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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0587 [new locus tag: SACOL_RS03045 ]
  • pan locus tag?: SAUPAN002312000
  • symbol: SACOL0587
  • pan gene symbol?: rsmC
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0587 [new locus tag: SACOL_RS03045 ]
  • symbol: SACOL0587
  • product: hypothetical protein
  • replicon: chromosome
  • strand: +
  • coordinates: 606165..606773
  • length: 609
  • 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
    361
    421
    481
    541
    601
    ATGAGTCATTATTACGATGAAGATCCAAGTGTAATTAGCAATGAACAACGTATTCAATAT
    CAATTAAACCATCATAAAATTGATTTAATAACTGATAACGGAGTGTTTTCGAAAGATAAA
    GTAGATTATGGTTCAGATGTTCTTGTTCAAACTTTTTTAAAAGCGCATCCACCTGGTCCA
    AGTAAGCGAATTGCCGATGTTGGTTGTGGTTACGGACCAATTGGTTTGATGATTGCTAAA
    GTATCACCACATCATTCAATTACAATGCTAGATGTTAATCACAGAGCGCTAGCCTTAGTT
    GAAAAAAACAAAAAATTAAATGGTATTGATAATGTGATCGTAAAGGAAAGTGATGCTTTG
    TCTGCTGTGGAAGACAAAAGTTTTGATTTTATTTTAACCAATCCACCAATAAGAGCAGGG
    AAAGAAACCGTGCATCGTATATTCGAGCAAGCATTACATAGATTAGACTCGAACGGTGAA
    CTATTCGTTGTAATTCAGAAGAAGCAAGGTATGCCATCTGCAAAGAAAAGAATGAATGAA
    CTTTTTGGAAATGTAGAAGTGGTAAATAAAGATAAAGGATATTACATTCTGAGAAGTATA
    AAAGCTTGA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    609

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0587 [new locus tag: SACOL_RS03045 ]
  • symbol: SACOL0587
  • description: hypothetical protein
  • length: 202
  • theoretical pI: 8.90035
  • theoretical MW: 22679.8
  • GRAVY: -0.378713

⊟Function[edit | edit source]

  • ⊞TIGRFAM:
    Genetic information processing Protein fate Protein modification and repair protein-(glutamine-N5) methyltransferase, release factor-specific (TIGR03534; EC 2.1.1.-; HMM-score: 71.5)
    Genetic information processing Protein fate Protein modification and repair methyltransferase, HemK family (TIGR00536; HMM-score: 59.8)
    and 24 more
    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: 53.3)
    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: 38.7)
    Unknown function Enzymes of unknown specificity putative methylase (TIGR00537; HMM-score: 29.4)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Biotin malonyl-acyl carrier protein O-methyltransferase BioC (TIGR02072; EC 2.1.1.-; HMM-score: 28.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone 3-demethylubiquinone-9 3-O-methyltransferase (TIGR01983; EC 2.1.1.64; HMM-score: 26.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone ubiquinone/menaquinone biosynthesis methyltransferase (TIGR01934; EC 2.1.1.-; HMM-score: 26.6)
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein L11 methyltransferase (TIGR00406; EC 2.1.1.-; HMM-score: 22.7)
    Genetic information processing Protein synthesis tRNA and rRNA base modification 23S rRNA (uracil-5-)-methyltransferase RumA (TIGR00479; EC 2.1.1.-; HMM-score: 22.3)
    Genetic information processing Protein synthesis tRNA and rRNA base modification 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG (TIGR00138; EC 2.1.1.170; HMM-score: 21.9)
    Genetic information processing Protein synthesis tRNA and rRNA base modification 23S rRNA (uracil-5-)-methyltransferase RumB (TIGR02085; EC 2.1.1.189; HMM-score: 21.5)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone demethylmenaquinone methyltransferase (TIGR02752; EC 2.1.1.163; HMM-score: 21.2)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides putative sugar O-methyltransferase (TIGR04371; EC 2.1.1.-; HMM-score: 18.9)
    Genetic information processing Protein synthesis tRNA and rRNA base modification ribosomal RNA small subunit methyltransferase A (TIGR00755; EC 2.1.1.182; HMM-score: 17.6)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll magnesium protoporphyrin O-methyltransferase (TIGR02021; EC 2.1.1.11; HMM-score: 17.6)
    Genetic information processing Protein fate Protein modification and repair protein-L-isoaspartate O-methyltransferase (TIGR00080; EC 2.1.1.77; HMM-score: 16.5)
    Metabolism Amino acid biosynthesis Aspartate family methionine biosynthesis protein MetW (TIGR02081; HMM-score: 16.3)
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA (guanine-N(7)-)-methyltransferase (TIGR00091; EC 2.1.1.33; HMM-score: 15.7)
    Genetic information processing Protein synthesis tRNA and rRNA base modification 16S rRNA (cytosine(967)-C(5))-methyltransferase (TIGR00563; EC 2.1.1.176; HMM-score: 13.4)
    Genetic information processing Protein synthesis tRNA and rRNA base modification N2,N2-dimethylguanosine tRNA methyltransferase (TIGR00308; EC 2.1.1.-; HMM-score: 13.2)
    methyltransferase, FkbM family (TIGR01444; HMM-score: 13.2)
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification putative protein-(glutamine-N5) methyltransferase, unknown substrate-specific (TIGR03704; EC 2.1.1.-; HMM-score: 11.9)
    Genetic information processing Transcription RNA processing 3' terminal RNA ribose 2'-O-methyltransferase Hen1 (TIGR04074; EC 2.1.1.-; HMM-score: 11.8)
    Genetic information processing Protein synthesis tRNA and rRNA base modification 3' terminal RNA ribose 2'-O-methyltransferase Hen1 (TIGR04074; EC 2.1.1.-; HMM-score: 11.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll C-20 methyltransferase BchU (TIGR02716; EC 2.1.1.-; HMM-score: 11.6)
  • TheSEED  :
    • 16S rRNA (guanine(1207)-N(2))-methyltransferase (EC 2.1.1.172)
  • ⊞PFAM:
    NADP_Rossmann (CL0063) MTS; Methyltransferase small domain (PF05175; HMM-score: 179.5)
    and 21 more
    Methyltransf_31; Methyltransferase domain (PF13847; HMM-score: 48)
    Methyltransf_25; Methyltransferase domain (PF13649; HMM-score: 38.1)
    GidB; rRNA small subunit methyltransferase G (PF02527; HMM-score: 28.9)
    Methyltransf_12; Methyltransferase domain (PF08242; HMM-score: 28.7)
    Methyltransf_11; Methyltransferase domain (PF08241; HMM-score: 28.1)
    PrmA; Ribosomal protein L11 methyltransferase (PrmA) (PF06325; HMM-score: 24.7)
    Methyltransf_18; Methyltransferase domain (PF12847; HMM-score: 24.5)
    TRM5-TYW2_MTfase; TRM5/TYW2 methyltransferase domain (PF02475; HMM-score: 22.9)
    Methyltransf_4; Putative methyltransferase (PF02390; HMM-score: 22.1)
    Cons_hypoth95; Conserved hypothetical protein 95 (PF03602; HMM-score: 21.2)
    TehB; Tellurite resistance protein TehB (PF03848; HMM-score: 20.2)
    Methyltransf_16; Lysine methyltransferase (PF10294; HMM-score: 19.9)
    Methyltransf_23; Methyltransferase domain (PF13489; HMM-score: 19.5)
    TRM; N2,N2-dimethylguanosine tRNA methyltransferase (PF02005; HMM-score: 19.2)
    UPF0020; RMKL-like, methyltransferase domain (PF01170; HMM-score: 19.1)
    PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT) (PF01135; HMM-score: 18.4)
    Ubie_methyltran; ubiE/COQ5 methyltransferase family (PF01209; HMM-score: 18.3)
    no clan defined MTS_N; Methyltransferase small domain N-terminal (PF08468; HMM-score: 17.5)
    NADP_Rossmann (CL0063) Methyltr_RsmB-F; 16S rRNA methyltransferase RsmB/F (PF01189; HMM-score: 17.4)
    Methyltransf_15; RNA cap guanine-N2 methyltransferase (PF09445; HMM-score: 14.9)
    Eco57I; Eco57I restriction-modification methylase (PF07669; HMM-score: 12.7)

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

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

⊟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
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.9969
    • Cytoplasmic Membrane Score: 0.0007
    • Cell wall & surface Score: 0.0002
    • Extracellular Score: 0.0021
  • ⊞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): 0.009464
    • TAT(Tat/SPI): 0.000641
    • LIPO(Sec/SPII): 0.00128
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSHYYDEDPSVISNEQRIQYQLNHHKIDLITDNGVFSKDKVDYGSDVLVQTFLKAHPPGPSKRIADVGCGYGPIGLMIAKVSPHHSITMLDVNHRALALVEKNKKLNGIDNVIVKESDALSAVEDKSFDFILTNPPIRAGKETVHRIFEQALHRLDSNGELFVVIQKKQGMPSAKKRMNELFGNVEVVNKDKGYYILRSIKA

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 180 [4]
  • 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: 41.63 h [5]

⊞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, 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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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