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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1662 [new locus tag: SACOL_RS08480 ]
  • pan locus tag?: SAUPAN004203000
  • symbol: SACOL1662
  • pan gene symbol?: —
  • synonym:
  • product: acetyl-CoA carboxylase, biotin carboxyl carrier protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1662 [new locus tag: SACOL_RS08480 ]
  • symbol: SACOL1662
  • product: acetyl-CoA carboxylase, biotin carboxyl carrier protein
  • replicon: chromosome
  • strand: -
  • coordinates: 1691374..1691823
  • length: 450
  • 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
    ATGAATATTGAAAAAATCGAACAAATAATCAAATTAGTGAAGGAAAATGATGTTAAGAAA
    TTTAAATATAAAAATTTTGAAGATGAAATAGAAATTGACTTCACTGACTTGAATCATTTG
    GCTGCACACAGTAATCAATCAAATCAAAGTATGAACAATAATGATTTGACAGCTTCAAAA
    GCGAATGATAACTCCGATGTTTCGACAAATGATTATCATGACATTAAATCACCAATGATA
    GGTACATTCTTTTTACAAGATAGTAAAGAATTAACTGAACCAATTGTGAATGTCGGTGAC
    AAAGTTAACAAGGGAGATATTATAGGATATGTTGAAGCGATGAAAGTATTAAACGAGGTA
    ACAACAGATGTTGCTGGAGAAATTACTGAAATAGTAGCTGATCATGGCACAAATGTTGAA
    TACGACCAAGTTTTGGTACGTATTAAGTAA
    60
    120
    180
    240
    300
    360
    420
    450

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1662 [new locus tag: SACOL_RS08480 ]
  • symbol: SACOL1662
  • description: acetyl-CoA carboxylase, biotin carboxyl carrier protein
  • length: 149
  • theoretical pI: 4.33078
  • theoretical MW: 16819.6
  • GRAVY: -0.540268

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxyl carrier protein (TIGR00531; HMM-score: 108.3)
    and 14 more
    Metabolism Central intermediary metabolism Nitrogen metabolism urea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 35.1)
    Metabolism Transport and binding proteins Cations and iron carrying compounds oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 34)
    Metabolism Energy metabolism Other oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 34)
    Metabolism Energy metabolism Pyruvate dehydrogenase dihydrolipoyllysine-residue acetyltransferase (TIGR01348; EC 2.3.1.12; HMM-score: 25.4)
    Metabolism Energy metabolism Glycolysis/gluconeogenesis pyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 25.2)
    Metabolism Energy metabolism TCA cycle dihydrolipoyllysine-residue succinyltransferase, E2 component of oxoglutarate dehydrogenase (succinyl-transferring) complex (TIGR01347; EC 2.3.1.61; HMM-score: 23.6)
    2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase (TIGR02927; EC 2.3.1.61; HMM-score: 18.5)
    Metabolism Energy metabolism ATP-proton motive force interconversion ATP synthase archaeal, A subunit (TIGR01043; EC 3.6.3.14; HMM-score: 17.3)
    selenium-dependent molybdenum hydroxylase system protein, YqeB family (TIGR03309; HMM-score: 16.7)
    Metabolism Energy metabolism Electron transport electron transport complex, RnfABCDGE type, C subunit (TIGR01945; HMM-score: 15.9)
    Metabolism Energy metabolism Amino acids and amines glycine cleavage system H protein (TIGR00527; HMM-score: 15.5)
    proline reductase-associated electron transfer protein PrdC (TIGR04481; HMM-score: 14.2)
    Metabolism Transport and binding proteins Unknown substrate efflux transporter, RND family, MFP subunit (TIGR01730; HMM-score: 12.6)
    Metabolism Energy metabolism Pyruvate dehydrogenase pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (TIGR01349; EC 2.3.1.12; HMM-score: 11.1)
  • TheSEED  :
    • Biotin carboxyl carrier protein
    Carbohydrates Central carbohydrate metabolism Pyruvate metabolism I: anaplerotic reactions, PEP  Biotin carboxyl carrier protein
  • PFAM:
    Hybrid (CL0105) Biotin_lipoyl; Biotin-requiring enzyme (PF00364; HMM-score: 67.3)
    and 7 more
    RnfC_N; RnfC Barrel sandwich hybrid domain (PF13375; HMM-score: 25.3)
    GCV_H; Glycine cleavage H-protein (PF01597; HMM-score: 21.1)
    Biotin_lipoyl_2; Biotin-lipoyl like (PF13533; HMM-score: 19.1)
    no clan defined ATP-synt_ab_Xtn; ATPsynthase alpha/beta subunit N-term extension (PF16886; HMM-score: 18.4)
    BET; Bromodomain extra-terminal - transcription regulation (PF17035; HMM-score: 16.1)
    Hybrid (CL0105) Peptidase_M23; Peptidase family M23 (PF01551; HMM-score: 13.8)
    no clan defined DUF1374; Protein of unknown function (DUF1374) (PF07118; HMM-score: 11.9)

⊟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): 0.024442
    • TAT(Tat/SPI): 0.000791
    • LIPO(Sec/SPII): 0.001078
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MNIEKIEQIIKLVKENDVKKFKYKNFEDEIEIDFTDLNHLAAHSNQSNQSMNNNDLTASKANDNSDVSTNDYHDIKSPMIGTFFLQDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 236 [5]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: CcpA regulon
    CcpA(TF)important in Carbon catabolism; RegPrecise    transcription unit transferred from N315 data RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 13.33 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, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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)
  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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