AccA

• Description: acetyl-CoA carboxylase (alpha subunit)
  
  

Gene name	accA
Synonyms
Essential	yes PubMed
Product	acetyl-CoA carboxylase (alpha subunit))
Function	production of malonyl-CoA, the substrate for fatty acid biosynthesis
Gene expression levels in SubtiExpress: accA
Interactions involving this protein in SubtInteract: AccA
Metabolic function and regulation of this protein in SubtiPathways: accA
MW, pI	36 kDa, 6.087
Gene length, protein length	975 bp, 325 aa
Immediate neighbours	pfkA, accD
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of lipids, essential genes

This gene is a member of the following regulons

Spo0A regulon

The gene

Basic information

• Locus tag: BSU29200

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU29200

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA (according to Swiss-Prot)

• Protein family: accA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • (AccA-AccD)-AccB-AccC (acetyl-CoA carboxylase complex)

• Localization: cytoplasm (according to Swiss-Prot), Membrane-proximal (Spotty) PubMed

Database entries

• BsubCyc: BSU29200

• Structure: 2F9I (from Staphylococcus aureus; equivalent to AccD-AccA, 64% identity) PubMed

• UniProt: O34847

• KEGG entry: [3]

• E.C. number: 6.4.1.2

Expression and regulation

• Operon: accD-accA PubMed

• Expression browser: accA PubMed

• Sigma factor:

• Regulation:
  • expressed under conditions that trigger sporulation (Spo0A) PubMed

• Regulatory mechanism:
  • Spo0A: transcription activation PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1047 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 795 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 910 PubMed

Biological materials

• Mutant:

• Expression vector:
  • purification from B. subtilis with an C-terminal Strep-tag, for SPINE, (in pGP382): pGP1723, available in Jörg Stülke's lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• FLAG-tag construct:
  • GP1487 (spc, based on pGP1331), available in Jörg Stülke's lab

• Antibody:

References

Original Publications

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

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)

Christoph Freiberg, Nina A Brunner, Guido Schiffer, Thomas Lampe, Jens Pohlmann, Michael Brands, Martin Raabe, Dieter Häbich, Karl Ziegelbauer
Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity.
J Biol Chem: 2004, 279(25);26066-73
[PubMed:15066985] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Hailong Zhang, Zhiru Yang, Yang Shen, Liang Tong
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
Science: 2003, 299(5615);2064-7
[PubMed:12663926] [WorldCat.org] [DOI] (I p)