Ggt

• Description: gamma-glutamyltransferase
  
  

Gene name	ggt
Synonyms	pac
Essential	no
Product	gamma-glutamyltransferase
Function	degradation of poly-glutamate capsules
Gene expression levels in SubtiExpress: ggt
MW, pI	64 kDa, 5.453
Gene length, protein length	1761 bp, 587 aa
Immediate neighbours	yoeD, yofA
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

capsule biosynthesis and degradation

This gene is a member of the following regulons

Efp-dependent proteins

The gene

Basic information

• Locus tag: BSU18410

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • extracellular (signal peptide) PubMed

Database entries

• Structure: 2V36

• UniProt: P54422

• KEGG entry: [2]

• E.C. number: 2.3.2.2

Expression and regulation

• Operon: ggt PubMed

• Expression browser: ggt PubMed

• Sigma factor:

• Regulation:
  • strongly induced in response to glucose starvation in M9 medium PubMed

• Regulatory mechanism:

• Additional information:
  • translation is likely to require Efp due to the presence of several consecutive proline residues PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

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)

Kei Wada, Machiko Irie, Hideyuki Suzuki, Keiichi Fukuyama
Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket.
FEBS J: 2010, 277(4);1000-9
[PubMed:20088880] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Keitarou Kimura, Lam-Son Phan Tran, Ikuo Uchida, Yoshifumi Itoh
Characterization of Bacillus subtilis gamma-glutamyltransferase and its involvement in the degradation of capsule poly-gamma-glutamate.
Microbiology (Reading): 2004, 150(Pt 12);4115-23
[PubMed:15583164] [WorldCat.org] [DOI] (P p)

Hiromichi Minami, Hideyuki Suzuki, Hidehiko Kumagai
A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity.
FEMS Microbiol Lett: 2003, 224(2);169-73
[PubMed:12892879] [WorldCat.org] [DOI] (P p)