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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2739 [new locus tag: SACOL_RS14315 ]
  • 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: SACOL2739 [new locus tag: SACOL_RS14315 ]
  • symbol: rnpA
  • product: ribonuclease P
  • replicon: chromosome
  • strand: -
  • coordinates: 2808624..2808971
  • length: 348
  • 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
    TTGGAAAAAGCTTACCGAATTAAAAAGAATGCAGATTTTCAGAGAATATATAAAAAAGGT
    CATTCTGTAGCCAACAGACAATTTGTTGTATACACTTGTAATAATAAAGAAATAGACCAT
    TTTCGCTTAGGTATTAGTGTTTCTAAAAAACTAGGTAATGCAGTGTTAAGAAACAAGATT
    AAAAGAGCAATACGTGAAAATTTCAAAGTACATAAGTCGCATATATTGGCCAAAGATATT
    ATTGTAATAGCAAGACAGCCAGCTAAAGATATGACGACTTTACAAATACAGAATAGTCTT
    GAGCACGTACTTAAAATTGCCAAAGTTTTTAATAAAAAGATTAAGTAA
    60
    120
    180
    240
    300
    348

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2739 [new locus tag: SACOL_RS14315 ]
  • 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: Cytoplasmic [1]
  • quantitative data / protein copy number per cell:
  • interaction partners:
    SACOL1062(atl)bifunctional autolysin  [2] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [2] (data from MRSA252)
    SACOL1727(infC)translation initiation factor IF-3  [2] (data from MRSA252)
    SACOL0033(mecA)penicillin-binding protein 2'  [2] (data from MRSA252)
    SACOL1390(parC)DNA topoisomerase IV subunit A  [2] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [2] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [2] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [2] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [2] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [2] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [2] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [2] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [2] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [2] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [2] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [2] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [2] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [2] (data from MRSA252)
    SACOL2231(rpmC)50S ribosomal protein L29  [2] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [2] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [2] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [2] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [2] (data from MRSA252)
    SACOL0592(rpsG)30S ribosomal protein S7  [2] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [2] (data from MRSA252)
    SACOL2215(rpsM)30S ribosomal protein S13  [2] (data from MRSA252)
    SACOL1292(rpsO)30S ribosomal protein S15  [2] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [2] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [2] (data from MRSA252)
    SACOL2287(sarR)accessory regulator R  [2] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [2] (data from MRSA252)
    SACOL03035'-nucleotidase  [2] (data from MRSA252)
    SACOL0587hypothetical protein  [2] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [2] (data from MRSA252)
    SACOL1098hypothetical protein  [2] (data from MRSA252)
    SACOL1753universal stress protein  [2] (data from MRSA252)
    SACOL1777serine protease HtrA  [2] (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. ↑ 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)
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 2.21 2.22 2.23 2.24 2.25 2.26 2.27 2.28 2.29 2.30 2.31 2.32 2.33 2.34 2.35 2.36 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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