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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2136 [new locus tag: SACOL_RS11180 ]
  • pan locus tag?: SAUPAN005442000
  • symbol: SACOL2136
  • pan gene symbol?: —
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2136 [new locus tag: SACOL_RS11180 ]
  • symbol: SACOL2136
  • product: hypothetical protein
  • replicon: chromosome
  • strand: -
  • coordinates: 2197465..2198130
  • length: 666
  • 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
    ATGAATATTTTGGTTATAGGTGCTAATGGCGGTGTAGGTTCGTTACTAGTGCAACAATTA
    GCAAAAGAAAATGTACCATTTACTGCTGGTGTTAGGCAATCAGATCAACTTAATGCGTTA
    AAATCACAAGGTATGAAAGCAATTCTTGTTGATGTTGAAAATGATTCAATAGAGACTTTA
    ACTGAGACGTTTAAACCATTCGATAAAGTTATCTTTTCAGTAGGTTCTGGAGGGAACACG
    GGTGCAGATAAAACAATTATTGTCGATTTAGATGGTGCTGTTAAATCAATGATTGCGAGT
    AAAGAGGCCAATATTAAACACTATGTCATGGTTTCAACATATGATTCGAGACGTCAGGCT
    TTTGATGATAGCGGTGATTTAAAGCCATATACAATAGCTAAACATTACGCTGATGACTAT
    TTAAGACGTTCAGGTTTGAATTATACAATTTTACATCCAGGGGCACTTACAAATGCAGCA
    GGATCTGGAAAGATAGAAGCTGCACAATATTTTGATGGTAAAGGTGAAATTCCTAGAGAA
    GATGTTGCGACAGTATTAAAAGAAATTGTCACATCCAATCATTTTAATCACCAAGAGTTT
    CAAATTATTAGTGGTGATCAGGACATTAAAGATGCTTTAACTCAATTTGAAAATGAAACG
    GATTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    666

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2136 [new locus tag: SACOL_RS11180 ]
  • symbol: SACOL2136
  • description: hypothetical protein
  • length: 221
  • theoretical pI: 4.70039
  • theoretical MW: 24031.7
  • GRAVY: -0.29638

⊟Function[edit | edit source]

  • TIGRFAM:
    Unknown function Enzymes of unknown specificity putative quinone oxidoreductase, YhdH/YhfP family (TIGR02823; HMM-score: 21.6)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pantothenate and coenzyme A 2-dehydropantoate 2-reductase (TIGR00745; EC 1.1.1.-; HMM-score: 18.9)
    and 9 more
    thioester reductase domain (TIGR01746; HMM-score: 16.2)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides ADP-glyceromanno-heptose 6-epimerase (TIGR02197; EC 5.1.3.20; HMM-score: 14.8)
    Metabolism Amino acid biosynthesis Aspartate family aspartate-semialdehyde dehydrogenase (TIGR01296; EC 1.2.1.11; HMM-score: 14.7)
    Metabolism Energy metabolism Fermentation zinc-binding alcohol dehydrogenase family protein (TIGR02817; HMM-score: 13.1)
    acetoacetyl-CoA reductase (TIGR01829; EC 1.1.1.36; HMM-score: 12.6)
    Metabolism Transport and binding proteins Carbohydrates, organic alcohols, and acids ABC transporter, substrate binding protein, PQQ-dependent alcohol dehydrogenase system (TIGR03863; HMM-score: 12.3)
    ergot alkaloid biosynthesis protein, AFUA_2G17970 family (TIGR03649; HMM-score: 12.2)
    Cell structure Cell envelope Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides dTDP-4-dehydrorhamnose reductase (TIGR01214; EC 1.1.1.133; HMM-score: 11.9)
    crotonyl-CoA carboxylase/reductase (TIGR01751; EC 1.3.1.85; HMM-score: 10.7)
  • TheSEED  :
    • oxidoreductase ylbE
  • PFAM:
    NADP_Rossmann (CL0063) NAD_binding_10; NAD(P)H-binding (PF13460; HMM-score: 138.7)
    and 10 more
    NmrA; NmrA-like family (PF05368; HMM-score: 44.6)
    Epimerase; NAD dependent epimerase/dehydratase family (PF01370; HMM-score: 36.6)
    3Beta_HSD; 3-beta hydroxysteroid dehydrogenase/isomerase family (PF01073; HMM-score: 20.8)
    ApbA; Ketopantoate reductase PanE/ApbA (PF02558; HMM-score: 19.2)
    RmlD_sub_bind; RmlD substrate binding domain (PF04321; HMM-score: 18.8)
    adh_short; short chain dehydrogenase (PF00106; HMM-score: 16.1)
    DapB_N; Dihydrodipicolinate reductase, N-terminus (PF01113; HMM-score: 14.5)
    Semialdhyde_dh; Semialdehyde dehydrogenase, NAD binding domain (PF01118; HMM-score: 13.7)
    TrkA_N; TrkA-N domain (PF02254; HMM-score: 13)
    NAD_binding_4; Male sterility protein (PF07993; HMM-score: 12.3)

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

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

⊟Localization[edit | edit source]

  • PSORTb: unknown (no significant prediction)
    • Cytoplasmic Score: 2.5
    • Cytoplasmic Membrane Score: 2.5
    • Cellwall Score: 2.5
    • Extracellular Score: 2.5
    • 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): 0.021841
    • TAT(Tat/SPI): 0.001265
    • LIPO(Sec/SPII): 0.003331
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MNILVIGANGGVGSLLVQQLAKENVPFTAGVRQSDQLNALKSQGMKAILVDVENDSIETLTETFKPFDKVIFSVGSGGNTGADKTIIVDLDGAVKSMIASKEANIKHYVMVSTYDSRRQAFDDSGDLKPYTIAKHYADDYLRRSGLNYTILHPGALTNAAGSGKIEAAQYFDGKGEIPREDVATVLKEIVTSNHFNHQEFQIISGDQDIKDALTQFENETD

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 1454 [4]
  • interaction partners:

⊟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: 50.25 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. ↑ 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. ↑ 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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