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NCBI: 03-AUG-2016

Summary[edit source | edit]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_02358
  • pan locus tag?: SAUPAN005408000
  • symbol: SAOUHSC_02358
  • pan gene symbol?: prmC
  • synonym:
  • product: HemK family modification methylase

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SAOUHSC_02358
  • symbol: SAOUHSC_02358
  • product: HemK family modification methylase
  • replicon: chromosome
  • strand: -
  • coordinates: 2179756..2180508
  • length: 753
  • essential: no DEG 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
    ATGTTAGATGTATTTCAATGGACGCGTACGGACTTTGTAGTCCACATGCATGATGATATG
    CCGAAAGCGATGATTATGAAGTTCGACTTAGCATTACAACGTATGTTATTAGGAGAGCCT
    ATACAGTATATAGTTGGCTTTGCCTCATTTTATGGTAGAACGTTTGATGTAAACTCAAAT
    TGTTTGATACCAAGACCTGAAACTGAAGAAGTAATGTTGCATTTCTTACAACAGTTAGAA
    GATGATGCAACAATCGTAGATATCGGAACGGGTAGTGGTGTACTTGCAATTACTTTGAAA
    TGTGAAAAGCCGGATTTAAATGTTATTGCTACTGATATTTCACTTGAAGCAATGAATATG
    GCTCGTAATAATGCTGAGAAGCATCAATCACAAATACAATTTTTAACAGGGGATGCATTA
    AAGCCCTTAATTAATGAAGGTATCAAGTTGAACGGCTTGATATCTAATCCACCATATATA
    GATGAAAAAGATATGGTTACGATGTCTCCAACGGTTACGAGATTCGAACCACATCAGGCA
    TTGTTTGCAGATAACCATGGATATGCTATTTATGAATCAATCATTGAAGATTTACCTCAC
    GTTATGGAAAAAGGCAGCCCAGTTGTTTTTGAAATTGGTTACAATCAAGGTGAGGCACTT
    AAATCAATAATTTTAAATAAATTTCCTGACAAAAAAATCGACATTATTAAAGATATAAAT
    GGCCACGATCGAATCGTCTCATTTAAATGGTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    753

Protein[edit source | edit]

General[edit source | edit]

  • locus tag: SAOUHSC_02358
  • symbol: SAOUHSC_02358
  • description: HemK family modification methylase
  • length: 250
  • theoretical pI: 4.69126
  • theoretical MW: 28341.5
  • GRAVY: -0.1072

Function[edit source | edit]

  • reaction:
    EC 2.1.1.297?  ExPASy
    Peptide chain release factor N5-glutamine methyltransferaseS-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N5-methyl-L-glutamine
  • TIGRFAM:
    Genetic information processingProtein fateProtein modification and repairprotein-(glutamine-N5) methyltransferase, release factor-specific (TIGR03534; EC 2.1.1.-; HMM-score: 253.6)
    Genetic information processingProtein fateProtein modification and repairmethyltransferase, HemK family (TIGR00536; HMM-score: 201)
    Genetic information processingProtein synthesisRibosomal proteins: synthesis and modificationprotein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific (TIGR03533; EC 2.1.1.-; HMM-score: 114.9)
    Genetic information processingProtein synthesisRibosomal proteins: synthesis and modificationputative protein-(glutamine-N5) methyltransferase, unknown substrate-specific (TIGR03704; EC 2.1.1.-; HMM-score: 71.9)
    Unknown functionEnzymes of unknown specificityputative methylase (TIGR00537; HMM-score: 47.7)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersHeme, porphyrin, and cobalaminprecorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit (TIGR02469; EC 2.1.1.132; HMM-score: 33.1)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersMenaquinone and ubiquinoneubiquinone/menaquinone biosynthesis methyltransferase (TIGR01934; EC 2.1.1.-; HMM-score: 30.6)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersBiotinmalonyl-acyl carrier protein O-methyltransferase BioC (TIGR02072; EC 2.1.1.-; HMM-score: 29)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersChlorophyll and bacteriochlorphyllmagnesium protoporphyrin O-methyltransferase (TIGR02021; EC 2.1.1.11; HMM-score: 27.6)
    Genetic information processingProtein synthesisRibosomal proteins: synthesis and modificationribosomal protein L11 methyltransferase (TIGR00406; EC 2.1.1.-; HMM-score: 27)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersMenaquinone and ubiquinone3-demethylubiquinone-9 3-O-methyltransferase (TIGR01983; EC 2.1.1.64; HMM-score: 23.7)
    Genetic information processingProtein synthesistRNA and rRNA base modificationribosomal RNA small subunit methyltransferase A (TIGR00755; EC 2.1.1.182; HMM-score: 23.3)
    Genetic information processingProtein synthesistRNA and rRNA base modificationtRNA (guanine-N(7)-)-methyltransferase (TIGR00091; EC 2.1.1.33; HMM-score: 21)
    Genetic information processingProtein synthesistRNA and rRNA base modification23S rRNA (uracil-5-)-methyltransferase RumA (TIGR00479; EC 2.1.1.-; HMM-score: 18.9)
    Genetic information processingProtein fateProtein modification and repairprotein-L-isoaspartate O-methyltransferase (TIGR00080; EC 2.1.1.77; HMM-score: 15.4)
    Genetic information processingTranscriptionRNA processing3' terminal RNA ribose 2'-O-methyltransferase Hen1 (TIGR04074; EC 2.1.1.-; HMM-score: 14.1)
    Genetic information processingProtein synthesistRNA and rRNA base modification3' terminal RNA ribose 2'-O-methyltransferase Hen1 (TIGR04074; EC 2.1.1.-; HMM-score: 14.1)
    Genetic information processingProtein synthesistRNA and rRNA base modification16S rRNA (guanine(527)-N(7))-methyltransferase RsmG (TIGR00138; EC 2.1.1.170; HMM-score: 14)
    2-ketoarginine methyltransferase (TIGR04543; EC 2.1.1.243; HMM-score: 13.4)
    Genetic information processingProtein synthesistRNA and rRNA base modificationN2,N2-dimethylguanosine tRNA methyltransferase (TIGR00308; EC 2.1.1.-; HMM-score: 12.3)
    Cell structureCell envelopeBiosynthesis and degradation of surface polysaccharides and lipopolysaccharidesputative sugar O-methyltransferase (TIGR04371; EC 2.1.1.-; HMM-score: 11.9)
    Genetic information processingProtein synthesistRNA and rRNA base modification23S rRNA (uracil-5-)-methyltransferase RumB (TIGR02085; EC 2.1.1.189; HMM-score: 11.1)
  • TheSEED:  
    RNA MetabolismRNA processing and modificationYrdC-YciO-Sua5 and associated protein families Protein-N(5)-glutamine methyltransferase PrmC, methylates polypeptide chain release factors RF1 and RF2 
  • PFAM:
    NADP_Rossmann (CL0063) MTS; Methyltransferase small domain (PF05175; HMM-score: 58)
    Methyltransf_25; Methyltransferase domain (PF13649; HMM-score: 34.6)
    Methyltransf_18; Methyltransferase domain (PF12847; HMM-score: 34.2)
    Methyltransf_31; Methyltransferase domain (PF13847; HMM-score: 33.7)
    PrmA; Ribosomal protein L11 methyltransferase (PrmA) (PF06325; HMM-score: 32)
    PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT) (PF01135; HMM-score: 26.2)
    Methyltransf_4; Putative methyltransferase (PF02390; HMM-score: 24.1)
    Methyltransf_12; Methyltransferase domain (PF08242; HMM-score: 24.1)
    Methyltransf_11; Methyltransferase domain (PF08241; HMM-score: 22.2)
    Methyltransf_23; Methyltransferase domain (PF13489; HMM-score: 21.2)
    Methyltransf_32; Methyltransferase domain (PF13679; HMM-score: 19.9)
    Methyltransf_2; O-methyltransferase (PF00891; HMM-score: 19.7)
    Methyltransf_16; Lysine methyltransferase (PF10294; HMM-score: 19.3)
    GidB; rRNA small subunit methyltransferase G (PF02527; HMM-score: 17.7)
    CmcI; Cephalosporin hydroxylase (PF04989; HMM-score: 17.1)
    Methyltransf_15; RNA cap guanine-N2 methyltransferase (PF09445; HMM-score: 16.9)
    TrmK; tRNA (adenine(22)-N(1))-methyltransferase (PF04816; HMM-score: 16.2)
    UPF0020; Putative RNA methylase family UPF0020 (PF01170; HMM-score: 14.1)
    CMAS; Mycolic acid cyclopropane synthetase (PF02353; HMM-score: 12.9)
    CheR; CheR methyltransferase, SAM binding domain (PF01739; HMM-score: 11.2)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:

Localization[edit source | edit]

  • 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
    • Ymax: 0.098
    • Ymax_pos: 68
    • Cmax: 0.111
    • Cmax_pos: 49
    • Smax: 0.143
    • Smax_pos: 26
    • Smean: 0.071
    • D: 0.088
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFDVNSNCLIPRPETEEVMLHFLQQLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQSQIQFLTGDALKPLINEGIKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQGEALKSIILNKFPDKKIDIIKDINGHDRIVSFKW

Experimental data[edit source | edit]

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: no data available

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. 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)
  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. 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 source | edit]