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NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1700 [new locus tag: SACOL_RS08670 ]
  • pan locus tag?: SAUPAN004251000
  • symbol: rpmA
  • pan gene symbol?: rpmA
  • synonym:
  • product: 50S ribosomal protein L27

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1700 [new locus tag: SACOL_RS08670 ]
  • symbol: rpmA
  • product: 50S ribosomal protein L27
  • replicon: chromosome
  • strand: -
  • coordinates: 1732531..1732815
  • length: 285
  • 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
    ATGTTAAAATTAAACTTACAATTCTTCGCATCTAAAAAAGGGGTAAGTTCTACAAAAAAC
    GGACGTGACTCTGAATCAAAACGCTTAGGTGCTAAACGTGCTGACGGTCAATTCGTAACA
    GGTGGTTCAATTTTATATCGCCAACGTGGTACTAAAATTTACCCTGGTGAAAATGTAGGT
    CGTGGTGGCGATGATACATTATTCGCTAAAATCGACGGCGTTGTTAAATTCGAACGTAAA
    GGTCGCGACAAAAAACAAGTTTCTGTATATGCAGTAGCTGAATAA
    60
    120
    180
    240
    285

Protein[edit | edit source]

Protein Data Bank: 4WCE
Protein Data Bank: 4WF9
Protein Data Bank: 4WFA
Protein Data Bank: 4WFB
Protein Data Bank: 5HKV
Protein Data Bank: 5HL7
Protein Data Bank: 5LI0
Protein Data Bank: 5ND8
Protein Data Bank: 5ND9
Protein Data Bank: 5NRG
Protein Data Bank: 5TCU

General[edit | edit source]

  • locus tag: SACOL1700 [new locus tag: SACOL_RS08670 ]
  • symbol: RpmA
  • description: 50S ribosomal protein L27
  • length: 94
  • theoretical pI: 10.8424
  • theoretical MW: 10314.7
  • GRAVY: -0.689362

Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Ribosomal proteins: synthesis and modification ribosomal protein bL27 (TIGR00062; HMM-score: 132.7)
  • TheSEED  :
    • LSU ribosomal protein L27p
    Protein Metabolism Protein biosynthesis Ribosome LSU bacterial  LSU ribosomal protein L27p
  • PFAM:
    no clan defined Ribosomal_L27; Ribosomal L27 protein (PF01016; HMM-score: 117.5)

Structure, modifications & cofactors[edit | edit source]

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

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 10
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0
    • Extracellular Score: 0
    • 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): 0.021947
    • TAT(Tat/SPI): 0.003805
    • LIPO(Sec/SPII): 0.0037
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MLKLNLQFFASKKGVSSTKNGRDSESKRLGAKRADGQFVTGGSILYRQRGTKIYPGENVGRGGDDTLFAKIDGVVKFERKGRDKKQVSVYAVAE

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 2042 [4]
  • interaction partners:

Expression & Regulation[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: 9.65 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]