAKSHLEDKEGTTIVVCGDTPLITKETLETLIAHHEDANAQATVLSASIQQPYGYGRIVRNASGRLERIVEEKDATQAEKDINEISSGIFAFNNKTLFEKLTQVKNDNAQGEYYLPDVLSLILNDGGIVEVYRTNDVEEIMGVNDRVMLSQAEKAMQRRTNHYHMLNGVTIIDPDSTYIGPDVTIGSDTVIEPGVRINGRTEIGEDVVIGQYSEINNSTIENGACIQQSVVNDASVGANTKVGPFAQLRPGAQLGADVKVGNFVEIKKADLKDGAKVSHLSYIGDAVIGERTNIGCGTITVNYDGENKFKTIVGKDSFVGCNVNLVAPVTIGDDVLVAAGSTITDDVPNDSLAVARARQTTKEGYRK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 305 [5]
  • interaction partners:
    SACOL2657(arcA)arginine deiminase  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (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. ↑ 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, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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)
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 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)

⊟Relevant publications[edit | edit source]

Retrieved from "http://aureowiki.med.uni-greifswald.de/index.php?title=SACOL0543&oldid=101149"