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NCBI: 03-AUG-2016

Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_02898
  • pan locus tag?: SAUPAN006253000
  • symbol: SAOUHSC_02898
  • pan gene symbol?: gbaB
  • synonym:
  • product: hypothetical protein

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_02898
  • symbol: SAOUHSC_02898
  • product: hypothetical protein
  • replicon: chromosome
  • strand: +
  • coordinates: 2667540..2668244
  • length: 705
  • essential: no 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
    ATGACTAAAATTGTGTTAATCACAGGAGGCAATAAAGGGTTAGGCTATGCAAGTGCAGAG
    GCACTTAAAGCATTGGGTTACAAAGTTTATATAGGTTCTCGGAATGATGTAAGAGGACAA
    CAAGCATCACAAAAATTAGGTGTTCATTATGTACAATTAGATGTTACAAGTGACTACTCA
    GTCAAAAATGCTTATAACATGATTGCTGAAAAAGAAGGCCGTCTTGATATCCTCATTAAC
    AATGCAGGTATATCTGGTCAATTTTCAGCACCTTCCAAATTGACACCTCGTGACGTTGAA
    GAAGTATATCAAACGAATGTATTCGGTATCGTACGAATGATGAATACATTCGTCCCTCTC
    TTAGAAAAATCTGAACAACCTGTTGTCGTCAACGTATCAAGTGGTTTAGGTTCATTTGGA
    ATGGTTACAAACCCCGAAACAGCTGAATCTAAAGTGAATTCATTAGCTTATTGTTCGTCT
    AAATCGGCAGTAACAATGCTAACGCTACAATACGCTAAAGGATTACCTAACATGCAAATC
    AATGCTGCTGATCCAGGCGCTACAAATACTGATTTAGTTGGTGATTTTAGTAATAATTCC
    AAACACGTTTCTGAAGGAATCAAGCCAATCATTCAATTAGCAACGATTGGTGCAGATGGC
    CCAACAGGTACATTTATTAATGGCGATGGAGAGATGCCTTGGTAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    705

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SAOUHSC_02898
  • symbol: SAOUHSC_02898
  • description: hypothetical protein
  • length: 234
  • theoretical pI: 5.80622
  • theoretical MW: 24931.1
  • GRAVY: -0.126923

Function[edit | edit source]

  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase (TIGR01830; EC 1.1.1.100; HMM-score: 79.9)
    2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (TIGR04316; EC 1.3.1.28; HMM-score: 79)
    Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR03971; EC 1.1.99.-; HMM-score: 69)
    Metabolism Energy metabolism Fermentation acetoin reductases (TIGR02415; EC 1.1.1.-; HMM-score: 64.8)
    acetoacetyl-CoA reductase (TIGR01829; EC 1.1.1.36; HMM-score: 64.1)
    and 12 more
    3-hydroxybutyrate dehydrogenase (TIGR01963; HMM-score: 62.9)
    Metabolism Energy metabolism Biosynthesis and degradation of polysaccharides 2-deoxy-D-gluconate 3-dehydrogenase (TIGR01832; EC 1.1.1.125; HMM-score: 58.1)
    cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (TIGR03325; EC 1.3.1.56; HMM-score: 49.1)
    Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR04504; EC 1.1.99.-; HMM-score: 47.3)
    2-hydroxycyclohexanecarboxyl-CoA dehydrogenase (TIGR03206; EC 1.1.1.-; HMM-score: 42.7)
    rhamnulose-1-phosphate aldolase/alcohol dehydrogenase (TIGR02632; EC 1.1.1.1,4.1.2.19; HMM-score: 36.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll light-dependent protochlorophyllide reductase (TIGR01289; EC 1.3.1.33; HMM-score: 34.4)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis putative 3-oxoacyl-(acyl-carrier-protein) reductase (TIGR01831; HMM-score: 33.3)
    sepiapterin reductase (TIGR01500; EC 1.1.1.153; HMM-score: 26.4)
    pteridine reductase (TIGR02685; EC 1.5.1.33; HMM-score: 16)
    Unknown function Enzymes of unknown specificity putative NAD(P)H quinone oxidoreductase, PIG3 family (TIGR02824; HMM-score: 13.5)
    Hypothetical proteins Conserved TIGR01777 family protein (TIGR01777; HMM-score: 12.1)
  • TheSEED  :
    • Oxidoreductase, short-chain dehydrogenase/reductase family
    Fatty Acids, Lipids, and Isoprenoids Fatty acids Fatty Acid Biosynthesis FASII  3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100)
  • PFAM:
    NADP_Rossmann (CL0063) adh_short; short chain dehydrogenase (PF00106; HMM-score: 135.4)
    and 6 more
    adh_short_C2; Enoyl-(Acyl carrier protein) reductase (PF13561; HMM-score: 93)
    KR; KR domain (PF08659; HMM-score: 39.4)
    Epimerase; NAD dependent epimerase/dehydratase family (PF01370; HMM-score: 17.6)
    ADH_zinc_N; Zinc-binding dehydrogenase (PF00107; HMM-score: 15.1)
    no clan defined PALP; Pyridoxal-phosphate dependent enzyme (PF00291; HMM-score: 14.5)
    GT-B (CL0113) Glyco_trans_4_2; Glycosyl transferase 4-like (PF13477; HMM-score: 13.9)

Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.67
    • Cytoplasmic Membrane Score: 0.01
    • Cellwall Score: 0.15
    • Extracellular Score: 0.17
    • 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): 0.030131
    • TAT(Tat/SPI): 0.001482
    • LIPO(Sec/SPII): 0.004751
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MTKIVLITGGNKGLGYASAEALKALGYKVYIGSRNDVRGQQASQKLGVHYVQLDVTSDYSVKNAYNMIAEKEGRLDILINNAGISGQFSAPSKLTPRDVEEVYQTNVFGIVRMMNTFVPLLEKSEQPVVVNVSSGLGSFGMVTNPETAESKVNSLAYCSSKSAVTMLTLQYAKGLPNMQINAADPGATNTDLVGDFSNNSKHVSEGIKPIIQLATIGADGPTGTFINGDGEMPW

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [1] [2]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • interaction partners:

Expression & Regulation[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. 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)
  2. 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)
  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 | edit source]