Difference between revisions of "Ggt"

From SubtiWiki
Jump to: navigation, search
(Extended information on the protein)
(References)
Line 127: Line 127:
 
=References=
 
=References=
 
'''Additional publications:''' {{PubMed|21513304}}
 
'''Additional publications:''' {{PubMed|21513304}}
<pubmed>15583164,12892879,,18957862,20088880</pubmed>
+
<pubmed>15583164,12892879, 21987357,18957862,20088880</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 07:25, 12 October 2011

  • 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
Ggt context.gif
This image was kindly provided by SubtiList



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:

Database entries

  • KEGG entry: [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

Additional publications: PubMed

Weiqiao Li, Bo Jiang, Wanmeng Mu, Ming Miao, Tao Zhang
Effects of pH and dissolved oxygen on the synthesis of γ-glutamyltranspeptidase from Bacillus subtilis SK 11.004.
J Sci Food Agric: 2012, 92(3);475-80
[PubMed:21987357] [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)