From AureoWiki
Jump to: navigation, search

NCBI: 10-JUN-2013

Summary[edit source | edit]

  • 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 source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • 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 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
    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 source | edit]

Protein Data Bank: 3SJ7

General[edit source | edit]

  • 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 source | edit]

  • 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:
    MetabolismFatty acid and phospholipid metabolismBiosynthesis3-oxoacyl-[acyl-carrier-protein] reductase (TIGR01830; EC 1.1.1.100; HMM-score: 362.9)
    acetoacetyl-CoA reductase (TIGR01829; EC 1.1.1.36; HMM-score: 284.5)
    MetabolismFatty acid and phospholipid metabolismBiosynthesisputative 3-oxoacyl-(acyl-carrier-protein) reductase (TIGR01831; HMM-score: 242.1)
    3-hydroxybutyrate dehydrogenase (TIGR01963; HMM-score: 207)
    MetabolismEnergy metabolismFermentationacetoin reductases (TIGR02415; EC 1.1.1.-; HMM-score: 206.7)
    Unknown functionEnzymes of unknown specificitySDR family mycofactocin-dependent oxidoreductase (TIGR03971; EC 1.1.99.-; HMM-score: 204.9)
    MetabolismEnergy metabolismBiosynthesis and degradation of polysaccharides2-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 functionEnzymes of unknown specificitySDR 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)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersChlorophyll and bacteriochlorphylllight-dependent protochlorophyllide reductase (TIGR01289; EC 1.3.1.33; HMM-score: 23.1)
    methylmalonyl-CoA mutase C-terminal domain (TIGR00640; HMM-score: 17.8)
    MetabolismEnergy metabolismSugarsUDP-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)
    MetabolismTransport and binding proteinsCarbohydrates, organic alcohols, and acidstricarboxylate carrier (TIGR00798; HMM-score: 11.8)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersThiamineglycine oxidase ThiO (TIGR02352; EC 1.4.3.19; HMM-score: 11.4)
  • TheSEED:  
    Fatty Acids, Lipids, and IsoprenoidsFatty acidsFatty Acid Biosynthesis FASII 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) 
    COG1399 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)
    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 definedSPOR; 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 & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SACOL0593(fusA)elongation factor G  [1] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [1] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [1] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [1] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [1] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [1] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.199
    • Ymax_pos: 24
    • Cmax: 0.175
    • Cmax_pos: 65
    • Smax: 0.549
    • Smax_pos: 19
    • Smean: 0.314
    • D: 0.244
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MTKSALVTGASRGIGRSIALQLAEEGYNVAVNYAGSKEKAEAVVEEIKAKGVDSFAIQANVADADEVKAMIKEVVSQFGSLDVLVNNAGITRDNLLMRMKEQEWDDVIDTNLKGVFNCIQKATPQMLRQRSGAIINLSSVVGAVGNPGQANYVATKAGVIGLTKSAARELASRGITVNAVAPGFIVSDMTDALSDELKEQMLTQIPLARFGQDTDIANTVAFLASDKAKYITGQTIHVNGGMYM

Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4] [5]
    quantitative data / protein copy number per cell: 1354 [6]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator: SACOL1242 (FapR*)
    FapR* (TF) important in Fatty acid biosynthesis  RegPrecise    transcription unit transferred from N315 data RegPrecise

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: 47.83 h [7]

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. 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)
  3. 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)
  4. 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)
  5. 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)
  6. 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)
  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 source | edit]