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NCBI: 26-AUG-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA2502 [new locus tag: SA_RS14305 ]
  • pan locus tag?: SAUPAN006490000
  • symbol: rnpA
  • pan gene symbol?: rnpA
  • synonym:
  • product: ribonuclease P

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SA2502 [new locus tag: SA_RS14305 ]
  • symbol: rnpA
  • product: ribonuclease P
  • replicon: chromosome
  • strand: -
  • coordinates: 2813991..2814338
  • length: 348
  • essential: yes 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
    TTGGAAAAAGCTTACCGAATTAAAAAGAATGCAGATTTTCAGAGAATATATAAAAAAGGT
    CATTCTGTAGCCAACAGACAATTTGTTGTATACACTTGTAATAATAAAGAAATAGACCAT
    TTTCGCTTAGGTATTAGTGTTTCTAAAAAACTAGGTAATGCAGTGTTAAGAAACAAGATT
    AAAAGAGCAATACGTGAAAATTTCAAAGTACATAAGTCGCATATATTGGCCAAAGATATT
    ATTGTAATAGCAAGACAGCCAGCTAAAGATATGACGACTTTACAAATACAGAATAGTCTT
    GAGCACGTACTTAAAATTGCCAAAGTTTTTAATAAAAAGATTAAGTAA
    60
    120
    180
    240
    300
    348

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SA2502 [new locus tag: SA_RS14305 ]
  • symbol: RnpA
  • description: ribonuclease P
  • length: 115
  • theoretical pI: 11.225
  • theoretical MW: 13425.8
  • GRAVY: -0.491304

⊟Function[edit | edit source]

  • reaction:
    EC 3.1.26.5?  ExPASy
    Ribonuclease P Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor
  • TIGRFAM:
    Genetic information processing Transcription RNA processing ribonuclease P protein component (TIGR00188; EC 3.1.26.5; HMM-score: 92)
    and 1 more
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides polysaccharide deacetylase family protein, PEP-CTERM locus subfamily (TIGR03006; HMM-score: 12.3)
  • TheSEED  :
    • Ribonuclease P protein component (EC 3.1.26.5)
    RNA Metabolism RNA processing and modification tRNA processing  Ribonuclease P protein component (EC 3.1.26.5)
  • PFAM:
    S5 (CL0329) Ribonuclease_P; Ribonuclease P (PF00825; HMM-score: 105.8)
    and 1 more
    no clan defined ATP-cone; ATP cone domain (PF03477; HMM-score: 15.2)

⊟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): 0.00618
    • TAT(Tat/SPI): 0.000432
    • LIPO(Sec/SPII): 0.021226
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MEKAYRIKKNADFQRIYKKGHSVANRQFVVYTCNNKEIDHFRLGISVSKKLGNAVLRNKIKRAIRENFKVHKSHILAKDIIVIARQPAKDMTTLQIQNSLEHVLKIAKVFNKKIK

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • interaction partners:
    SA0905(atl)autolysin, N-acetylmuramyl-L-alanine amidase and endo-b-N-acetylglucosaminidas  [1] (data from MRSA252)
    SA1305(hu)DNA-binding protein II  [1] (data from MRSA252)
    SA1504(infC)translation initiation factor IF-3  [1] (data from MRSA252)
    SA0038(mecA)penicillin binding protein 2 prime  [1] (data from MRSA252)
    SA1189(parC)DNA topoisomerase IV subunit A  [1] (data from MRSA252)
    SA0496(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    SA2044(rplB)50S ribosomal protein L2  [1] (data from MRSA252)
    SA2047(rplC)50S ribosomal protein L3  [1] (data from MRSA252)
    SA2046(rplD)50S ribosomal protein L4  [1] (data from MRSA252)
    SA2033(rplF)50S ribosomal protein L6  [1] (data from MRSA252)
    SA0498(rplL)50S ribosomal protein L7/L12  [1] (data from MRSA252)
    SA2029(rplO)50S ribosomal protein L15  [1] (data from MRSA252)
    SA2040(rplP)50S ribosomal protein L16  [1] (data from MRSA252)
    SA2022(rplQ)50S ribosomal protein L17  [1] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [1] (data from MRSA252)
    SA1473(rplU)50S ribosomal protein L21  [1] (data from MRSA252)
    SA2042(rplV)50S ribosomal protein L22  [1] (data from MRSA252)
    SA2045(rplW)50S ribosomal protein L23  [1] (data from MRSA252)
    SA2039(rpmC)50S ribosomal protein L29  [1] (data from MRSA252)
    SA2041(rpsC)30S ribosomal protein S3  [1] (data from MRSA252)
    SAS052(rpsD)30S ribosomal protein S4  [1] (data from MRSA252)
    SA2031(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SA0352(rpsF)30S ribosomal protein S6  [1] (data from MRSA252)
    SA0504(rpsG)30S ribosomal protein S7  [1] (data from MRSA252)
    SA2024(rpsK)30S ribosomal protein S11  [1] (data from MRSA252)
    SA2025(rpsM)30S ribosomal protein S13  [1] (data from MRSA252)
    SA1116(rpsO)30S ribosomal protein S15  [1] (data from MRSA252)
    SA2038(rpsQ)30S ribosomal protein S17  [1] (data from MRSA252)
    SA2043(rpsS)30S ribosomal protein S19  [1] (data from MRSA252)
    SA2089(sarR)hypothetical protein  [1] (data from MRSA252)
    SA1245(sucA)2-oxoglutarate dehydrogenase E1  [1] (data from MRSA252)
    SA0295hypothetical protein  [1] (data from MRSA252)
    SA0499hypothetical protein  [1] (data from MRSA252)
    SA0627hypothetical protein  [1] (data from MRSA252)
    SA0940hypothetical protein  [1] (data from MRSA252)
    SA1528hypothetical protein  [1] (data from MRSA252)
    SA1549hypothetical protein  [1] (data from MRSA252)

⊟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. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 1.28 1.29 1.30 1.31 1.32 1.33 1.34 1.35 1.36 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
    Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
    J Proteome Res: 2011, 10(3);1139-50
    [PubMed:21166474] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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