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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01074
  • pan locus tag?: SAUPAN003351000
  • symbol: SAOUHSC_01074
  • pan gene symbol?: rsmD
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_01074
  • symbol: SAOUHSC_01074
  • product: hypothetical protein
  • replicon: chromosome
  • strand: +
  • coordinates: 1038980..1039450
  • length: 471
  • 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
    ATGGATAAAGTTAAAGAAGGTATCTTTAATAGTTTATATGATGTGTCAGGTATAGGTTTA
    GATTTATTTGCAGGAAGCGGGGCGCTTGGAATAGAAGCACTCTCTCGAGGTATGGATAAG
    GTAATCTTTGTTGATCAAAATTTTAAAGCTGTAAAAGTTATTAAATCAAATCTTGCGAAT
    TTGGATTTAGAGGCACAATCTGAAGTTTATAAAAATAATGCAGATAGAGCTTTAAAAGCA
    TTGTCAAAACGTGATATTCAATTTGATGTCATTTTCTTAGATCCACCTTATAATAAAGGT
    CTCATTGATAAAGCTTTAAAACTAATTTCAGAGTTTAATTTATTGAAAGAAAATGGTATC
    ATCGTTTGTGAATTTAGCAATCATGAAGAAATAGATTATCAACCGTTTAATATGATTAAA
    CGTTACCATTATGGGTTGACAGACACATTGTTATTAGAAAAGGGAGAATAG
    60
    120
    180
    240
    300
    360
    420
    471

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_01074
  • symbol: SAOUHSC_01074
  • description: hypothetical protein
  • length: 156
  • theoretical pI: 4.84693
  • theoretical MW: 17566.1
  • GRAVY: -0.136538

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis tRNA and rRNA base modification 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD (TIGR00095; EC 2.1.1.171; HMM-score: 142)
    and 11 more
    Genetic information processing Protein fate Protein modification and repair protein-(glutamine-N5) methyltransferase, release factor-specific (TIGR03534; EC 2.1.1.-; HMM-score: 34.6)
    Genetic information processing Protein fate Protein modification and repair methyltransferase, HemK family (TIGR00536; HMM-score: 33.9)
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific (TIGR03533; EC 2.1.1.-; HMM-score: 31)
    Genetic information processing Protein synthesis tRNA and rRNA base modification 23S rRNA (uracil-5-)-methyltransferase RumA (TIGR00479; EC 2.1.1.-; HMM-score: 27.7)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit (TIGR02469; EC 2.1.1.132; HMM-score: 26.4)
    Genetic information processing Protein synthesis tRNA and rRNA base modification N2,N2-dimethylguanosine tRNA methyltransferase (TIGR00308; EC 2.1.1.-; HMM-score: 24.7)
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein L11 methyltransferase (TIGR00406; EC 2.1.1.-; HMM-score: 23.5)
    Genetic information processing DNA metabolism Restriction/modification type II restriction m6 adenine DNA methyltransferase, Alw26I/Eco31I/Esp3I family (TIGR02987; EC 2.1.1.72; HMM-score: 20.7)
    Hypothetical proteins Conserved putative methyltransferase, TIGR01177 family (TIGR01177; HMM-score: 20.5)
    Unknown function Enzymes of unknown specificity putative methylase (TIGR00537; HMM-score: 14.9)
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA (uracil(54)-C(5))-methyltransferase (TIGR02143; EC 2.1.1.35; HMM-score: 13.4)
  • TheSEED  :
    • 16S rRNA (guanine(966)-N(2))-methyltransferase (EC 2.1.1.171)
    CBSS-269801.1.peg.1715  Ribosomal RNA small subunit methyltransferase D (EC 2.1.1.-)
  • PFAM:
    NADP_Rossmann (CL0063) Cons_hypoth95; Conserved hypothetical protein 95 (PF03602; HMM-score: 141.8)
    and 18 more
    MTS; Methyltransferase small domain (PF05175; HMM-score: 37.3)
    Methyltransf_31; Methyltransferase domain (PF13847; HMM-score: 30.6)
    Methyltransf_15; RNA cap guanine-N2 methyltransferase (PF09445; HMM-score: 27.1)
    MethyltransfD12; D12 class N6 adenine-specific DNA methyltransferase (PF02086; HMM-score: 26.6)
    TRM; N2,N2-dimethylguanosine tRNA methyltransferase (PF02005; HMM-score: 25.2)
    Methyltransf_25; Methyltransferase domain (PF13649; HMM-score: 23.1)
    PrmA; Ribosomal protein L11 methyltransferase (PrmA) (PF06325; HMM-score: 21.6)
    Methyltransf_24; Methyltransferase domain (PF13578; HMM-score: 18.9)
    UPF0020; Putative RNA methylase family UPF0020 (PF01170; HMM-score: 16.1)
    N6_N4_Mtase; DNA methylase (PF01555; HMM-score: 15.9)
    RsmJ; Ribosomal RNA large subunit methyltransferase D, RlmJ (PF04378; HMM-score: 15.7)
    Methyltr_RsmB-F; 16S rRNA methyltransferase RsmB/F (PF01189; HMM-score: 14.3)
    Methyltransf_16; Lysine methyltransferase (PF10294; HMM-score: 13.7)
    tRNA_U5-meth_tr; tRNA (Uracil-5-)-methyltransferase (PF05958; HMM-score: 13.3)
    Methyltransf_3; O-methyltransferase (PF01596; HMM-score: 13.2)
    Met_10; Met-10+ like-protein (PF02475; HMM-score: 13.2)
    Spermine_synth; Spermine/spermidine synthase domain (PF01564; HMM-score: 13.1)
    N6-adenineMlase; Probable N6-adenine methyltransferase (PF10237; HMM-score: 13)

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

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: unknown (no significant prediction)
    • Cytoplasmic Score: 2.5
    • Cytoplasmic Membrane Score: 2.5
    • Cellwall Score: 2.5
    • Extracellular Score: 2.5
    • 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): 0.020202
    • TAT(Tat/SPI): 0.013568
    • LIPO(Sec/SPII): 0.002534
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MDKVKEGIFNSLYDVSGIGLDLFAGSGALGIEALSRGMDKVIFVDQNFKAVKVIKSNLANLDLEAQSEVYKNNADRALKALSKRDIQFDVIFLDPPYNKGLIDKALKLISEFNLLKENGIIVCEFSNHEEIDYQPFNMIKRYHYGLTDTLLLEKGE

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [1] [2]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • interaction partners:

⊟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. ↑ 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)
  2. ↑ 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)
  3. ↑ 3.0 3.1 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]

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