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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1788 [new locus tag: SACOL_RS09165 ]
  • pan locus tag?: SAUPAN004405000
  • symbol: SACOL1788
  • pan gene symbol?: —
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1788 [new locus tag: SACOL_RS09165 ]
  • symbol: SACOL1788
  • product: hypothetical protein
  • replicon: chromosome
  • strand: -
  • coordinates: 1833625..1835142
  • length: 1518
  • 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
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    ATGACGCAGCAACAAAATGATAAAAGAACATTAAAAAATAAACACACTTATCAAAATGAA
    CCACTACCAAACCGTAAAGATTTTGTTGTTAGTTTTATAACTGGCGCGCTTGTTGGTTCA
    GCTTTAGGTTTGTATTTTAAAAATAAAGTTTATCAAAAAGCAGATGATTTAAAAGTCAAA
    GAACAAGAACTGTCGCAAAAGTTTGAAGAAAGAAAAACGCAACTTGAAGAAACGGTTGCC
    TATACAAAAGAACGTGTTGAAGGATTTTTAAACAAATCTAAAAATGAGCAAGCGGCATTA
    AAGGCACAACAAGCAGCGATAAAAGAAGAAGCAAGTGCAAATAATTTAAGTGATACATCA
    CAAGAAGCACAAGAGATTCAAGAAGCTAAAAGAGAAGCACAAGCAGAAGCGGATAAAAGT
    GTGGCTGTATCAAATAAAGAATCAAAAGCAGTGGCATTGAAAGCACAACAAGCAGCGATA
    AAAGAAGAAGCAAGTGCAAATAATTTGAGTGATACATCACAAGAGGCACAAGAGATTCAA
    GAAGCTAAAAAAGAAGCACAAGCAGAAACAGATAAAAGTGCAGCTGTATCAAATGAAGAA
    CCAAAAGCAGTGGCATTGAAAGCACAACAAGCAGCGATAAAAGAAGAAGCAAGTGCAAAT
    AATTTAAGTGATACATCACAAGAGGCACAAGAGGTTCAAGAAGCTAAAAAAGAAGCACAA
    GCAGAAACAGATAAAAGTGCAGCTGTATCAAATGAAGAACCAAAAGCAGTGGCATTGAAA
    GCACAACAAGCAGCGATAAAAGAAGAAGCAAGTGCAAATAATTTAAGTGATATATCACAA
    GAGGCACAAGAGGTTCAAGAAGCTAAAAAAGAAGCACAAGCAGAGAAAGACAGTGACACA
    TTAACTAAAGATGCAAGTGCAGCAAAGGTAGAAGTATCAAAACCAGAGTCACAAGCTGAA
    AGATTAGCAAACGCTGCAAAACAGAAGCAAGCTAAATTAACACCAGGTTCAAAAGAGAGT
    CAATTAACTGAAGCGTTATTTGCAGAAAAACCAGTTGCTAAAAATGACTTGAAAGAAATT
    CCTCAATTAGTTACTAAAAAGAATGATGTATCAGAGACAGAGACGGTTAATATAGATAAT
    AAAGACACTGTTAAACAAAAAGAAGCTAAATTTGAAAATGGTGTTATTACACGTAAAGCT
    GATGAAAAAACAACTAATAATACAGCTGTTGACAAGAAATCAGGTAAACAATCTAAAAAA
    ACAACACCTTCAAATAAACGAAATGCATCAAAAGCATCTACAAATAAAACTTCAGGTCAG
    AAAAAGCAACATAATAAGAAATCATCACAAGGTGCAAAGAAACAAAGTAGTTCAAGTAAG
    TCAACTCAAAAGAATAATCAAACTAGTAATAAGAATTCAAAAACAACAAATGCTAAATCA
    TCCAATGCATCAAAAACGCCAAATGCTAAAGTTGAGAAAGCTAAAAGTAAAATAGAGAAA
    CGTACATTCAATGACTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1518

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1788 [new locus tag: SACOL_RS09165 ]
  • symbol: SACOL1788
  • description: hypothetical protein
  • length: 505
  • theoretical pI: 9.87695
  • theoretical MW: 55090.3
  • GRAVY: -1.18812

⊟Function[edit | edit source]

  • TIGRFAM:
  • TheSEED  :
    • Maebl
  • PFAM:

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cellwall
    • Cytoplasmic Score: 0.01
    • Cytoplasmic Membrane Score: 0.11
    • Cellwall Score: 9.25
    • Extracellular Score: 0.63
    • Internal Helices: 0
  • LocateP: N-terminally anchored (No CS)
    • Prediction by SwissProt Classification: Membrane
    • Pathway Prediction: Sec-(SPI)
    • Intracellular possibility: 0.17
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 5
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.014086
    • TAT(Tat/SPI): 0.022843
    • LIPO(Sec/SPII): 0.00329
  • predicted transmembrane helices (TMHMM): 1

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTQQQNDKRTLKNKHTYQNEPLPNRKDFVVSFITGALVGSALGLYFKNKVYQKADDLKVKEQELSQKFEERKTQLEETVAYTKERVEGFLNKSKNEQAALKAQQAAIKEEASANNLSDTSQEAQEIQEAKREAQAEADKSVAVSNKESKAVALKAQQAAIKEEASANNLSDTSQEAQEIQEAKKEAQAETDKSAAVSNEEPKAVALKAQQAAIKEEASANNLSDTSQEAQEVQEAKKEAQAETDKSAAVSNEEPKAVALKAQQAAIKEEASANNLSDISQEAQEVQEAKKEAQAEKDSDTLTKDASAAKVEVSKPESQAERLANAAKQKQAKLTPGSKESQLTEALFAEKPVAKNDLKEIPQLVTKKNDVSETETVNIDNKDTVKQKEAKFENGVITRKADEKTTNNTAVDKKSGKQSKKTTPSNKRNASKASTNKTSGQKKQHNKKSSQGAKKQSSSSKSTQKNNQTSNKNSKTTNAKSSNASKTPNAKVEKAKSKIEKRTFND

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cell wall associated [1] [2] [3]
  • quantitative data / protein copy number per cell:
  • interaction partners:
    SACOL2095(atpD)F0F1 ATP synthase subunit beta  [4] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [4] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [4] (data from MRSA252)
    SACOL2105(glyA)serine hydroxymethyltransferase  [4] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [4] (data from MRSA252)
    SACOL1727(infC)translation initiation factor IF-3  [4] (data from MRSA252)
    SACOL0033(mecA)penicillin-binding protein 2'  [4] (data from MRSA252)
    SACOL1390(parC)DNA topoisomerase IV subunit A  [4] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [4] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [4] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [4] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [4] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [4] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [4] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [4] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [4] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [4] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [4] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [4] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [4] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [4] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [4] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [4] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [4] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [4] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [4] (data from MRSA252)
    SACOL2112(rpmE2)50S ribosomal protein L31  [4] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [4] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [4] (data from MRSA252)
    SACOL0437(rpsF)30S ribosomal protein S6  [4] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [4] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [4] (data from MRSA252)
    SACOL0591(rpsL)30S ribosomal protein S12  [4] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [4] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [4] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [4] (data from MRSA252)
    SACOL1202(ylmF)hypothetical protein  [4] (data from MRSA252)
    SACOL03035'-nucleotidase  [4] (data from MRSA252)
    SACOL0555cell division protein FtsH  [4] (data from MRSA252)
    SACOL0721hypothetical protein  [4] (data from MRSA252)
    SACOL1484hypothetical protein  [4] (data from MRSA252)
    SACOL1651hypothetical protein  [4] (data from MRSA252)
    SACOL1692bifunctional preprotein translocase subunit SecD/SecF  [4] (data from MRSA252)
    SACOL1753universal stress protein  [4] (data from MRSA252)
    SACOL1777serine protease HtrA  [4] (data from MRSA252)
    SACOL1791FtsK/SpoIIIE family protein  [4] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: SigB* (activation) regulon
    SigB*(sigma factor)controlling a large regulon involved in stress/starvation response and adaptation [5] [6]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 9.28 h [7]

⊟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. ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 4.28 4.29 4.30 4.31 4.32 4.33 4.34 4.35 4.36 4.37 4.38 4.39 4.40 4.41 4.42 4.43 4.44 4.45 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)
  5. ↑ Markus Bischoff, Paul Dunman, Jan Kormanec, Daphne Macapagal, Ellen Murphy, William Mounts, Brigitte Berger-Bächi, Steven Projan
    Microarray-based analysis of the Staphylococcus aureus sigmaB regulon.
    J Bacteriol: 2004, 186(13);4085-99
    [PubMed:15205410] [WorldCat.org] [DOI] (P p)
  6. ↑ Jan Pané-Farré, Beate Jonas, Konrad Förstner, Susanne Engelmann, Michael Hecker
    The sigmaB regulon in Staphylococcus aureus and its regulation.
    Int J Med Microbiol: 2006, 296(4-5);237-58
    [PubMed:16644280] [WorldCat.org] [DOI] (P p)
  7. ↑ 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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