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NCBI: 26-AUG-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA0992 [new locus tag: SA_RS05620 ]
  • 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: SA0992 [new locus tag: SA_RS05620 ]
  • symbol: trxA
  • product: thioredoxin
  • replicon: chromosome
  • strand: +
  • coordinates: 1124617..1124931
  • length: 315
  • essential: no DEG 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: SA0992 [new locus tag: SA_RS05620 ]
  • 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: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA1409(dnaK)molecular chaperone DnaK  [1] (data from MRSA252)
    SA0731(eno)phosphopyruvate hydratase  [1] (data from MRSA252)
    SA0505(fus)elongation factor G  [1] (data from MRSA252)
    SA0727(gap)glyceraldehyde-3-phosphate dehydrogenase  [1] (data from MRSA252)
    SA1112(infB)translation initiation factor IF-2  [1] (data from MRSA252)
    SA0946(pdhD)dihydrolipoamide dehydrogenase  [1] (data from MRSA252)
    SA1938(pdp)pyrimidine-nucleoside phosphorylase  [1] (data from MRSA252)
    SA0218(pflB)formate acetyltransferase  [1] (data from MRSA252)
    SA0454(purR)pur operon repressor  [1] (data from MRSA252)
    SA1520(pykA)pyruvate kinase  [1] (data from MRSA252)
    SA0496(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    SA2044(rplB)50S ribosomal protein L2  [1] (data from MRSA252)
    SA2035(rplE)50S ribosomal protein L5  [1] (data from MRSA252)
    SA2033(rplF)50S ribosomal protein L6  [1] (data from MRSA252)
    SA0497(rplJ)50S ribosomal protein L10  [1] (data from MRSA252)
    SA2022(rplQ)50S ribosomal protein L17  [1] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [1] (data from MRSA252)
    SA1502(rplT)50S ribosomal protein L20  [1] (data from MRSA252)
    SA1473(rplU)50S ribosomal protein L21  [1] (data from MRSA252)
    SA2042(rplV)50S ribosomal protein L22  [1] (data from MRSA252)
    SA2045(rplW)50S ribosomal protein L23  [1] (data from MRSA252)
    SA0501(rpoC)DNA-directed RNA polymerase subunit beta'  [1] (data from MRSA252)
    SA1099(rpsB)30S ribosomal protein S2  [1] (data from MRSA252)
    SA2041(rpsC)30S ribosomal protein S3  [1] (data from MRSA252)
    SA2031(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SA2016(rpsI)30S ribosomal protein S9  [1] (data from MRSA252)
    SA2038(rpsQ)30S ribosomal protein S17  [1] (data from MRSA252)
    SA0506(tuf)elongation factor Tu  [1] (data from MRSA252)
    SA0627hypothetical protein  [1] (data from MRSA252)
    SA0802hypothetical protein  [1] (data from MRSA252)
    SA0829hypothetical protein  [1] (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: no data available

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. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 1.28 1.29 1.30 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)

Relevant publications[edit | edit source]

Alexander Scherl, Patrice François, Manuela Bento, Jacques M Deshusses, Yvan Charbonnier, Véronique Converset, Antoine Huyghe, Nadia Walter, Christine Hoogland, Ron D Appel, Jean-Charles Sanchez, Catherine G Zimmermann-Ivol, Garry L Corthals, Denis F Hochstrasser, Jacques Schrenzel
Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth.
J Microbiol Methods: 2005, 60(2);247-57
[PubMed:15590099] [WorldCat.org] [DOI] (P p)