GabR

• Description: transcription activator of gabT-gabD, repressor of gabR (MocR/ GabR family)
  
  

Gene name	gabR
Synonyms	ycnF
Essential	no
Product	transcription regulator
Function	regulation of gamma-amino butyric acid utilization
Gene expression levels in SubtiExpress: gabR
MW, pI	54 kDa, 6.709
Gene length, protein length	1437 bp, 479 aa
Immediate neighbours	yczG, gabT
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

utilization of amino acids, transcription factors and their control

This gene is a member of the following regulons

GabR regulon

The GabR regulon:

• gabT-gabD, gabR

The gene

Basic information

• Locus tag: BSU03890

Database entries

• BsubCyc: BSU03890

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • transcription activation of the gabT-gabD operon in the presence of GABA and PLP, transcription repression of gabR PubMed

• Protein family: MocR/ GabR family PubMed

• Paralogous protein(s): none, but there are 7 members of the MocR/ GabR family in B. subtilis

Extended information on the protein

• Kinetic information:

• Domains:
  • N-terminal DNA-binding helix-turn-helix motif (corresponding to domains of the GntR family) PubMed
  • C-terminal domain is homologous to PLP-binding large domain of aminotransferases PubMed

• Modification:

• Cofactors: gamma-aminobutyric acid, PLP PubMed

• Effectors of protein activity:
  • activation of gabT-gabD expression is triggered by gamma-amino butyrate and pyridoxalphosphate PubMed

• Interactions:
  • forms head-to-tail domain-swapped dimers PubMed

• Localization:

Database entries

• BsubCyc: BSU03890

• Structure:
  • 4MGR (the apo-protein) PubMed
  • 4N0B (the complex with PLP) PubMed

• UniProt: P94426

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: gabR (according to DBTBS)

• Expression browser: gabR PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:
  • GabR: negative autoregulation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

References

Keita Okuda, Shiro Kato, Tomokazu Ito, Shunsuke Shiraki, Yumiko Kawase, Masaru Goto, Susumu Kawashima, Hisashi Hemmi, Harumi Fukada, Tohru Yoshimura
Role of the aminotransferase domain in Bacillus subtilis GabR, a pyridoxal 5'-phosphate-dependent transcriptional regulator.
Mol Microbiol: 2015, 95(2);245-57
[PubMed:25388514] [WorldCat.org] [DOI] (I p)

Raji Edayathumangalam, Rui Wu, Roman Garcia, Yuguang Wang, Wei Wang, Cheryl A Kreinbring, Alicia Bach, Jingling Liao, Todd A Stone, Thomas C Terwilliger, Quyen Q Hoang, Boris R Belitsky, Gregory A Petsko, Dagmar Ringe, Dali Liu
Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabT.
Proc Natl Acad Sci U S A: 2013, 110(44);17820-5
[PubMed:24127574] [WorldCat.org] [DOI] (I p)

E Bramucci, T Milano, S Pascarella
Genomic distribution and heterogeneity of MocR-like transcriptional factors containing a domain belonging to the superfamily of the pyridoxal-5'-phosphate dependent enzymes of fold type I.
Biochem Biophys Res Commun: 2011, 415(1);88-93
[PubMed:22020104] [WorldCat.org] [DOI] (I p)

Boris R Belitsky
Bacillus subtilis GabR, a protein with DNA-binding and aminotransferase domains, is a PLP-dependent transcriptional regulator.
J Mol Biol: 2004, 340(4);655-64
[PubMed:15223311] [WorldCat.org] [DOI] (P p)

Boris R Belitsky, Abraham L Sonenshein
GabR, a member of a novel protein family, regulates the utilization of gamma-aminobutyrate in Bacillus subtilis.
Mol Microbiol: 2002, 45(2);569-83
[PubMed:12123465] [WorldCat.org] [DOI] (P p)

Sébastien Rigali, Adeline Derouaux, Fabrizio Giannotta, Jean Dusart
Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies.
J Biol Chem: 2002, 277(15);12507-15
[PubMed:11756427] [WorldCat.org] [DOI] (P p)