From AureoWiki
Jump to navigation Jump to search

NCBI: 03-AUG-2016

Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01269
  • pan locus tag?: SAUPAN003596000
  • symbol: SAOUHSC_01269
  • pan gene symbol?: miaB
  • synonym:
  • product: (dimethylallyl)adenosine tRNA methylthiotransferase

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_01269
  • symbol: SAOUHSC_01269
  • product: (dimethylallyl)adenosine tRNA methylthiotransferase
  • replicon: chromosome
  • strand: +
  • coordinates: 1223950..1225494
  • length: 1545
  • 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
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    GTGAACGAAGAACAAAGAAAAGCAAGTTCTGTAGATGTTTTAGCTGAGAGAGATAAGAAA
    GCAGAAAAAGATTATAGTAAATATTTTGAACATGTTTATCAGCCGCCTAATTTAAAAGAA
    GCGAAAAAAAGAGGTAAACAAGAAGTTCGTTATAATAGAGATTTCCAAATTGATGAAAAA
    TATCGCGGTATGGGGAACGAGCGTACATTTTTAATTAAAACATATGGATGTCAAATGAAT
    GCACATGACACTGAGGTCATTGCTGGTATACTTGAAGCATTAGGCTATCAAGCAACGACT
    GATATTAACACTGCAGATGTTATTTTAATTAATACATGTGCGATTAGAGAAAATGCCGAG
    AACAAAGTGTTTAGTGAAATAGGTAATTTGAAGCATTTGAAAAAAGAACGACCTGATATT
    TTAATCGGTGTTTGTGGTTGTATGTCACAAGAAGAGTCAGTAGTGAATAAAATTTTAAAA
    TCGTATCAAAATGTAGATATGATATTTGGTACACATAATATTCATCATTTACCAGAAATT
    TTAGAAGAAGCATACTTATCTAAAGCAATGGTTGTTGAAGTATGGTCTAAAGAAGGAGAC
    GTTATTGAAAATCTTCCAAAAGTCCGTGAAGGCAACATTAAAGCATGGGTCAATATTATG
    TATGGTTGTGATAAGTTTTGTACATATTGTATTGTTCCATTTACAAGAGGTAAAGAACGA
    AGCCGTAGACCTGAAGACATTATAGATGAAGTACGTGAACTTGCTCGTGAAGGTTACAAA
    GAAATAACGCTTTTAGGTCAAAATGTAAATTCTTATGGTAAAGATTTACAGGATATAGAA
    TATGACTTAGGAGATCTTTTACAAGCAATTTCTAAAATAGCGATTCCAAGAGTTCGTTTC
    ACAACAAGTCATCCTTGGGACTTTACAGATCACATGATTGATGTTATTTCAGAGGGTGGT
    AATATCGTTCCGCATATCCACTTGCCAGTTCAATCTGGAAATAATGCAGTATTAAAAATA
    ATGGGTAGAAAATATACACGAGAAAGTTATTTGGATTTAGTAAAACGAATCAAAGATAGA
    ATTCCTAATGTAGCATTAACTACAGATATTATTGTAGGGTATCCAAATGAATCAGAGGAA
    CAATTTGAAGAAACTTTAACTCTGTATGATGAAGTTGGTTTTGAACATGCATATACGTAC
    TTGTATTCACAACGTGATGGTACGCCTGCTGCTAAAATGAAAGATAATGTACCTTTAAAT
    GTCAAAAAGGAACGATTGCAACGTTTGAATAAAAAAGTTGGTCATTATTCACAAATAGCT
    ATGAGTAAGTACGAAGGACAAACTGTAACAGTACTTTGTGAAGGAAGTAGTAAAAAAGAT
    GATCAGGTTCTTGCTGGCTACACTGATAAAAATAAGCTAGTTAATTTCAAAGCGCCTAAA
    GAAATGATTGGTAAACTAGTGGAAGTACGAATAGATGAAGCTAAACAGTATTCATTAAAT
    GGCAGTTTTATAAAGGAAGTAGAGCCGGAAATGGTGATTCAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1545

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SAOUHSC_01269
  • symbol: SAOUHSC_01269
  • description: (dimethylallyl)adenosine tRNA methylthiotransferase
  • length: 514
  • theoretical pI: 6.26459
  • theoretical MW: 58930.8
  • GRAVY: -0.545914

Function[edit | edit source]

  • reaction:
    EC 2.8.4.3?  ExPASy
    tRNA-2-methylthio-N6-dimethylallyladenosine synthase N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
  • TIGRFAM:
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA-i(6)A37 thiotransferase enzyme MiaB (TIGR01574; EC 2.-.-.-; HMM-score: 630.8)
    radical SAM methylthiotransferase, MiaB/RimO family (TIGR00089; EC 2.1.1.-,2.8.1.-; HMM-score: 528)
    and 16 more
    Genetic information processing Protein synthesis tRNA and rRNA base modification MiaB-like tRNA modifying enzyme (TIGR01579; HMM-score: 334.6)
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein S12 methylthiotransferase RimO (TIGR01125; EC 2.1.1.-,2.8.1.-; HMM-score: 284.3)
    Genetic information processing Protein synthesis tRNA and rRNA base modification MiaB-like tRNA modifying enzyme, archaeal-type (TIGR01578; HMM-score: 261.7)
    Unknown function Enzymes of unknown specificity B12-binding domain/radical SAM domain protein, MJ_0865 family (TIGR04014; HMM-score: 82.7)
    Unknown function Enzymes of unknown specificity B12-binding domain/radical SAM domain protein, MJ_1487 family (TIGR04013; HMM-score: 63.1)
    Cellular processes Cellular processes Toxin production and resistance radical SAM P-methyltransferase, PhpK family (TIGR04479; EC 2.1.-.-; HMM-score: 40)
    hopanoid biosynthesis associated radical SAM protein HpnJ (TIGR03471; HMM-score: 29.5)
    putative heme utilization radical SAM enzyme HutW (TIGR04107; HMM-score: 29.3)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin coproporphyrinogen dehydrogenase HemZ (TIGR03994; EC 1.3.99.22; HMM-score: 22.7)
    Unknown function Enzymes of unknown specificity radical SAM protein, TIGR01212 family (TIGR01212; HMM-score: 22.6)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin putative oxygen-independent coproporphyrinogen III oxidase (TIGR00539; EC 1.3.99.22; HMM-score: 15.4)
    putative variant cofactor biosynthesis B12-binding domain/radical SAM domain protein 1 (TIGR04385; HMM-score: 14.2)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin oxygen-independent coproporphyrinogen III oxidase (TIGR00538; EC 1.3.99.22; HMM-score: 13.9)
    Cellular processes Cellular processes Toxin production and resistance tryptophan 2-C-methyltransferase (TIGR04428; EC 2.1.1.106; HMM-score: 13.2)
    Unknown function Enzymes of unknown specificity uncharacterized radical SAM protein YgiQ (TIGR03904; HMM-score: 12.9)
    magnesium-protoporphyrin IX monomethyl ester anaerobic oxidative cyclase (TIGR02026; HMM-score: 11.7)
  • TheSEED:  
    Protein Metabolism Protein processing and modification Ribosomal protein S12p Asp methylthiotransferase  tRNA-i(6)A37 methylthiotransferase
    and 4 more
    RNA Metabolism RNA processing and modification Methylthiotransferases  tRNA-i(6)A37 methylthiotransferase
    tRNA modification Archaea  tRNA-i(6)A37 methylthiotransferase
    tRNA mods Archaea  tRNA-i(6)A37 methylthiotransferase
    tRNA processing  tRNA-i(6)A37 methylthiotransferase
  • PFAM:
    TIM_barrel (CL0036) Radical_SAM; Radical SAM superfamily (PF04055; HMM-score: 119.1)
    CheY (CL0304) UPF0004; Uncharacterized protein family UPF0004 (PF00919; HMM-score: 103)
    and 3 more
    OB (CL0021) TRAM; TRAM domain (PF01938; HMM-score: 50)
    NTF2 (CL0051) DUF3887; Protein of unknown function (DUF3887) (PF13026; HMM-score: 14.7)
    TIM_barrel (CL0036) AP_endonuc_2; Xylose isomerase-like TIM barrel (PF01261; HMM-score: 13.4)

Structure, modifications & interactions[edit | edit source]

  • domains:
  • modifications:
  • cofactors: [4Fe-4S] cluster
  • effectors:
  • protein partners:
    SAOUHSC_00530elongation factor Tu  [1] (data from MRSA252)

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): 0.009083
    • TAT(Tat/SPI): 0.002069
    • LIPO(Sec/SPII): 0.003372
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MNEEQRKASSVDVLAERDKKAEKDYSKYFEHVYQPPNLKEAKKRGKQEVRYNRDFQIDEKYRGMGNERTFLIKTYGCQMNAHDTEVIAGILEALGYQATTDINTADVILINTCAIRENAENKVFSEIGNLKHLKKERPDILIGVCGCMSQEESVVNKILKSYQNVDMIFGTHNIHHLPEILEEAYLSKAMVVEVWSKEGDVIENLPKVREGNIKAWVNIMYGCDKFCTYCIVPFTRGKERSRRPEDIIDEVRELAREGYKEITLLGQNVNSYGKDLQDIEYDLGDLLQAISKIAIPRVRFTTSHPWDFTDHMIDVISEGGNIVPHIHLPVQSGNNAVLKIMGRKYTRESYLDLVKRIKDRIPNVALTTDIIVGYPNESEEQFEETLTLYDEVGFEHAYTYLYSQRDGTPAAKMKDNVPLNVKKERLQRLNKKVGHYSQIAMSKYEGQTVTVLCEGSSKKDDQVLAGYTDKNKLVNFKAPKEMIGKLVEVRIDEAKQYSLNGSFIKEVEPEMVIQ

Experimental data[edit | edit source]

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. 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. Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  3. Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  4. Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

Relevant publications[edit | edit source]