Difference between revisions of "Ggt"
(→Database entries) |
(→References) |
||
Line 118: | Line 118: | ||
=References= | =References= | ||
− | <pubmed>15583164,12892879,,18957862, </pubmed> | + | <pubmed>15583164,12892879,,18957862,20088880 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:19, 22 January 2010
- 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
|
Contents
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:
- Interactions:
- 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:
- 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
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)