Difference between revisions of "AccB"

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(Biological materials)
(Biological materials)
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** GP1477 (chromosomal ''accB''-Strep fusion, ''aphA''3), purification from ''B. subtilis'', for [[SPINE]], available in [[Jörg Stülke]]'s lab'''
 
** GP1477 (chromosomal ''accB''-Strep fusion, ''aphA''3), purification from ''B. subtilis'', for [[SPINE]], available in [[Jörg Stülke]]'s lab'''
 
** pGP2649: IPTG inducible expression, purification in ''E. coli'' with N-terminal His-tag, in [[pWH844]], available in [[Jörg Stülke]]'s lab
 
** pGP2649: IPTG inducible expression, purification in ''E. coli'' with N-terminal His-tag, in [[pWH844]], available in [[Jörg Stülke]]'s lab
 +
** pGP2650: IPTG inducible expression, purification in ''E. coli'' with N-terminal Strep-tag, in [[pGP172]], available in [[Jörg Stülke]]'s lab
 
          
 
          
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''

Revision as of 12:25, 1 April 2015

  • Description: acetyl-CoA carboxylase (biotin carboxyl carrier subunit)

Gene name accB
Synonyms fabE, yqhW
Essential yes PubMed
Product acetyl-CoA carboxylase (biotin carboxyl carrier subunit)
Function production of malonyl-CoA, the substrate for fatty acid biosynthesis
Gene expression levels in SubtiExpress: accB
Interactions involving this protein in SubtInteract: AccB
Metabolic function and regulation of this protein in SubtiPathways:
accB
MW, pI 17 kDa, 4.394
Gene length, protein length 477 bp, 159 aa
Immediate neighbours accC, spoIIIAH
Sequences Protein DNA DNA_with_flanks
Genetic context
AccB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AccB expression.png















Categories containing this gene/protein

biosynthesis of lipids, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU24350

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 1BDO (the protein from E. coli) PubMed
  • KEGG entry: [3]

Additional information

AccB binds to StrepTactin, and may be co-purified when purifying Strep-tagged proteins by SPINE.

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3355 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 889 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 28 PubMed

Biological materials

  • Mutant:
  • Expression vector:
    • GP1477 (chromosomal accB-Strep fusion, aphA3), purification from B. subtilis, for SPINE, available in Jörg Stülke's lab
    • pGP2649: IPTG inducible expression, purification in E. coli with N-terminal His-tag, in pWH844, available in Jörg Stülke's lab
    • pGP2650: IPTG inducible expression, purification in E. coli with N-terminal Strep-tag, in pGP172, 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
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews


Original Publications

F K Athappilly, W A Hendrickson
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.
Structure: 1995, 3(12);1407-19
[PubMed:8747466] [WorldCat.org] [DOI] (P p)

P Marini, S J Li, D Gardiol, J E Cronan, D de Mendoza
The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis.
J Bacteriol: 1995, 177(23);7003-6
[PubMed:7592499] [WorldCat.org] [DOI] (P p)