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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1748 [new locus tag: SACOL_RS08945 ]
  • pan locus tag?: SAUPAN004348000
  • symbol: accD
  • pan gene symbol?: accD
  • synonym:
  • product: acetyl-CoA carboxylase subunit beta

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1748 [new locus tag: SACOL_RS08945 ]
  • symbol: accD
  • product: acetyl-CoA carboxylase subunit beta
  • replicon: chromosome
  • strand: -
  • coordinates: 1785886..1786743
  • length: 858
  • 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
    ATGTTTAAAGATTTTTTTAATCGAACAAAGAAAAAGAAATATCTTACAGTACAAGACTCT
    AAAAATAATGATGTGCCTGCAGGTATTATGACTAAGTGTCCAAAGTGTAAGAAAATTATG
    TACACAAAAGAATTAGCTGAAAATTTAAATGTGTGCTTTAATTGTGATCATCATATTGCT
    TTAACTGCGTATAAACGTATAGAAGCAATTTCTGATGAAGGATCATTTACAGAATTCGAT
    AAGGGAATGACCTCTGCGAATCCATTAGATTTTCCAAGTTATTTAGAAAAAATTGAAAAG
    GACCAACAAAAGACAGGTCTTAAAGAAGCAGTTGTGACTGGTACAGCACAACTAGATGGT
    ATGAAATTTGGCGTTGCTGTCATGGATTCACGTTTTAGAATGGGAAGTATGGGATCGGTT
    ATCGGTGAAAAGATATGTCGCATCATTGATTACTGCACTGAGAACCGTTTACCATTTATT
    CTTTTCTCTGCAAGTGGTGGTGCACGTATGCAAGAAGGTATTATTTCCTTGATGCAAATG
    GGTAAAACCAGTGTATCTTTAAAACGTCATTCTGACGCTGGACTATTATATATATCATAT
    TTAACACATCCAACTACTGGTGGTGTATCTGCAAGTTTTGCATCAGTTGGTGATATAAAT
    TTAAGTGAGCCAAAAGCGTTGATAGGTTTTGCAGGTCGTCGAGTTATTGAACAGACAATA
    AACGAAAAATTGCCAGATGATTTCCAAACTGCAGAATTTTTATTAGAGCATGGACAATTG
    GATAAAGTTGTACATCGTAATGATATGCGTCAAACATTGTCTGAAATTCTAAAAATCCAT
    CAAGAGGTGACTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    858

⊟Protein[edit | edit source]

Protein Data Bank: 2F9I
Protein Data Bank: 5KDR

⊟General[edit | edit source]

  • locus tag: SACOL1748 [new locus tag: SACOL_RS08945 ]
  • symbol: AccD
  • description: acetyl-CoA carboxylase subunit beta
  • length: 285
  • theoretical pI: 8.35802
  • theoretical MW: 31871.6
  • GRAVY: -0.302105

⊟Function[edit | edit source]

  • reaction:
    EC 6.4.1.2?  ExPASy
    Acetyl-CoA carboxylase ATP + acetyl-CoA + HCO3(-) = ADP + phosphate + malonyl-CoA
  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis acetyl-CoA carboxylase, carboxyl transferase, beta subunit (TIGR00515; EC 6.4.1.2; HMM-score: 415.1)
    and 4 more
    Metabolism Transport and binding proteins Cations and iron carrying compounds methylmalonyl-CoA decarboxylase alpha subunit (TIGR01117; EC 4.1.1.41; HMM-score: 52.4)
    Metabolism Energy metabolism Fermentation methylmalonyl-CoA decarboxylase alpha subunit (TIGR01117; EC 4.1.1.41; HMM-score: 52.4)
    Metabolism Energy metabolism ATP-proton motive force interconversion methylmalonyl-CoA decarboxylase alpha subunit (TIGR01117; EC 4.1.1.41; HMM-score: 52.4)
    biotin-independent malonate decarboxylase, beta subunit (TIGR03133; EC 4.1.1.88; HMM-score: 46.5)
  • TheSEED  :
    • Acetyl-coenzyme A carboxyl transferase beta chain (EC 6.4.1.2)
    Fatty Acids, Lipids, and Isoprenoids Fatty acids Fatty Acid Biosynthesis FASII  Acetyl-coenzyme A carboxyl transferase beta chain (EC 6.4.1.2)
    and 1 more
    Virulence, Disease and Defense Bacteriocins, ribosomally synthesized antibacterial peptides Colicin V and Bacteriocin Production Cluster  Acetyl-coenzyme A carboxyl transferase beta chain (EC 6.4.1.2)
  • PFAM:
    ClpP_crotonase (CL0127) Carboxyl_trans; Carboxyl transferase domain (PF01039; HMM-score: 66.9)
    and 2 more
    AB_hydrolase (CL0028) FSH1; Serine hydrolase (FSH1) (PF03959; HMM-score: 12)
    Zn_Beta_Ribbon (CL0167) RNA_POL_M_15KD; RNA polymerases M/15 Kd subunit (PF02150; HMM-score: 9.6)

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

  • domains:
  • modifications:
  • cofactors: Zn2+
  • 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): 0.054236
    • TAT(Tat/SPI): 0.001063
    • LIPO(Sec/SPII): 0.003453
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MFKDFFNRTKKKKYLTVQDSKNNDVPAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIALTAYKRIEAISDEGSFTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDGMKFGVAVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLMQMGKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTINEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEVTK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 228 [4]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 25.74 h [5]

⊟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. ↑ 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]

Patrick Bilder, Sandra Lightle, Graeme Bainbridge, Jeffrey Ohren, Barry Finzel, Fang Sun, Susan Holley, Loola Al-Kassim, Cindy Spessard, Michael Melnick, Marcia Newcomer, Grover L Waldrop
The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.
Biochemistry: 2006, 45(6);1712-22
[PubMed:16460018] [WorldCat.org] [DOI] (P p)

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