Difference between revisions of "Ggt"
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<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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| + | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ggt_2004677_2006440_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:ggt_expression.png|500px]] | ||
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Revision as of 10:39, 19 April 2012
- Description: gamma-glutamyltransferase
| Gene name | ggt |
| Synonyms | pac |
| Essential | no |
| Product | gamma-glutamyltransferase |
| Function | degradation of poly-glutamate capsules |
| MW, pI | 64 kDa, 5.453 |
| Gene length, protein length | 1761 bp, 587 aa |
| Immediate neighbours | yoeD, yofA |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
capsule biosynthesis and degradation
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU18410
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
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:
- Localization:
- extracellular (signal peptide) PubMed
Database entries
- Structure: 2V36
- UniProt: P54422
- KEGG entry: [2]
- E.C. number: 2.3.2.2
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
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)
