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AccB DNA-binding transcriptional repressor

Synonyms: AccB
The accB gene encodes the biotin carboxyl carrier protein (BCCP), a component of acetyl CoA carboxylase [2]. AccB is active as a dimer [3]. 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 [5]. Biotinylation results in loss of conformational flexibility of the biotin interaction region [6]; a "thumb" domain comprising amino acids 94-101 fastens the biotin moiety to the surface of the protein [7] and this interaction results in increased protein stability [8].
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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 nd
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

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)

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 accBp1 Sigma70 nd nd accB, accC nd nd [GEA], [IMP], [BPP] [1]

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


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

 [2] 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

 [3] Cronan JE, 2001, The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure id essential and that the domain functions as a dimer., J Biol Chem, 276(40):37355 10.1074/jbc.M106353200

 [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, 271(13):7559 10.1074/jbc.271.13.7559

 [5] Chapman-Smith A, Forbes BE, Wallace JC, Cronan JE, 1997, Covalent modification of an exposed surface turn alters the global conformation of the biotin carrier domain of Escherichia coli acetyl-CoA carboxylase., J Biol Chem, 272(41):26017 10.1074/jbc.272.41.26017

 [6] Yao X, Soden C, Summers MF, Beckett D, 1999, Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase., Protein Sci, 8(2):307 10.1110/ps.8.2.307

 [7] Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE, Perham RN, 1999, Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy., Biochemistry, 38(16):5045 10.1021/bi982466o

 [8] Solbiati J, Chapman-Smith A, Cronan JE, 2002, Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding "thumb" structure., J Biol Chem, 277(24):21604 10.1074/jbc.M201928200

 [9] Chapman-Smith A, Mulhern TD, Whelan F, Cronan JE, Wallace JC, 2001, The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity., Protein Sci, 10(12):2608 10.1110/ps.22401

 [10] 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, 10(12):2618 10.1110/ps.32701

 [11] Athappilly FK, Hendrickson WA, 1995, Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing., Structure, 3(12):1407 10.1016/s0969-2126(01)00277-5

 [12] Yao X, Wei D, Soden C, Summers MF, Beckett D, 1997, Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase., Biochemistry, 36(49):15089 10.1021/bi971485f

 [13] Toh H, Kondo H, Tanabe T, 1993, Molecular evolution of biotin-dependent carboxylases., Eur J Biochem, 215(3):687 10.1111/j.1432-1033.1993.tb18080.x

 [14] 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

 [15] 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

 [16] Chapman-Smith A, Morris TW, Wallace JC, Cronan JE, 1999, Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase., J Biol Chem, 274(3):1449 10.1074/jbc.274.3.1449

 [17] 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 10.1074/jbc.M201249200

 [18] 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

 [19] Han L, Yang K, Kulowski K, Wendt-Pienkowski E, Hutchinson CR, Vining LC, 2000, An acyl-coenzyme A carboxylase encoding gene associated with jadomycin biosynthesis in Streptomyces venezuelae ISP5230., Microbiology (Reading), 146 ( Pt 4)(None):903 10.1099/00221287-146-4-903

 [20] Best EA, Knauf VC, 1993, Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase., J Bacteriol, 175(21):6881 10.1128/jb.175.21.6881-6889.1993

 [21] Weiss E, Chatellier J, Orfanoudakis G, 1994, In vivo biotinylated recombinant antibodies: construction, characterization, and application of a bifunctional Fab-BCCP fusion protein produced in Escherichia coli., Protein Expr Purif, 5(5):509 10.1006/prep.1994.1070

 [22] Sibler AP, Kempf E, Glacet A, Orfanoudakis G, Bourel D, Weiss E, 1999, In vivo biotinylated recombinant antibodies: high efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments., J Immunol Methods, 224(1-2):129 10.1016/s0022-1759(99)00016-2

 [23] Cronan JE, Waldrop GL, 2002, Multi-subunit acetyl-CoA carboxylases., Prog Lipid Res, 41(5):407 10.1016/s0163-7827(02)00007-3

 [24] Chapman-Smith A, Cronan JE, 1999, The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity., Trends Biochem Sci, 24(9):359 10.1016/s0968-0004(99)01438-3