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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1148 [new locus tag: SACOL_RS05865 ]
  • pan locus tag?: SAUPAN003374000
  • symbol: pheS
  • pan gene symbol?: pheS
  • synonym:
  • product: phenylalanyl-tRNA synthetase subunit alpha

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1148 [new locus tag: SACOL_RS05865 ]
  • symbol: pheS
  • product: phenylalanyl-tRNA synthetase subunit alpha
  • replicon: chromosome
  • strand: +
  • coordinates: 1155545..1156603
  • length: 1059
  • 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
    ATGTCTGAACAACAAACAATGTCAGAGTTAAAACAACAAGCGCTTGTAGATATTAATGAA
    GCAAATGATGAACGTGCACTGCAAGAAGTTAAAGTGAAATACTTAGGTAAAAAAGGGTCA
    GTTAGCGGACTAATGAAATTGATGAAGGATTTGCCGAATGAAGATAAACCTGCGTTTGGT
    CAAAAAGTGAATGAATTGCGTCAAACAATTCAAAATGAATTAGATGAAAGACAACAGATG
    TTAGTTAAAGAAAAATTAAATAAGCAATTGGCTGAAGAAACAATTGATGTATCATTACCA
    GGTCGTCATATTGAAATCGGTTCAAAGCATCCATTAACACGTACAATAGAAGAAATTGAA
    GACTTATTCTTAGGTTTAGGTTATGAAATTGTGAATGGATATGAAGTTGAACAAGATCAT
    TATAACTTCGAAATGCTGAATTTACCTAAATCACACCCTGCACGTGATATGCAAGATAGT
    TTCTATATTACGGATGAAATTTTATTACGTACGCATACATCACCAGTGCAGGCACGTACG
    ATGGAATCACGTCATGGTCAAGGTCCAGTTAAAATTATTTGCCCTGGTAAAGTGTATCGT
    CGTGACTCTGATGATGCGACACATAGTCATCAATTTACACAAATCGAAGGATTAGTTGTT
    GATAAAAACGTTAAAATGAGTGATTTGAAAGGTACTTTAGAATTGTTAGCTAAGAAATTA
    TTTGGTGCTGATCGTGAAATTCGTTTACGTCCAAGTTACTTCCCATTCACTGAACCTTCT
    GTAGAAGTTGATGTGTCATGTTTTAAATGTAAAGGAAAAGGTTGTAATGTGTGTAAACAC
    ACAGGATGGATTGAAATTTTAGGTGCTGGAATGGTACATCCTAATGTATTAGAAATGGCT
    GGTTTTGATTCTTCAGAGTACTCTGGATTTGCATTTGGTATGGGACCAGACCGTATTGCA
    ATGTTGAAATATGGTATAGAAGATATTCGTCATTTCTATACTAATGATGTGAGATTTTTA
    GATCAATTTAAAGCGGTAGAAGATAGAGGTGACATGTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1059

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1148 [new locus tag: SACOL_RS05865 ]
  • symbol: PheS
  • description: phenylalanyl-tRNA synthetase subunit alpha
  • length: 352
  • theoretical pI: 5.47515
  • theoretical MW: 40106.4
  • GRAVY: -0.540057

⊟Function[edit | edit source]

  • reaction:
    EC 6.1.1.20?  ExPASy
    Phenylalanine--tRNA ligase ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
  • TIGRFAM:
    Genetic information processing Protein synthesis tRNA aminoacylation phenylalanine--tRNA ligase, alpha subunit (TIGR00468; EC 6.1.1.20; HMM-score: 380.5)
    and 7 more
    Genetic information processing Protein synthesis tRNA aminoacylation phenylalanine--tRNA ligase (TIGR00469; EC 6.1.1.20; HMM-score: 124.3)
    Genetic information processing Protein synthesis tRNA aminoacylation O-phosphoserine--tRNA ligase (TIGR00470; EC 6.1.1.27; HMM-score: 48.9)
    Metabolism Amino acid biosynthesis Serine family O-phosphoserine--tRNA ligase (TIGR00470; EC 6.1.1.27; HMM-score: 48.9)
    Genetic information processing Protein synthesis tRNA aminoacylation phenylalanine--tRNA ligase, beta subunit (TIGR00471; EC 6.1.1.20; HMM-score: 18.9)
    Genetic information processing Protein synthesis tRNA aminoacylation pyrrolysine--tRNA ligase, C-terminal region (TIGR02367; EC 6.1.1.26; HMM-score: 15.6)
    Metabolism Amino acid biosynthesis Histidine family ATP phosphoribosyltransferase, regulatory subunit (TIGR00443; HMM-score: 13.3)
    Genetic information processing Transcription Degradation of RNA ribonuclease, Rne/Rng family (TIGR00757; EC 3.1.4.-; HMM-score: 6.9)
  • TheSEED  :
    • Phenylalanyl-tRNA synthetase alpha chain (EC 6.1.1.20)
    Protein Metabolism Protein biosynthesis tRNA aminoacylation, Phe  Phenylalanyl-tRNA synthetase alpha chain (EC 6.1.1.20)
  • PFAM:
    tRNA_synt_II (CL0040) tRNA-synt_2d; tRNA synthetases class II core domain (F) (PF01409; HMM-score: 361.7)
    and 3 more
    tRNA_bind_arm (CL0298) Phe_tRNA-synt_N; Aminoacyl tRNA synthetase class II, N-terminal domain (PF02912; HMM-score: 85)
    no clan defined ORF11CD3; ORF11CD3 domain (PF10549; HMM-score: 12.5)
    tRNA_synt_II (CL0040) tRNA-synt_His; Histidyl-tRNA synthetase (PF13393; HMM-score: 9.7)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors: Mg2+
  • 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): 0.003802
    • TAT(Tat/SPI): 0.003535
    • LIPO(Sec/SPII): 0.000434
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSEQQTMSELKQQALVDINEANDERALQEVKVKYLGKKGSVSGLMKLMKDLPNEDKPAFGQKVNELRQTIQNELDERQQMLVKEKLNKQLAEETIDVSLPGRHIEIGSKHPLTRTIEEIEDLFLGLGYEIVNGYEVEQDHYNFEMLNLPKSHPARDMQDSFYITDEILLRTHTSPVQARTMESRHGQGPVKIICPGKVYRRDSDDATHSHQFTQIEGLVVDKNVKMSDLKGTLELLAKKLFGADREIRLRPSYFPFTEPSVEVDVSCFKCKGKGCNVCKHTGWIEILGAGMVHPNVLEMAGFDSSEYSGFAFGMGPDRIAMLKYGIEDIRHFYTNDVRFLDQFKAVEDRGDM

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 455 [4]
  • interaction partners:
    SACOL1734(gapA2)glyceraldehyde 3-phosphate dehydrogenase 2  [5] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL1149(pheT)phenylalanyl-tRNA synthetase subunit beta  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [5] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [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)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: T-box(Phe) (transcription antitermination) regulon
    T-box(Phe)(RNA)important in Amino acid metabolism; regulatory site identified based on RegPrecise data for N315 RegPrecise 

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: 66.7 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. ↑ 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 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)
  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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