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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0818 [new locus tag: SACOL_RS04205 ]
  • pan locus tag?: SAUPAN002664000
  • symbol: prfB
  • pan gene symbol?: prfB
  • synonym:
  • product: peptide chain release factor 2

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0818 [new locus tag: SACOL_RS04205 ]
  • symbol: prfB
  • product: peptide chain release factor 2
  • replicon: chromosome
  • strand: +
  • coordinates: join(841862..841933,841935..842972)
  • length: 1110
  • 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
    961
    1021
    1081
    ATGGAATTATCAGAAATCAAACGAAATATAGATAAGTATAATCAAGATTTAACACAAATT
    AGGGGGTCTCTTGACTTAGAGAACAAAGAAACTAATATTCAAGAATATGAAGAAATGATG
    GCAGAACCTAATTTTTGGGATAACCAAACGAAAGCGCAAGATATTATAGATAAAAATAAT
    GCGTTAAAAGCAATAGTTAATGGTTATAAAACACTACAAGCAGAAGTAGATGACATGGAT
    GCTACTTGGGATTTATTACAAGAAGAATTTGATGAAGAAATGAAAGAAGACTTAGAGCAA
    GAGGTCATTAATTTTAAGGCTAAAGTGGATGAATACGAATTGCAATTATTATTAGATGGG
    CCTCACGATGCCAATAACGCAATTCTAGAGTTACATCCTGGTGCAGGTGGCACGGAGTCT
    CAAGATTGGGCTAATATGCTATTTAGAATGTATCAACGTTATTGTGAGAAGAAAGGCTTT
    AAAGTTGAAACTGTTGATTATCTACCTGGGGATGAAGCGGGGATTAAAAGTGTAACATTG
    CTCATCAAAGGGCATAATGCTTATGGTTATTTAAAAGCTGAAAAAGGTGTACACCGACTA
    GTACGAATTTCTCCATTTGATTCATCAGGACGTCGTCATACATCATTTGCATCATGCGAC
    GTTATTCCAGATTTTAATAATGATGAAATAGAGATTGAAATCAATCCGGATGATATTACA
    GTTGATACATTCAGAGCTTCTGGTGCAGGTGGTCAGCATATTAACAAAACTGAATCGGCA
    ATACGAATTACCCACCACCCCTCAGGTATAGTTGTTAATAACCAAAATGAACGTTCTCAA
    ATTAAAAACCGTGAAGCAGCTATGAAAATGTTAAAGTCTAAATTATATCAATTAAAATTG
    GAAGAGCAGGCACGTGAAATGGCTGAAATTCGTGGCGAACAAAAAGAAATCGGCTGGGGA
    AGCCAAATTAGATCATATGTTTTCCATCCATACTCAATGGTGAAAGATCATCGTACGAAC
    GAAGAAACAGGTAAGGTTGATGCAGTGATGGATGGAGACATTGGACCATTTATCGAATCA
    TATTTAAGACAGACAATGTCGCACGATTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1110

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0818 [new locus tag: SACOL_RS04205 ]
  • symbol: PrfB
  • description: peptide chain release factor 2
  • length: 369
  • theoretical pI: 4.57447
  • theoretical MW: 42331
  • GRAVY: -0.759079

⊟Function[edit | edit source]

  • TIGRFAM:
    Genetic information processing Protein synthesis Translation factors peptide chain release factor 2 (TIGR00020; HMM-score: 532.1)
    and 5 more
    Genetic information processing Protein synthesis Translation factors peptide chain release factor 1 (TIGR00019; HMM-score: 305)
    Genetic information processing Protein synthesis Translation factors putative peptide chain release factor H (TIGR03072; HMM-score: 120.2)
    SH3 domain protein (TIGR04211; HMM-score: 9)
    Cellular processes Cellular processes Cell division chromosome segregation protein SMC (TIGR02169; HMM-score: 4.7)
    Genetic information processing DNA metabolism Chromosome-associated proteins chromosome segregation protein SMC (TIGR02169; HMM-score: 4.7)
  • TheSEED  :
    • Peptide chain release factor 2
    • programmed frameshift-containing
    Protein Metabolism Protein biosynthesis Programmed frameshift  Peptide chain release factor 2
    and 2 more
    Protein Metabolism Protein biosynthesis Programmed frameshift  programmed frameshift-containing
    Protein Metabolism Protein biosynthesis Translation termination factors bacterial  Peptide chain release factor 2
  • PFAM:
    no clan defined PCRF; PCRF domain (PF03462; HMM-score: 214.4)
    and 3 more
    RF (CL0337) RF-1; RF-1 domain (PF00472; HMM-score: 146.2)
    no clan defined Occludin_ELL; Occludin homology domain (PF07303; HMM-score: 13.4)
    CCDC-167; Coiled-coil domain-containing protein 167 (PF15188; HMM-score: 10.1)

⊟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): 0.005866
    • TAT(Tat/SPI): 0.00034
    • LIPO(Sec/SPII): 0.000817
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MELSEIKRNIDKYNQDLTQIRGSLDLENKETNIQEYEEMMAEPNFWDNQTKAQDIIDKNNALKAIVNGYKTLQAEVDDMDATWDLLQEEFDEEMKEDLEQEVINFKAKVDEYELQLLLDGPHDANNAILELHPGAGGTESQDWANMLFRMYQRYCEKKGFKVETVDYLPGDEAGIKSVTLLIKGHNAYGYLKAEKGVHRLVRISPFDSSGRRHTSFASCDVIPDFNNDEIEIEINPDDITVDTFRASGAGGQHINKTESAIRITHHPSGIVVNNQNERSQIKNREAAMKMLKSKLYQLKLEEQAREMAEIRGEQKEIGWGSQIRSYVFHPYSMVKDHRTNEETGKVDAVMDGDIGPFIESYLRQTMSHD

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 97 [4]
  • interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL2272(modA)molybdenum ABC transporter molybdenum-binding protein ModA  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [5] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [5] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [5] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [5] (data from MRSA252)
    SACOL2207(rplM)50S ribosomal protein L13  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2223(rplR)50S ribosomal protein L18  [5] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [5] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [5] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [5] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [5] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL0211acetyl-CoA acetyltransferase  [5] (data from MRSA252)
    SACOL02123-hydroxyacyl-CoA dehydrogenase  [5] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (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. ↑ 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. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 5.24 5.25 5.26 5.27 5.28 5.29 5.30 5.31 5.32 5.33 5.34 5.35 5.36 5.37 5.38 5.39 5.40 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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