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NCBI: 03-AUG-2016

Summary[edit source | edit]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00722
  • pan locus tag?: SAUPAN002599000
  • symbol: SAOUHSC_00722
  • pan gene symbol?: pabA
  • synonym:
  • product: para-aminobenzoate synthase glutamine amidotransferase component II

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SAOUHSC_00722
  • symbol: SAOUHSC_00722
  • product: para-aminobenzoate synthase glutamine amidotransferase component II
  • replicon: chromosome
  • strand: +
  • coordinates: 705285..705878
  • length: 594
  • essential: no DEG other strains

Accession numbers[edit source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    ATGATTCTAGTCATAGATAATAATGATTCATTTACATATAATTTAATAGACTATATTAAG
    ACTCAAACGAAACTAACAGTTCAAGTTGTTGGTATTGATAATCTGCTGATAGAAGACGTC
    ATTAATATGAAGCCAAAAGCAATTGTTATTTCGCCTGGGCCGGGTAATCCGGATGATTAT
    CCTATCTTGAATGAAGTGTTAGAACAATTTTATCAGCGTGTACCTATACTAGGTGTATGT
    TTAGGATTTCAATGTATCGTGTCTTATTTTGGTGGAAATATCATTCACGGCTATCATCCT
    GTACACGGACATACTACACAGTTACGCCATACCAATGAAGGTATTTTTCAAGGACTGCCT
    CAAAATTTCAATGTAATGCGTTATCATTCATTAATTGCTGACGGAGCGACTTTTCCAAAT
    TGCTTAAAGATTACAGCAAAAAACGATGAAGCGATTATTATGGCATTTGAGCATATTAGA
    TTTCCGGTTTTTGGTGTGCAATATCATCCTGAATCTATTTTGAGTGAATACGGTTATCGA
    CAAGTTGAATTATTTTTATCGAAGGTAGGTGATTACTGTGAGAATAGAATATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    594

Protein[edit source | edit]

General[edit source | edit]

  • locus tag: SAOUHSC_00722
  • symbol: SAOUHSC_00722
  • description: para-aminobenzoate synthase glutamine amidotransferase component II
  • length: 197
  • theoretical pI: 5.79556
  • theoretical MW: 22377.5
  • GRAVY: 0.0126904

Function[edit source | edit]

  • reaction:
    EC 4.1.3.27?  ExPASy
    Anthranilate synthaseChorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
  • TIGRFAM:
    glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase (TIGR00566; HMM-score: 184.5)
    MetabolismAmino acid biosynthesisAromatic amino acid familyanthranilate synthase (TIGR01815; EC 4.1.3.27; HMM-score: 154.8)
    aminodeoxychorismate synthase (TIGR01823; EC 2.6.1.85; HMM-score: 140.2)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPurine ribonucleotide biosynthesisGMP synthase (glutamine-hydrolyzing), N-terminal domain (TIGR00888; EC 6.3.5.2; HMM-score: 90.5)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPyrimidine ribonucleotide biosynthesiscarbamoyl-phosphate synthase, small subunit (TIGR01368; EC 6.3.5.5; HMM-score: 62.5)
    MetabolismAmino acid biosynthesisHistidine familyimidazole glycerol phosphate synthase, glutamine amidotransferase subunit (TIGR01855; EC 2.4.2.-; HMM-score: 18.1)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPyrimidine ribonucleotide biosynthesisCTP synthase (TIGR00337; EC 6.3.4.2; HMM-score: 15.9)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPurine ribonucleotide biosynthesisphosphoribosylformylglycinamidine synthase I (TIGR01737; EC 6.3.5.3; HMM-score: 12.2)
  • TheSEED:  
    Amino Acids and DerivativesAromatic amino acids and derivativesTryptophan synthesis Para-aminobenzoate synthase, amidotransferase component (EC 2.6.1.85) 
    Cofactors, Vitamins, Prosthetic Groups, PigmentsFolate and pterinesFolate Biosynthesis Para-aminobenzoate synthase, amidotransferase component (EC 2.6.1.85) 
  • PFAM:
    Glutaminase_I (CL0014) GATase; Glutamine amidotransferase class-I (PF00117; HMM-score: 153.5)
    Peptidase_C26; Peptidase C26 (PF07722; HMM-score: 41.9)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SAOUHSC_02117(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [1] (data from MRSA252)
    SAOUHSC_01232(rpsB)30S ribosomal protein S2  [1] (data from MRSA252)
    SAOUHSC_02353(upp)uracil phosphoribosyltransferase  [1] (data from MRSA252)
    SAOUHSC_00206L-lactate dehydrogenase  [1] (data from MRSA252)
    SAOUHSC_01794glyceraldehyde 3-phosphate dehydrogenase 2  [1] (data from MRSA252)
    SAOUHSC_02849pyruvate oxidase  [1] (data from MRSA252)
    SAOUHSC_02860HMG-CoA synthase  [1] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.113
    • Ymax_pos: 51
    • Cmax: 0.108
    • Cmax_pos: 58
    • Smax: 0.179
    • Smax_pos: 43
    • Smean: 0.095
    • D: 0.106
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MILVIDNNDSFTYNLIDYIKTQTKLTVQVVGIDNLLIEDVINMKPKAIVISPGPGNPDDYPILNEVLEQFYQRVPILGVCLGFQCIVSYFGGNIIHGYHPVHGHTTQLRHTNEGIFQGLPQNFNVMRYHSLIADGATFPNCLKITAKNDEAIIMAFEHIRFPVFGVQYHPESILSEYGYRQVELFLSKVGDYCENRI

Experimental data[edit source | edit]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

Protein synthesis (provided by Aureolib)[edit source | edit]

Protein stability[edit source | edit]

  • half-life: no data available

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 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)
  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);3648-3661
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  3. 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 source | edit]