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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1155 [new locus tag: SACOL_RS05900 ]
  • pan locus tag?: SAUPAN003383000
  • symbol: trxA
  • pan gene symbol?: trxA
  • synonym:
  • product: thioredoxin

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1155 [new locus tag: SACOL_RS05900 ]
  • symbol: trxA
  • product: thioredoxin
  • replicon: chromosome
  • strand: +
  • coordinates: 1165588..1165902
  • length: 315
  • 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
    ATGGCAATCGTAAAAGTAACAGATGCAGATTTTGATTCAAAAGTAGAATCTGGTGTACAA
    CTAGTAGATTTTTGGGCAACATGGTGTGGTCCATGTAAAATGATCGCTCCGGTATTAGAA
    GAATTAGCAGCTGACTATGAAGGTAAAGCTGACATTTTAAAATTAGATGTTGATGAAAAT
    CCATCAACTGCAGCTAAATATGAAGTGATGAGTATTCCAACATTAATCGTCTTTAAAGAC
    GGTCAACCAGTTGATAAAGTTGTTGGTTTCCAACCAAAAGAAAACTTAGCTGAAGTTTTA
    GATAAACATTTATAA
    60
    120
    180
    240
    300
    315

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1155 [new locus tag: SACOL_RS05900 ]
  • symbol: TrxA
  • description: thioredoxin
  • length: 104
  • theoretical pI: 4.14487
  • theoretical MW: 11440.1
  • GRAVY: 0.0288462

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Energy metabolism Electron transport thioredoxin (TIGR01068; HMM-score: 132.2)
    and 9 more
    Genetic information processing Protein fate Protein folding and stabilization protein disulfide-isomerase domain (TIGR01126; HMM-score: 65.5)
    protein disulfide isomerase (TIGR01130; HMM-score: 56.6)
    Unknown function General redox-active disulfide protein 1 (TIGR00411; HMM-score: 34.4)
    Genetic information processing Protein fate Protein folding and stabilization periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily (TIGR00385; HMM-score: 31.6)
    glutaredoxin-like domain protein (TIGR02187; HMM-score: 24.2)
    glutaredoxin-like protein, YruB-family (TIGR02196; HMM-score: 22.3)
    glutaredoxin-like protein (TIGR02200; HMM-score: 22.1)
    Metabolism Central intermediary metabolism Sulfur metabolism 5'-adenylylsulfate reductase, thioredoxin-independent (TIGR00424; HMM-score: 14.9)
    type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB (TIGR02738; HMM-score: 12.6)
  • TheSEED  :
    • Thioredoxin
    Prolyl-tRNA synthetase associated editing enzymes  Thioredoxin
  • PFAM:
    Thioredoxin (CL0172) Thioredoxin; Thioredoxin (PF00085; HMM-score: 113.1)
    and 14 more
    Thioredoxin_2; Thioredoxin-like domain (PF13098; HMM-score: 36.5)
    Thioredoxin_8; Thioredoxin-like (PF13905; HMM-score: 31.5)
    Thioredoxin_3; Thioredoxin domain (PF13192; HMM-score: 24.8)
    Thioredoxin_9; Thioredoxin (PF14595; HMM-score: 24.6)
    AhpC-TSA; AhpC/TSA family (PF00578; HMM-score: 19.6)
    KaiB; KaiB domain (PF07689; HMM-score: 18)
    Redoxin; Redoxin (PF08534; HMM-score: 18)
    OST3_OST6; OST3 / OST6 family, transporter family (PF04756; HMM-score: 17.3)
    DUF836; Glutaredoxin-like domain (DUF836) (PF05768; HMM-score: 16.7)
    TraF; F plasmid transfer operon protein (PF13728; HMM-score: 16)
    Glutaredoxin; Glutaredoxin (PF00462; HMM-score: 15.2)
    HyaE; Hydrogenase-1 expression protein HyaE (PF07449; HMM-score: 14.9)
    Thioredoxin_7; Thioredoxin-like (PF13899; HMM-score: 14.9)
    DSBA; DSBA-like thioredoxin domain (PF01323; HMM-score: 13.5)

⊟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): 0.01275
    • TAT(Tat/SPI): 0.000543
    • LIPO(Sec/SPII): 0.001187
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAIVKVTDADFDSKVESGVQLVDFWATWCGPCKMIAPVLEELAADYEGKADILKLDVDENPSTAAKYEVMSIPTLIVFKDGQPVDKVVGFQPKENLAEVLDKHL

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 7846 [5]
  • interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    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)
    SACOL1288(infB)translation initiation factor IF-2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL0539(purR)pur operon repressor  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [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)
    SACOL2212(rplQ)50S ribosomal protein L17  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 34.93 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 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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