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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • 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 source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • 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 source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 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 source | edit]

General[edit source | edit]

  • 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 source | edit]

  • reaction:
  • TIGRFAM:
    MetabolismFatty acid and phospholipid metabolismBiosynthesisacetyl-CoA carboxylase, biotin carboxyl carrier protein (TIGR00531; HMM-score: 108.3)
    MetabolismCentral intermediary metabolismNitrogen metabolismurea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 35.1)
    MetabolismTransport and binding proteinsCations and iron carrying compoundsoxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 34)
    MetabolismEnergy metabolismOtheroxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 34)
    MetabolismEnergy metabolismPyruvate dehydrogenasedihydrolipoyllysine-residue acetyltransferase (TIGR01348; EC 2.3.1.12; HMM-score: 25.4)
    MetabolismEnergy metabolismGlycolysis/gluconeogenesispyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 25.2)
    MetabolismEnergy metabolismTCA cycledihydrolipoyllysine-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)
    MetabolismEnergy metabolismATP-proton motive force interconversionATP 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)
    MetabolismEnergy metabolismElectron transportelectron transport complex, RnfABCDGE type, C subunit (TIGR01945; HMM-score: 15.9)
    MetabolismEnergy metabolismAmino acids and aminesglycine cleavage system H protein (TIGR00527; HMM-score: 15.5)
    proline reductase-associated electron transfer protein PrdC (TIGR04481; HMM-score: 14.2)
    MetabolismTransport and binding proteinsUnknown substrateefflux transporter, RND family, MFP subunit (TIGR01730; HMM-score: 12.6)
    MetabolismEnergy metabolismPyruvate dehydrogenasepyruvate dehydrogenase complex dihydrolipoamide acetyltransferase (TIGR01349; EC 2.3.1.12; HMM-score: 11.1)
  • TheSEED:  
    CarbohydratesCentral carbohydrate metabolismPyruvate metabolism I: anaplerotic reactions, PEP Biotin carboxyl carrier protein 
    Allophanate hydrolase 2 and Biotin carboxylase cluster Biotin carboxyl carrier protein 
  • PFAM:
    Hybrid (CL0105) Biotin_lipoyl; Biotin-requiring enzyme (PF00364; HMM-score: 67.3)
    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 definedATP-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 definedDUF1374; Protein of unknown function (DUF1374) (PF07118; HMM-score: 11.9)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:

Localization[edit source | edit]

  • 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
    • Ymax: 0.131
    • Ymax_pos: 62
    • Cmax: 0.114
    • Cmax_pos: 59
    • Smax: 0.209
    • Smax_pos: 51
    • Smean: 0.12
    • D: 0.127
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MNIEKIEQIIKLVKENDVKKFKYKNFEDEIEIDFTDLNHLAAHSNQSNQSMNNNDLTASKANDNSDVSTNDYHDIKSPMIGTFFLQDSKELTEPIVNVGDKVNKGDIIGYVEAMKVLNEVTTDVAGEITEIVADHGTNVEYDQVLVRIK

Experimental data[edit source | edit]

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

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: 13.33 h [6]

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  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 source | edit]