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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0988 [new locus tag: SACOL_RS05055 ]
  • pan locus tag?: SAUPAN003128000
  • symbol: fabF
  • pan gene symbol?: fabF
  • synonym:
  • product: 3-oxoacyl-ACP synthase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0988 [new locus tag: SACOL_RS05055 ]
  • symbol: fabF
  • product: 3-oxoacyl-ACP synthase
  • replicon: chromosome
  • strand: +
  • coordinates: 995709..996953
  • length: 1245
  • 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
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    ATGAGTCAAAATAAAAGAGTAGTTATTACAGGTATGGGAGCCCTTTCTCCAATCGGTAAT
    GATGTCAAAACAACATGGGAGAATGCTCTAAAAGGCGTAAATGGTATCGATAAAATTACA
    CGTATCGATACTGAACCTTATAGCGTTCACTTAGCAGGAGAACTTAAAAACTTTAATATT
    GAAGATCATATCGACAAAAAAGAAGCGCGTCGTATGGATAGATTTACTCAATATGCAATT
    GTAGCAGCTAGAGAGGCTGTTAAAGATGCGCAATTAGATATCAATGAAAATACTGCAGAT
    CGAATCGGTGTATGGATTGGTTCTGGTATCGGTGGTATGGAAACATTTGAAATTGCACAT
    AAACAATTAATGGATAAAGGCCCAAGACGTGTGAGTCCATTTTTCGTACCAATGTTAATT
    CCTGATATGGCAACTGGGCAAGTATCAATTGACTTAGGTGCAAAAGGACCAAATGGTGCA
    ACAGTTACAGCATGTGCAACAGGTACAAATTCAATCGGAGAAGCATTTAAAATTGTGCAA
    CGCGGTGATGCAGATGCAATGATTACTGGTGGTACAGAAGCACCAATTACTCATATGGCA
    ATTGCTGGTTTCAGTGCAAGTCGAGCGCTTTCTACAAATGATGACATTGAAACAGCATGT
    CGTCCATTCCAAGAAGGTAGAGATGGTTTTGTTATGGGTGAAGGTGCTGGTATTTTAGTA
    ATTGAATCTTTAGAATCAGCACAAGCTCGAGGTGCCAATATTTATGCTGAGATAGTTGGC
    TATGGTACTACAGGTGATGCTTATCATATTACAGCGCCAGCTCCAGAAGGTGAAGGTGGT
    TCTAGAGCAATGCAAGCAGCTATGGATGATGCTGGTATTGAACCTAAAGATGTACAATAC
    TTAAATGCCCATGGTACAAGTACTCCTGTTGGTGACTTAAATGAAGTTAAAGCTATTAAA
    AATACATTTGGTGAAGCAGCTAAACACTTAAAAGTTAGCTCAACAAAATCAATGACTGGT
    CACTTACTTGGTGCAACAGGTGGAATTGAAGCAATCTTCTCAGCGCTTTCAATTAAAGAC
    TCTAAAGTCGCACCGACAATTCATGCGGTAACACCAGATCCAGAATGTGATTTGGATATT
    GTTCCAAATGAAGCGCAAGACCTTGATATTACTTATGCAATGAGTAATAGCTTAGGATTC
    GGTGGACATAACGCAGTATTAGTATTCAAGAAATTTGAAGCATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1245

⊟Protein[edit | edit source]

Protein Data Bank: 2GQD

⊟General[edit | edit source]

  • locus tag: SACOL0988 [new locus tag: SACOL_RS05055 ]
  • symbol: FabF
  • description: 3-oxoacyl-ACP synthase
  • length: 414
  • theoretical pI: 4.82119
  • theoretical MW: 43739
  • GRAVY: -0.167633

⊟Function[edit | edit source]

  • reaction:
    EC 2.3.1.41?  ExPASy
    Beta-ketoacyl-[acyl-carrier-protein] synthase I Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]
    EC 2.3.1.179?  ExPASy
    Beta-ketoacyl-[acyl-carrier-protein] synthase II (Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]
  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis beta-ketoacyl-acyl-carrier-protein synthase II (TIGR03150; EC 2.3.1.179; HMM-score: 639.4)
    and 3 more
    polyketide-type polyunsaturated fatty acid synthase PfaA (TIGR02813; HMM-score: 106.6)
    Metabolism Fatty acid and phospholipid metabolism Other acetyl-CoA C-acyltransferase (TIGR01930; EC 2.3.1.16; HMM-score: 23.7)
    3-oxoadipyl-CoA thiolase (TIGR02430; EC 2.3.1.174; HMM-score: 12.7)
  • TheSEED  :
    • 3-oxoacyl-[acyl-carrier-protein] synthase, KASII (EC 2.3.1.179)
    Fatty Acids, Lipids, and Isoprenoids Fatty acids Fatty Acid Biosynthesis FASII  3-oxoacyl-[acyl-carrier-protein] synthase, KASII (EC 2.3.1.179)
  • PFAM:
    Thiolase (CL0046) ketoacyl-synt; Beta-ketoacyl synthase, N-terminal domain (PF00109; HMM-score: 208.5)
    and 2 more
    Ketoacyl-synt_C; Beta-ketoacyl synthase, C-terminal domain (PF02801; HMM-score: 130.9)
    Thiolase_N; Thiolase, N-terminal domain (PF00108; HMM-score: 16.1)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic Membrane
    • Cytoplasmic Score: 1.05
    • Cytoplasmic Membrane Score: 8.78
    • Cellwall Score: 0.08
    • Extracellular Score: 0.09
    • 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): 0.036712
    • TAT(Tat/SPI): 0.001296
    • LIPO(Sec/SPII): 0.00713
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSQNKRVVITGMGALSPIGNDVKTTWENALKGVNGIDKITRIDTEPYSVHLAGELKNFNIEDHIDKKEARRMDRFTQYAIVAAREAVKDAQLDINENTADRIGVWIGSGIGGMETFEIAHKQLMDKGPRRVSPFFVPMLIPDMATGQVSIDLGAKGPNGATVTACATGTNSIGEAFKIVQRGDADAMITGGTEAPITHMAIAGFSASRALSTNDDIETACRPFQEGRDGFVMGEGAGILVIESLESAQARGANIYAEIVGYGTTGDAYHITAPAPEGEGGSRAMQAAMDDAGIEPKDVQYLNAHGTSTPVGDLNEVKAIKNTFGEAAKHLKVSSTKSMTGHLLGATGGIEAIFSALSIKDSKVAPTIHAVTPDPECDLDIVPNEAQDLDITYAMSNSLGFGGHNAVLVFKKFEA

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1987 [5]
  • interaction partners:
    SACOL1385(acnA)aconitate hydratase  [6] (data from MRSA252)
    SACOL0451(ahpF)alkyl hydroperoxide reductase subunit F  [6] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [6] (data from MRSA252)
    SACOL0833(clpP)ATP-dependent Clp protease proteolytic subunit  [6] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [6] (data from MRSA252)
    SACOL1245(fabG1)3-oxoacyl-ACP reductase  [6] (data from MRSA252)
    SACOL2091(fabZ)(3R)-hydroxymyristoyl-ACP dehydratase  [6] (data from MRSA252)
    SACOL2117(fbaA)fructose-bisphosphate aldolase  [6] (data from MRSA252)
    SACOL2622(fdaB)fructose-1,6-bisphosphate aldolase  [6] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [6] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [6] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [6] (data from MRSA252)
    SACOL0961(gluD)glutamate dehydrogenase  [6] (data from MRSA252)
    SACOL0461(guaA)GMP synthase  [6] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [6] (data from MRSA252)
    SACOL0554(hpt)hypoxanthine phosphoribosyltransferase  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1288(infB)translation initiation factor IF-2  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [6] (data from MRSA252)
    SACOL0746(norR)MarR family transcriptional regulator  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL1005(pepF)oligoendopeptidase F  [6] (data from MRSA252)
    SACOL1746(pfkA)6-phosphofructokinase  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [6] (data from MRSA252)
    SACOL1982(ppaC)manganese-dependent inorganic pyrophosphatase  [6] (data from MRSA252)
    SACOL1091(ptsH)phosphocarrier protein HPr  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL0545(rplY)50S ribosomal protein L25/general stress protein Ctc  [6] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [6] (data from MRSA252)
    SACOL2225(rpsH)30S ribosomal protein S8  [6] (data from MRSA252)
    SACOL2240(rpsJ)30S ribosomal protein S10  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [6] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [6] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL1262(sucC)succinyl-CoA synthetase subunit beta  [6] (data from MRSA252)
    SACOL1831(tal)translaldolase  [6] (data from MRSA252)
    SACOL1722(tig)trigger factor  [6] (data from MRSA252)
    SACOL1377(tkt)transketolase  [6] (data from MRSA252)
    SACOL0840(tpiA)triosephosphate isomerase  [6] (data from MRSA252)
    SACOL1762(tpx)thiol peroxidase  [6] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [6] (data from MRSA252)
    SACOL02123-hydroxyacyl-CoA dehydrogenase  [6] (data from MRSA252)
    SACOL03035'-nucleotidase  [6] (data from MRSA252)
    SACOL0564pyridoxal biosynthesis lyase PdxS  [6] (data from MRSA252)
    SACOL0721hypothetical protein  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL0815ribosomal subunit interface protein  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL1020hypothetical protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [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: 31.1 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. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 6.38 6.39 6.40 6.41 6.42 6.43 6.44 6.45 6.46 6.47 6.48 6.49 6.50 6.51 6.52 6.53 6.54 6.55 6.56 6.57 6.58 6.59 6.60 6.61 6.62 6.63 6.64 6.65 6.66 6.67 6.68 6.69 6.70 6.71 6.72 6.73 6.74 6.75 6.76 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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