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AccB DNA-binding transcriptional repressor

Synonyms: AccB
Summary:
The accB gene encodes the biotin carboxyl carrier protein (BCCP), a component of acetyl CoA carboxylase [3]. AccB is active as a dimer []. The kinetics of the biotinylation reaction have been determined, and the N terminus does not appear to have any role in the modification [4]. Biotinylation causes a large structural change in the C-terminal region of the protein []. Biotinylation results in loss of conformational flexibility of the biotin interaction region []; a "thumb" domain comprising amino acids 94-101 fastens the biotin moiety to the surface of the protein [] and this interaction results in increased protein stability [].
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Transcription factor      
TF conformation(s):
Name Conformation Type TF-Effector Interaction Type Apo/Holo Conformation Evidence (Confirmed, Strong, Weak) References
AccB Functional   nd [1], [2]
Connectivity class: Local Regulator
Gene name: accB
  Genome position: 3405436-3405906
  Length: 471 bp / 156 aa
Operon name: accBC
TU(s) encoding the TF:
Transcription unit        Promoter
accBC
accBp
accBC
accBp2


Regulon       
Regulated gene(s) accB, accC
Multifun term(s) of regulated gene(s) MultiFun Term (List of genes associated to the multifun term)
biotin carboxyl carrier protein (1)
fatty acids and phosphatidic acid (1)
Regulated operon(s) accBC
First gene in the operon(s) accB
Simple and complex regulons AccB
Simple and complex regulatory phrases Regulatory phrase (List of promoters regulated by the phrase)
[AccB,-](1)


Transcription factor regulation    


Transcription factor binding sites (TFBSs) arrangements
      

  Functional conformation Function Promoter Sigma factor Central Rel-Pos Distance to first Gene Genes Sequence LeftPos RightPos Evidence (Confirmed, Strong, Weak) References
  AccB repressor accBp Sigma70 nd nd accB, accC nd nd [GEA], [IMP] [2]


Evolutionary conservation of regulatory elements    
     Note: Evolutionary conservation of regulatory interactions and promoters is limited to gammaproteobacteria.
Promoter-target gene evolutionary conservation


Evidence    

 [GEA] Gene expression analysis

 [IMP] Inferred from mutant phenotype



Reference(s)    

 [1] Blanchard CZ., Chapman-Smith A., Wallace JC., Waldrop GL., 1999, The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin., J Biol Chem 274(45):31767-9

 [2] James ES., Cronan JE., 2004, Expression of two Escherichia coli acetyl-CoA carboxylase subunits is autoregulated., J Biol Chem 279(4):2520-7

 [3] Alix JH., 1989, A rapid procedure for cloning genes from lambda libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome., DNA 8(10):779-89

 [4] Nenortas E, Beckett D, 1996, Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase., J Biol Chem, 1996 Mar 29

 [5] Chapman-Smith A, Mulhern TD, Whelan F, Cronan JE Jr, Wallace JC, 2001, The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity., Protein Sci, 2001 Dec

 [6] Weaver LH, Kwon K, Beckett D, Matthews BW, 2001, Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor., Protein Sci, 2001 Dec

 [7] Reche P., Li YL., Fuller C., Eichhorn K., Perham RN., 1998, Selectivity of post-translational modification in biotinylated proteins: the carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli., Biochem J 329 ( Pt 3):589-96

 [8] Li SJ., Cronan JE., 1992, The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase., J Biol Chem 267(2):855-63

 [9] Cronan JE., 2002, Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a linker from the lipoylated subunit of pyruvate dehydrogenase., J Biol Chem 277(25):22520-7

 [10] Karow M., Fayet O., Georgopoulos C., 1992, The lethal phenotype caused by null mutations in the Escherichia coli htrB gene is suppressed by mutations in the accBC operon, encoding two subunits of acetyl coenzyme A carboxylase., J Bacteriol 174(22):7407-18

 [11] Chapman-Smith A, Cronan JE Jr, 1999, The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity., Trends Biochem Sci, 1999 Sep



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