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NCBI: 02-MAR-2017

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA_RS02635 [old locus tag: SA0457 ]
  • pan locus tag?: SAUPAN002239000
  • symbol: SA_RS02635
  • 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: SA_RS02635 [old locus tag: SA0457 ]
  • symbol: SA_RS02635
  • product: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase
  • replicon: chromosome
  • strand: +
  • coordinates: 527067..528419
  • length: 1353
  • essential: yes DEG other strains

⊟Accession numbers[edit | edit source]

  • Location: NC_002745 (527067..528419) NCBI
  • BioCyc: SA_RS02635 BioCyc
  • MicrobesOnline: see SA0457

⊟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
    GGACATTTAGGCGAGCGTTCTTTATACAGTTTTCAAGAGAAACAACTCGGTACTGCGCAT
    GCAGTGCAAATGGCGAAATCACACTTAGAAGACAAGGAAGGTACGACAATCGTTGTATGT
    GGTGACACACCGCTCATCACAAAGGAAACATTAGAAACATTGATTGCGCATCATGAGGAT
    GCTAATGCTCAAGCAACTGTATTATCTGCATCGATTCAACAACCATATGGATACGGAAGA
    ATCGTTCGAAATGCGTCAGGTCGTTTAGAACGCATAGTTGAAGAGAAAGATGCAACGCAA
    GCTGAAAAGGATATTAATGAAATTAGTTCAGGTATTTTTGCGTTTAATAATAAAACGTTG
    TTTGAAAAATTAACACAAGTGAAAAATGATAATGCGCAAGGTGAATATTACCTCCCTGAT
    GTATTGTCGTTAATTTTAAATGATGGCGGCATCGTAGAAGTGTATCGTACCAATGATGTT
    GAAGAAATCATGGGTGTAAATGATCGTGTAATGCTTAGTCAGGCTGAGAAGGCGATGCAA
    CGTCGTACGAATCATTATCACATGCTAAATGGTGTGACAATCATCGATCCTGACAGCACT
    TTTATTGGTCCAGACGTTACAATTGGTAGTGATACAGTCATTGAACCAGGCGTACGAATT
    AATGGTCGTACAGAAATTGGCGAAGATGTTGTTATTGGTCAGTACTCTGAAATTAACAAT
    AGTACGATTGAAAATGGTGCATGTATTCAACAGTCTGTTGTTAATGATGCTAGCGTAGGA
    GCTAATACTAAGGTCGGACCGTTTGCGCAATTGAGACCAGGCGCGCAATTAGGTGCAGAT
    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: SA_RS02635 [old locus tag: SA0457 ]
  • symbol: SA_RS02635
  • description: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase
  • length: 450
  • theoretical pI: 5.79238
  • theoretical MW: 48515.4
  • GRAVY: -0.257556

⊟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: 589.4)
    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: 589.4)
    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: 589.4)
    and 25 more
    UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase (TIGR03992; EC 2.3.1.157,2.7.7.23; HMM-score: 205.1)
    glucose-1-phosphate thymidylyltransferase (TIGR01208; EC 2.7.7.24; HMM-score: 94.7)
    sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family (TIGR03570; HMM-score: 62.6)
    molybdenum cofactor cytidylyltransferase (TIGR03310; EC 2.7.7.76; HMM-score: 57.8)
    Metabolism Energy metabolism Biosynthesis and degradation of polysaccharides glucose-1-phosphate adenylyltransferase (TIGR02091; EC 2.7.7.27; HMM-score: 46.5)
    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: 42.8)
    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: 41.2)
    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: 38.7)
    Hypothetical proteins Conserved TIGR00454 family protein (TIGR00454; HMM-score: 38.4)
    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: 37.4)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides glucose-1-phosphate thymidylyltransferase (TIGR01207; EC 2.7.7.24; HMM-score: 37.2)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Molybdopterin molybdenum cofactor guanylyltransferase (TIGR02665; EC 2.7.7.77; HMM-score: 36.3)
    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: 36.1)
    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: 27.3)
    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: 27.3)
    colanic acid biosynthesis acetyltransferase WcaB (TIGR04016; EC 2.3.1.-; HMM-score: 27.2)
    phosphonate metabolim protein, transferase hexapeptide repeat family (TIGR03308; HMM-score: 26.3)
    2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase (TIGR03532; EC 2.3.1.89; HMM-score: 25.5)
    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: 20.7)
    Metabolism Amino acid biosynthesis Serine family serine O-acetyltransferase (TIGR01172; EC 2.3.1.30; HMM-score: 19.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other 2-phospho-L-lactate guanylyltransferase (TIGR03552; EC 2.7.7.68; HMM-score: 19.5)
    xanthine dehydrogenase accessory protein pucB (TIGR03202; HMM-score: 18.8)
    Metabolism Energy metabolism Other phenylacetic acid degradation protein PaaY (TIGR02287; HMM-score: 17.4)
    colanic acid biosynthesis acetyltransferase WcaF (TIGR04008; EC 2.3.1.-; HMM-score: 16.4)
  • TheSEED: see SA0457
  • PFAM:
    HEXAPEP (CL0536) Hexapep; Bacterial transferase hexapeptide (six repeats) (PF00132; HMM-score: 97)
    GT-A (CL0110) NTP_transferase; Nucleotidyl transferase (PF00483; HMM-score: 84.2)
    NTP_transf_3; MobA-like NTP transferase domain (PF12804; HMM-score: 80.1)
    and 4 more
    HEXAPEP (CL0536) Hexapep_2; Hexapeptide repeat of succinyl-transferase (PF14602; HMM-score: 37.7)
    GT-A (CL0110) IspD; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (PF01128; HMM-score: 36.6)
    CTP_transf_3; Cytidylyltransferase (PF02348; HMM-score: 32.2)
    CofC; Guanylyl transferase CofC like (PF01983; HMM-score: 17.3)

⊟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:
  • 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]

  • MRRHAIILAAGKGTRMKSKKYKVLHEVAGKPMVEHVLESVKGSGVDQVVTIVGHGAESVKGHLGERSLYSFQEKQLGTAHAVQMAKSHLEDKEGTTIVVCGDTPLITKETLETLIAHHEDANAQATVLSASIQQPYGYGRIVRNASGRLERIVEEKDATQAEKDINEISSGIFAFNNKTLFEKLTQVKNDNAQGEYYLPDVLSLILNDGGIVEVYRTNDVEEIMGVNDRVMLSQAEKAMQRRTNHYHMLNGVTIIDPDSTFIGPDVTIGSDTVIEPGVRINGRTEIGEDVVIGQYSEINNSTIENGACIQQSVVNDASVGANTKVGPFAQLRPGAQLGADVKVGNFVEIKKADLKDGAKVSHLSYIGDAVIGERTNIGCGTITVNYDGENKFKTIVGKDSFVGCNVNLVAPVTIGDDVLVAAGSTITDDVPNDSLAVARARQTTKEGYRK

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA_RS01275formate acetyltransferase  [1] (data from MRSA252)
    SA_RS0290550S ribosomal protein L11  [1] (data from MRSA252)
    SA_RS0292050S ribosomal protein L7/L12  [1] (data from MRSA252)
    SA_RS02960elongation factor Tu  [1] (data from MRSA252)
    SA_RS04575NADH dehydrogenase  [1] (data from MRSA252)
    SA_RS05350pyruvate dehydrogenase E1 component subunit alpha  [1] (data from MRSA252)
    SA_RS05355pyruvate dehydrogenase E1 component subunit beta  [1] (data from MRSA252)
    SA_RS05360dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex  [1] (data from MRSA252)
    SA_RS07385DNA-binding protein HU  [1] (data from MRSA252)
    SA_RS0829550S ribosomal protein L21  [1] (data from MRSA252)
    SA_RS08545isocitrate dehydrogenase (NADP(+))  [1] (data from MRSA252)
    SA_RS11430Asp23/Gls24 family envelope stress response protein  [1] (data from MRSA252)
    SA_RS1160030S ribosomal protein S9  [1] (data from MRSA252)
    SA_RS1168030S ribosomal protein S5  [1] (data from MRSA252)
    SA_RS1170550S ribosomal protein L5  [1] (data from MRSA252)
    SA_RS13920arginine deiminase  [1] (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. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 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]

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