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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0927 [new locus tag: SACOL_RS04755 ]
  • pan locus tag?: SAUPAN003022000
  • symbol: lipA
  • pan gene symbol?: lipA
  • synonym:
  • product: lipoyl synthase

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SACOL0927 [new locus tag: SACOL_RS04755 ]
  • symbol: lipA
  • product: lipoyl synthase
  • replicon: chromosome
  • strand: +
  • coordinates: 933228..934145
  • length: 918
  • 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
    781
    841
    901
    ATGGCGACAAAAAACGAGGAAATATTACGTAAACCGGATTGGTTGAAAATAAAATTAAAT
    ACCAACGAAAACTATACAGGACTTAAGAAGATGATGAGGGAAAAAAATCTTAATACTGTA
    TGTGAAGAAGCTAAATGTCCTAATATACATGAATGTTGGGGTGCACGTCGTACAGCGACA
    TTTATGATTTTAGGTGCCGTATGTACAAGAGCTTGTCGTTTTTGTGCGGTTAAGACAGGT
    TTACCTAATGAACTTGATTTAAATGAGCCTGAACGTGTAGCTGAATCAGTTGAATTAATG
    AATTTGAAACACGTTGTTATCACTGCTGTTGCGCGTGATGATTTAAGAGATGCTGGTTCA
    AATGTTTATGCTGAGACAGTACGTAAAGTTAGAGAAAGAAATCCATTTACAACGATTGAA
    ATTTTACCATCAGATATGGGCGGGGACTATGATGCGTTAGAAACATTAATGGCGTCAAGA
    CCTGACATTTTAAACCATAATATTGAAACTGTTCGTCGCTTAACACCGAGAGTTCGTGCG
    CGTGCGACTTACGACAGAACATTAGAGTTTTTACGTCGTTCAAAAGAATTACAACCGGAT
    ATCCCAACTAAATCAAGTATTATGGTTGGATTAGGTGAAACTATAGAAGAAATTTATGAA
    ACGATGGATGATTTACGTGCGAATGATGTAGATATTTTAACGATTGGTCAATATTTACAA
    CCTTCACGTAAACATTTAAAGGTTCAAAAATATTACACGCCTTTAGAGTTTGGTAAATTA
    AGAAAAGTGGCAATGGATAAAGGGTTTAAACATTGCCAAGCTGGACCTTTAGTACGTAGT
    TCTTATCATGCGGATGAGCAAGTAAATGAAGCTGCTAAAGAAAAGCAACGCCAAGGTGAG
    GCACAGTTAAATAGTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    918

Protein[edit source | edit]

General[edit source | edit]

  • locus tag: SACOL0927 [new locus tag: SACOL_RS04755 ]
  • symbol: LipA
  • description: lipoyl synthase
  • length: 305
  • theoretical pI: 8.26846
  • theoretical MW: 34884.8
  • GRAVY: -0.598033

Function[edit source | edit]

  • reaction:
    EC 2.8.1.8?  ExPASy
    Lipoyl synthaseProtein N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin
  • TIGRFAM:
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersLipoatelipoyl synthase (TIGR00510; EC 2.8.1.8; HMM-score: 400.6)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersBiotinbiotin synthase (TIGR00433; EC 2.8.1.6; HMM-score: 34.8)
    Unknown functionEnzymes of unknown specificityradical SAM protein, MSMEG_0568 family (TIGR04043; HMM-score: 24.2)
    radical SAM methylthiotransferase, MiaB/RimO family (TIGR00089; EC 2.1.1.-,2.8.1.-; HMM-score: 15.7)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersOther7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit (TIGR03550; EC 2.5.1.77; HMM-score: 14.4)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersOther7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit (TIGR03551; EC 2.5.1.77; HMM-score: 14.3)
    Hypothetical proteinsConservedradical SAM domain protein, CofH subfamily (TIGR00423; HMM-score: 13.6)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersMenaquinone and ubiquinonedehypoxanthine futalosine cyclase (TIGR03699; HMM-score: 13.5)
    Genetic information processingProtein synthesisRibosomal proteins: synthesis and modificationribosomal protein S12 methylthiotransferase RimO (TIGR01125; EC 2.1.1.-,2.8.1.-; HMM-score: 12.9)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersThiaminethiazole biosynthesis protein ThiH (TIGR02351; HMM-score: 11.6)
  • TheSEED:  
    Lipoic acid metabolism Lipoyl synthase (EC 2.8.1.8) 
  • PFAM:
    TIM_barrel (CL0036) Radical_SAM; Radical SAM superfamily (PF04055; HMM-score: 51.4)
    no clan definedLIAS_N; N-terminal domain of lipoyl synthase of Radical_SAM family (PF16881; HMM-score: 42.3)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors: [4Fe-4S] cluster
  • effectors:
  • protein partners:
    SACOL0568hypothetical protein  [1] (data from MRSA252)
    SACOL0569ATP:guanido phosphotransferase  [1] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [1] (data from MRSA252)
    SACOL1759universal stress protein  [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: 0.128
    • Ymax_pos: 11
    • Cmax: 0.104
    • Cmax_pos: 56
    • Smax: 0.215
    • Smax_pos: 4
    • Smean: 0.17
    • D: 0.144
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MATKNEEILRKPDWLKIKLNTNENYTGLKKMMREKNLNTVCEEAKCPNIHECWGARRTATFMILGAVCTRACRFCAVKTGLPNELDLNEPERVAESVELMNLKHVVITAVARDDLRDAGSNVYAETVRKVRERNPFTTIEILPSDMGGDYDALETLMASRPDILNHNIETVRRLTPRVRARATYDRTLEFLRRSKELQPDIPTKSSIMVGLGETIEEIYETMDDLRANDVDILTIGQYLQPSRKHLKVQKYYTPLEFGKLRKVAMDKGFKHCQAGPLVRSSYHADEQVNEAAKEKQRQGEAQLNS

Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4] [5]
    quantitative data / protein copy number per cell: 243 [6]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: 0.97 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 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)

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