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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1572 [new locus tag: SACOL_RS08005 ]
  • pan locus tag?: SAUPAN004082000
  • symbol: accB
  • pan gene symbol?: accB
  • 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: SACOL1572 [new locus tag: SACOL_RS08005 ]
  • symbol: accB
  • product: acetyl-CoA carboxylase, biotin carboxyl carrier protein
  • replicon: chromosome
  • strand: -
  • coordinates: 1607302..1607766
  • length: 465
  • 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
    ATGAACTTTAAAGAAATCAAAGAATTAATTGAAATTCTGGATAAATCAACTTTAACGGAA
    ATCAATATTGAAGATACTAAAGGCAAAGTGACGCTTAAGAAAGAAAAAGAAACTGAGATT
    ATCACGCCACAAATCTCACAAATGCCAGTTGAAGCTGCGGCAATGCCTATGCCTCAAGCA
    CAATCAACTGATAGCAATAAAACTGAAGCTCCAAAGCCAACTTCAGATAATCACAAAACA
    ATTAATGCACCTATGGTAGGTACATTTTACAAATCGCCATCTCCAGACGAAGAAGCATAT
    GTGCAAGTTGGGGACACTGTTTCAAATGAAACAACAGTGTGTATTTTAGAGGCAATGAAA
    CTATTTAATGAAATTCAAGCAGAAATTTCAGGTGAAATTGTTGAAATCTTAGTAGAAGAC
    GGACAAATGGTAGAGTATGGCCAACCGTTATTTAAGGTGAAATAA
    60
    120
    180
    240
    300
    360
    420
    465

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1572 [new locus tag: SACOL_RS08005 ]
  • symbol: AccB
  • description: acetyl-CoA carboxylase, biotin carboxyl carrier protein
  • length: 154
  • theoretical pI: 4.2253
  • theoretical MW: 17121.4
  • GRAVY: -0.423377

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, biotin carboxyl carrier protein (TIGR00531; HMM-score: 170.6)
    and 16 more
    Metabolism Central intermediary metabolism Nitrogen metabolism urea carboxylase (TIGR02712; EC 6.3.4.6; HMM-score: 39.4)
    Metabolism Transport and binding proteins Cations and iron carrying compounds oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 38.5)
    Metabolism Energy metabolism Other oxaloacetate decarboxylase alpha subunit (TIGR01108; EC 4.1.1.3; HMM-score: 38.5)
    Metabolism Energy metabolism Pyruvate dehydrogenase dihydrolipoyllysine-residue acetyltransferase (TIGR01348; EC 2.3.1.12; HMM-score: 31.1)
    Metabolism Energy metabolism Glycolysis/gluconeogenesis pyruvate carboxylase (TIGR01235; EC 6.4.1.1; HMM-score: 30.1)
    Metabolism Energy metabolism TCA cycle dihydrolipoyllysine-residue succinyltransferase, E2 component of oxoglutarate dehydrogenase (succinyl-transferring) complex (TIGR01347; EC 2.3.1.61; HMM-score: 22.2)
    Metabolism Transport and binding proteins Unknown substrate efflux transporter, RND family, MFP subunit (TIGR01730; HMM-score: 22)
    Cellular processes Cellular processes Biosynthesis of natural products NHLM bacteriocin system secretion protein (TIGR03794; HMM-score: 16.3)
    Metabolism Transport and binding proteins Amino acids, peptides and amines NHLM bacteriocin system secretion protein (TIGR03794; HMM-score: 16.3)
    Metabolism Transport and binding proteins Other efflux pump membrane protein (TIGR00998; HMM-score: 15)
    Genetic information processing Protein fate Protein and peptide secretion and trafficking type I secretion membrane fusion protein, HlyD family (TIGR01843; HMM-score: 14.9)
    Cell structure Cell envelope Other uncharacterized lipoprotein (TIGR02722; HMM-score: 14.7)
    glycine cleavage protein H-like protein (TIGR03077; HMM-score: 13.7)
    Metabolism Energy metabolism Amino acids and amines glycine cleavage system H protein (TIGR00527; HMM-score: 13.3)
    Genetic information processing DNA metabolism DNA replication, recombination, and repair UV excision repair protein Rad23 (TIGR00601; HMM-score: 13)
    2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase (TIGR02927; EC 2.3.1.61; HMM-score: 10.2)
  • TheSEED  :
    • Biotin carboxyl carrier protein of acetyl-CoA carboxylase
    Fatty Acids, Lipids, and Isoprenoids Fatty acids Fatty Acid Biosynthesis FASII  Biotin carboxyl carrier protein of acetyl-CoA carboxylase
    and 1 more
    Miscellaneous Miscellaneous - no subcategory EC 6.3.4.- Ligases that form carbon-nitrogen bonds  Biotin carboxyl carrier protein of acetyl-CoA carboxylase
  • PFAM:
    Hybrid (CL0105) Biotin_lipoyl; Biotin-requiring enzyme (PF00364; HMM-score: 80.6)
    and 6 more
    Biotin_lipoyl_2; Biotin-lipoyl like (PF13533; HMM-score: 30.1)
    GCV_H; Glycine cleavage H-protein (PF01597; HMM-score: 20.7)
    HlyD_3; HlyD family secretion protein (PF13437; HMM-score: 19.1)
    HlyD_D23; Barrel-sandwich domain of CusB or HlyD membrane-fusion (PF16576; HMM-score: 14.8)
    RnfC_N; RnfC Barrel sandwich hybrid domain (PF13375; HMM-score: 12.2)
    no clan defined Dicty_REP; Dictyostelium (Slime Mold) REP protein (PF05086; HMM-score: 11.1)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • 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): 0.063844
    • TAT(Tat/SPI): 0.002354
    • LIPO(Sec/SPII): 0.001119
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MNFKEIKELIEILDKSTLTEINIEDTKGKVTLKKEKETEIITPQISQMPVEAAAMPMPQAQSTDSNKTEAPKPTSDNHKTINAPMVGTFYKSPSPDEEAYVQVGDTVSNETTVCILEAMKLFNEIQAEISGEIVEILVEDGQMVEYGQPLFKVK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1418 [5]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: FapR* (repression) regulon
    FapR*(TF)important in Fatty acid biosynthesis; RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 18.43 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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