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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0557 [new locus tag: SACOL_RS02850 ]
  • pan locus tag?: SAUPAN002255000
  • symbol: cysK
  • pan gene symbol?: cysK
  • synonym:
  • product: cysteine synthase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0557 [new locus tag: SACOL_RS02850 ]
  • symbol: cysK
  • product: cysteine synthase
  • replicon: chromosome
  • strand: +
  • coordinates: 567101..568033
  • length: 933
  • 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
    ATGGCACAAAAACCAGTAGATAATATTACTCAAATTATTGGCGGTACACCGGTAGTCAAA
    TTGAGAAATGTAGTAGATGATAATGCAGCAGATGTTTATGTAAAATTGGAATATCAAAAT
    CCAGGTGGTTCTGTAAAGGATAGAATTGCTTTAGCAATGATTGAAAAAGCAGAGCGAGAA
    GGCAAAATTAAACCTGGCGATACAATTGTAGAACCAACAAGTGGTAATACAGGTATCGGT
    TTAGCATTTGTATGTGCTGCTAAAGGATATAAAGCAGTATTTACTATGCCCGAAACAATG
    AGCCAAGAGCGTCGTAATTTATTAAAAGCATACGGTGCGGAATTAGTTTTAACGCCTGGA
    TCAGAAGCGATGAAAGGTGCAATTAAAAAAGCTAAAGAATTGAAAGAAGAACATGGTTAC
    TTCGAGCCACAACAATTTGAAAACCCTGCGAACCCTGAAGTTCATGAGTTAACTACAGGT
    CCTGAGTTATTACAACAATTTGAAGGGAAAACTATCGATGCGTTCCTAGCTGGTGTTGGT
    ACTGGTGGTACGTTATCTGGTGTAGGTAAAGTTCTGAAAAAAGAATATCCTAACATCGAA
    ATTGTTGCTATAGAGCCTGAGGCTTCTCCAGTATTGAGCGGTGGTGAGCCAGGTCCACAT
    AAATTACAAGGTTTAGGTGCTGGATTTATTCCAGGCACTTTGAATACAGAAATCTATGAC
    AGTATTATTAAAGTAGGAAATGATACAGCGATGGAAATGTCTCGTCGAGTTGCTAAAGAG
    GAAGGTATTTTAGCAGGTATTTCATCAGGTGCTGCGATTTATGCTGCCATTCAAAAAGCA
    AAAGAATTAGGAAAAGGTAAAACAGTAGTAACAGTATTGCCGAGTAATGGTGAACGCTAC
    TTATCAACACCTTTATATTCATTCGATGACTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    933

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0557 [new locus tag: SACOL_RS02850 ]
  • symbol: CysK
  • description: cysteine synthase
  • length: 310
  • theoretical pI: 5.12885
  • theoretical MW: 32975.4
  • GRAVY: -0.237419

⊟Function[edit | edit source]

  • reaction:
    EC 2.5.1.47?  ExPASy
    Cysteine synthase O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
  • TIGRFAM:
    Metabolism Amino acid biosynthesis Serine family cysteine synthase A (TIGR01139; EC 2.5.1.47; HMM-score: 463.6)
    Metabolism Amino acid biosynthesis Serine family cysteine synthase (TIGR01136; EC 2.5.1.47; HMM-score: 440.6)
    and 12 more
    Metabolism Amino acid biosynthesis Serine family cystathionine beta-synthase (TIGR01137; EC 4.2.1.22; HMM-score: 326.6)
    Metabolism Amino acid biosynthesis Serine family cysteine synthase B (TIGR01138; EC 2.5.1.47; HMM-score: 293)
    Cellular processes Cellular processes Biosynthesis of natural products 2,3-diaminopropionate biosynthesis protein SbnA (TIGR03945; HMM-score: 245.2)
    Metabolism Amino acid biosynthesis Pyruvate family threonine ammonia-lyase, biosynthetic (TIGR01124; EC 4.3.1.19; HMM-score: 73.8)
    Metabolism Amino acid biosynthesis Pyruvate family threonine ammonia-lyase (TIGR01127; EC 4.3.1.19; HMM-score: 73.7)
    Metabolism Amino acid biosynthesis Pyruvate family threonine dehydratase (TIGR02079; EC 4.3.1.19; HMM-score: 72.7)
    ectoine utilization protein EutB (TIGR02991; HMM-score: 48)
    Metabolism Amino acid biosynthesis Aspartate family threonine synthase (TIGR00260; EC 4.2.3.1; HMM-score: 41.3)
    Metabolism Amino acid biosynthesis Aromatic amino acid family tryptophan synthase, beta subunit (TIGR00263; EC 4.2.1.20; HMM-score: 33.4)
    Unknown function Enzymes of unknown specificity pyridoxal-phosphate dependent TrpB-like enzyme (TIGR01415; HMM-score: 33.4)
    diaminopropionate ammonia-lyase (TIGR03528; EC 4.3.1.15; HMM-score: 23.2)
    Metabolism Energy metabolism Other diaminopropionate ammonia-lyase family (TIGR01747; EC 4.3.1.15; HMM-score: 23.1)
  • TheSEED  :
    • Cysteine synthase (EC 2.5.1.47)
    Amino Acids and Derivatives Lysine, threonine, methionine, and cysteine Cysteine Biosynthesis  Cysteine synthase (EC 2.5.1.47)
    and 1 more
    Amino Acids and Derivatives Lysine, threonine, methionine, and cysteine Methionine Biosynthesis  Cysteine synthase (EC 2.5.1.47)
  • PFAM:
    no clan defined PALP; Pyridoxal-phosphate dependent enzyme (PF00291; HMM-score: 241.3)
    and 3 more
    NADP_Rossmann (CL0063) ADH_zinc_N; Zinc-binding dehydrogenase (PF00107; HMM-score: 18.1)
    Periplas_BP (CL0144) Peripla_BP_4; Periplasmic binding protein domain (PF13407; HMM-score: 11.7)
    Thiolase (CL0046) ACP_syn_III_C; 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal (PF08541; HMM-score: 10.2)

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

  • domains:
  • modifications:
  • cofactors: pyridoxal 5'-phosphate
  • effectors:

⊟Localization[edit | edit source]

  • 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
    • SP(Sec/SPI): 0.003491
    • TAT(Tat/SPI): 0.000228
    • LIPO(Sec/SPII): 0.000529
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAQKPVDNITQIIGGTPVVKLRNVVDDNAADVYVKLEYQNPGGSVKDRIALAMIEKAEREGKIKPGDTIVEPTSGNTGIGLAFVCAAKGYKAVFTMPETMSQERRNLLKAYGAELVLTPGSEAMKGAIKKAKELKEEHGYFEPQQFENPANPEVHELTTGPELLQQFEGKTIDAFLAGVGTGGTLSGVGKVLKKEYPNIEIVAIEPEASPVLSGGEPGPHKLQGLGAGFIPGTLNTEIYDSIIKVGNDTAMEMSRRVAKEEGILAGISSGAAIYAAIQKAKELGKGKTVVTVLPSNGERYLSTPLYSFDD

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 5242 [5]
  • interaction partners:
    SACOL0842(eno)phosphopyruvate hydratase  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [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)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL1681Rrf2 family protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: CymR* (repression) regulon
    CymR*(TF)important in Cysteine metabolism; RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 366.64 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 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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