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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1635 [new locus tag: SACOL_RS08335 ]
  • pan locus tag?: SAUPAN004161000
  • symbol: prmA
  • pan gene symbol?: prmA
  • synonym:
  • product: 50S ribosomal protein L11 methyltransferase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1635 [new locus tag: SACOL_RS08335 ]
  • symbol: prmA
  • product: 50S ribosomal protein L11 methyltransferase
  • replicon: chromosome
  • strand: -
  • coordinates: 1664357..1665295
  • length: 939
  • 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
    661
    721
    781
    841
    901
    ATGAACTGGACAGAGCTTTCAATTATTATTAATCATGAAGCAGTAGAATTGGCTACCAAT
    ATACTTGAAAATCATGGATCAAATGGTGTCGTGATAGAAGATTCAGATGGTTTAATTAAC
    CAACCAGAAGATAAATACGGTGAAATTTACGCTTTGAAAAAAGAGGATTATCCAGATAAG
    GGAGTAAGATTGAAAGCCTATTTTAATGAAATGACTTATGATGATAAGTTGCGACAGCAA
    ATTAAAGATGAGTTATTAAATTTAGATGAACTTGATCAACATAACGTTCAATTCAGTGAG
    CAAATTATTGCAGAGACGGATTGGGAAAATGAATGGAAAAACTATTTCCATCCATTCCGA
    GCGTCGAAGAAGTTCACAATAGTTCCTAGTTGGGAAACATATGCTAAAGAAGCGGATGAA
    GAGCTTTGCATTGAGCTCGACCCAGGTATGGCTTTTGGAACAGGTGATCATCCGACTACA
    AGTATGTGTTTGAAGGCAATAGAAACATATGTATTGCCACAGCATTCAGTAATTGATGTT
    GGTACTGGCTCAGGTATATTAAGTATTGCAAGTCATCTAATCGGTGTAAAACGTATTAAA
    GCGTTGGATATTGATGAAATGGCAGTGAGTGTAGCTAAAGAAAACTTCAGAAGAAATCAT
    TGTGAAACGTTAATTGAAGCTGTTCCAGGTAACTTATTGAAAGACGAAACAGAAAAATTT
    GATATTGTAATAGCAAATATTTTAGCGCATATTATTGATGAAATGATTGAAGATGCTTAT
    AATACTCTAAATGAAGGCGGTTATTTTATTACTTCTGGTATTATAAAAGAGAAGTATGAA
    GGTATACAGTCACATATGGAGCGTGTAGGTTTTAAAATTATTTCAGAACAACATGACAAC
    GGTTGGGTTTGTCTTGTTGGCCAGAAAGTGAGTGAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    939

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1635 [new locus tag: SACOL_RS08335 ]
  • symbol: PrmA
  • description: 50S ribosomal protein L11 methyltransferase
  • length: 312
  • theoretical pI: 4.36505
  • theoretical MW: 35454.7
  • GRAVY: -0.366987

⊟Function[edit | edit source]

  • reaction:
    EC 2.1.1.-?  ExPASy
  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein L11 methyltransferase (TIGR00406; EC 2.1.1.-; HMM-score: 255.1)
    and 13 more
    Genetic information processing Protein fate Protein modification and repair protein-(glutamine-N5) methyltransferase, release factor-specific (TIGR03534; EC 2.1.1.-; HMM-score: 45.4)
    Genetic information processing Protein fate Protein modification and repair methyltransferase, HemK family (TIGR00536; HMM-score: 39.6)
    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: 37.7)
    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: 37.6)
    Unknown function Enzymes of unknown specificity putative methylase (TIGR00537; HMM-score: 36.7)
    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: 32)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll magnesium protoporphyrin O-methyltransferase (TIGR02021; EC 2.1.1.11; HMM-score: 30.4)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Biotin malonyl-acyl carrier protein O-methyltransferase BioC (TIGR02072; EC 2.1.1.-; HMM-score: 24.5)
    methyltransferase, ATP-grasp peptide maturase system (TIGR04188; HMM-score: 18.4)
    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: 17)
    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: 16.2)
    Genetic information processing Protein synthesis tRNA and rRNA base modification ribosomal RNA small subunit methyltransferase A (TIGR00755; EC 2.1.1.182; HMM-score: 15.5)
    Hypothetical proteins Conserved putative methyltransferase, TIGR01177 family (TIGR01177; HMM-score: 14.6)
  • TheSEED  :
    • Ribosomal protein L11 methyltransferase (EC 2.1.1.-)
    Protein Metabolism Protein biosynthesis Ribosome biogenesis bacterial  Ribosomal protein L11 methyltransferase (EC 2.1.1.-)
    and 1 more
    Stress Response Heat shock Heat shock dnaK gene cluster extended  Ribosomal protein L11 methyltransferase (EC 2.1.1.-)
  • PFAM:
    NADP_Rossmann (CL0063) PrmA; Ribosomal protein L11 methyltransferase (PrmA) (PF06325; HMM-score: 355.6)
    and 14 more
    MTS; Methyltransferase small domain (PF05175; HMM-score: 56.6)
    Methyltransf_31; Methyltransferase domain (PF13847; HMM-score: 40.3)
    Methyltransf_18; Methyltransferase domain (PF12847; HMM-score: 36)
    Methyltransf_25; Methyltransferase domain (PF13649; HMM-score: 35.8)
    Methyltransf_11; Methyltransferase domain (PF08241; HMM-score: 30.8)
    Methyltransf_12; Methyltransferase domain (PF08242; HMM-score: 27.9)
    Methyltransf_23; Methyltransferase domain (PF13489; HMM-score: 24.8)
    Met_10; Met-10+ like-protein (PF02475; HMM-score: 19.3)
    PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT) (PF01135; HMM-score: 18.7)
    Spermine_synth; Spermine/spermidine synthase domain (PF01564; HMM-score: 17.9)
    Cons_hypoth95; Conserved hypothetical protein 95 (PF03602; HMM-score: 15.7)
    UPF0020; Putative RNA methylase family UPF0020 (PF01170; HMM-score: 13)
    GidB; rRNA small subunit methyltransferase G (PF02527; HMM-score: 12.9)
    TRM; N2,N2-dimethylguanosine tRNA methyltransferase (PF02005; HMM-score: 12)

⊟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): 0.008118
    • TAT(Tat/SPI): 0.000273
    • LIPO(Sec/SPII): 0.001161
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MNWTELSIIINHEAVELATNILENHGSNGVVIEDSDGLINQPEDKYGEIYALKKEDYPDKGVRLKAYFNEMTYDDKLRQQIKDELLNLDELDQHNVQFSEQIIAETDWENEWKNYFHPFRASKKFTIVPSWETYAKEADEELCIELDPGMAFGTGDHPTTSMCLKAIETYVLPQHSVIDVGTGSGILSIASHLIGVKRIKALDIDEMAVSVAKENFRRNHCETLIEAVPGNLLKDETEKFDIVIANILAHIIDEMIEDAYNTLNEGGYFITSGIIKEKYEGIQSHMERVGFKIISEQHDNGWVCLVGQKVSE

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 91 [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: 88.98 h [6]

⊟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. ↑ Arnaud Chastanet, Juliette Fert, Tarek Msadek
    Comparative genomics reveal novel heat shock regulatory mechanisms in Staphylococcus aureus and other Gram-positive bacteria.
    Mol Microbiol: 2003, 47(4);1061-73
    [PubMed:12581359] [WorldCat.org] [DOI] (P p)
  6. ↑ 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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