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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1245 [new locus tag: SACOL_RS06365 ]
  • pan locus tag?: SAUPAN003515000
  • symbol: fabG1
  • pan gene symbol?: fabG
  • synonym:
  • product: 3-oxoacyl-ACP reductase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1245 [new locus tag: SACOL_RS06365 ]
  • symbol: fabG1
  • product: 3-oxoacyl-ACP reductase
  • replicon: chromosome
  • strand: +
  • coordinates: 1254334..1255068
  • length: 735
  • 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
    ATGACTAAGAGTGCTTTAGTAACAGGTGCATCAAGAGGAATTGGACGTAGTATTGCGTTA
    CAATTAGCAGAAGAAGGATATAATGTAGCAGTAAACTATGCAGGCAGCAAAGAGAAAGCT
    GAAGCAGTAGTCGAAGAAATCAAAGCTAAAGGTGTTGACAGTTTTGCGATTCAAGCAAAT
    GTTGCCGATGCTGATGAAGTTAAAGCAATGATTAAAGAAGTAGTTAGCCAATTTGGTTCT
    TTAGATGTTTTAGTAAATAATGCAGGTATTACTCGCGATAATTTATTAATGCGTATGAAA
    GAACAAGAGTGGGATGATGTTATTGACACAAACTTAAAAGGTGTATTTAACTGTATCCAA
    AAAGCAACACCACAAATGTTAAGACAACGTAGTGGTGCTATCATCAATTTATCAAGTGTT
    GTTGGAGCAGTAGGTAATCCGGGACAAGCAAACTATGTTGCAACAAAAGCAGGTGTTATT
    GGTTTAACTAAATCTGCGGCGCGTGAATTAGCATCTCGTGGTATCACTGTAAATGCAGTT
    GCACCTGGTTTTATTGTTTCTGATATGACAGATGCTTTAAGTGATGAGCTTAAAGAACAA
    ATGTTGACTCAAATTCCGTTAGCACGTTTTGGTCAAGACACAGATATTGCTAATACAGTA
    GCGTTCTTAGCATCAGACAAAGCAAAATATATTACAGGTCAAACAATCCATGTAAATGGT
    GGAATGTACATGTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    735

⊟Protein[edit | edit source]

Protein Data Bank: 3SJ7

⊟General[edit | edit source]

  • locus tag: SACOL1245 [new locus tag: SACOL_RS06365 ]
  • symbol: FabG1
  • description: 3-oxoacyl-ACP reductase
  • length: 244
  • theoretical pI: 5.10093
  • theoretical MW: 25886.4
  • GRAVY: 0.0172131

⊟Function[edit | edit source]

  • reaction:
    EC 1.1.1.100?  ExPASy
    3-oxoacyl-[acyl-carrier-protein] reductase (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH
  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase (TIGR01830; EC 1.1.1.100; HMM-score: 362.9)
    and 19 more
    acetoacetyl-CoA reductase (TIGR01829; EC 1.1.1.36; HMM-score: 284.5)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis putative 3-oxoacyl-(acyl-carrier-protein) reductase (TIGR01831; HMM-score: 242.1)
    3-hydroxybutyrate dehydrogenase (TIGR01963; HMM-score: 207)
    Metabolism Energy metabolism Fermentation acetoin reductases (TIGR02415; EC 1.1.1.-; HMM-score: 206.7)
    Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR03971; EC 1.1.99.-; HMM-score: 204.9)
    Metabolism Energy metabolism Biosynthesis and degradation of polysaccharides 2-deoxy-D-gluconate 3-dehydrogenase (TIGR01832; EC 1.1.1.125; HMM-score: 197.2)
    2-hydroxycyclohexanecarboxyl-CoA dehydrogenase (TIGR03206; EC 1.1.1.-; HMM-score: 167.2)
    2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (TIGR04316; EC 1.3.1.28; HMM-score: 162.7)
    Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR04504; EC 1.1.99.-; HMM-score: 140.8)
    pteridine reductase (TIGR02685; EC 1.5.1.33; HMM-score: 131.8)
    rhamnulose-1-phosphate aldolase/alcohol dehydrogenase (TIGR02632; EC 1.1.1.1,4.1.2.19; HMM-score: 117.4)
    cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (TIGR03325; EC 1.3.1.56; HMM-score: 90.5)
    sepiapterin reductase (TIGR01500; EC 1.1.1.153; HMM-score: 35.7)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll light-dependent protochlorophyllide reductase (TIGR01289; EC 1.3.1.33; HMM-score: 23.1)
    methylmalonyl-CoA mutase C-terminal domain (TIGR00640; HMM-score: 17.8)
    Metabolism Energy metabolism Sugars UDP-glucose 4-epimerase GalE (TIGR01179; EC 5.1.3.2; HMM-score: 15)
    NAD dependent epimerase/dehydratase, LLPSF_EDH_00030 family (TIGR04180; HMM-score: 13.3)
    Metabolism Transport and binding proteins Carbohydrates, organic alcohols, and acids tricarboxylate carrier (TIGR00798; HMM-score: 11.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine glycine oxidase ThiO (TIGR02352; EC 1.4.3.19; HMM-score: 11.4)
  • TheSEED  :
    • 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100)
    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_C2; Enoyl-(Acyl carrier protein) reductase (PF13561; HMM-score: 244.9)
    adh_short; short chain dehydrogenase (PF00106; HMM-score: 219.3)
    and 8 more
    KR; KR domain (PF08659; HMM-score: 82.8)
    Epimerase; NAD dependent epimerase/dehydratase family (PF01370; HMM-score: 21.2)
    F420_oxidored; NADP oxidoreductase coenzyme F420-dependent (PF03807; HMM-score: 18.3)
    NAD_binding_2; NAD binding domain of 6-phosphogluconate dehydrogenase (PF03446; HMM-score: 14.8)
    NmrA; NmrA-like family (PF05368; HMM-score: 14)
    NAD_binding_10; NAD(P)H-binding (PF13460; HMM-score: 13.3)
    no clan defined SPOR; Sporulation related domain (PF05036; HMM-score: 13)
    NADP_Rossmann (CL0063) 3Beta_HSD; 3-beta hydroxysteroid dehydrogenase/isomerase family (PF01073; HMM-score: 12.7)

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

  • domains:
  • modifications:
  • cofactors:
  • 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): 0.019676
    • TAT(Tat/SPI): 0.002441
    • LIPO(Sec/SPII): 0.003352
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTKSALVTGASRGIGRSIALQLAEEGYNVAVNYAGSKEKAEAVVEEIKAKGVDSFAIQANVADADEVKAMIKEVVSQFGSLDVLVNNAGITRDNLLMRMKEQEWDDVIDTNLKGVFNCIQKATPQMLRQRSGAIINLSSVVGAVGNPGQANYVATKAGVIGLTKSAARELASRGITVNAVAPGFIVSDMTDALSDELKEQMLTQIPLARFGQDTDIANTVAFLASDKAKYITGQTIHVNGGMYM

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1354 [5]
  • interaction partners:
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: FapR* (repression) regulon
    FapR*(TF)important in Fatty acid biosynthesis; RegPrecise    transcription unit transferred from N315 data RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 47.83 h [7]

⊟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. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 6.6 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)
  7. ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
    Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
    Mol Cell Proteomics: 2012, 11(9);558-70
    [PubMed:22556279] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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