Difference between revisions of "YvmC"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU35070&redirect=T BSU35070]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU35070&redirect=T BSU35070]
  
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3S7T 3S7T] (from ''B. licheniformis'', 70% identity, 86% similarity) {{PubMed|21325056}}
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3S7T 3S7T] (from ''B. licheniformis'', 70% identity, 86% similarity) {{PubMed|21325056}}

Revision as of 14:54, 2 April 2014

  • Description: cyclodipeptide synthase

Gene name yvmC
Synonyms
Essential no
Product cyclodipeptide synthase
Function biosynthesis of the extracellular iron chelate pulcherrimin
Gene expression levels in SubtiExpress: yvmC
MW, pI 28 kDa, 6.612
Gene length, protein length 744 bp, 248 aa
Immediate neighbours cypX, yvmB
Sequences Protein DNA DNA_with_flanks
Genetic context
YvmC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YvmC expression.png













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Categories containing this gene/protein

acquisition of iron, iron metabolism

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

  • Locus tag: BSU35070

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • synthesis of the cyclic dipeptide cyclo-L-leucyl-L-leucyl with the corresponding charged tRNAs as substrates in an ATP-dependent manner PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3S7T (from B. licheniformis, 70% identity, 86% similarity) PubMed
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • 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

Luc Bonnefond, Taiga Arai, Yuriko Sakaguchi, Tsutomu Suzuki, Ryuichiro Ishitani, Osamu Nureki
Structural basis for nonribosomal peptide synthesis by an aminoacyl-tRNA synthetase paralog.
Proc Natl Acad Sci U S A: 2011, 108(10);3912-7
[PubMed:21325056] [WorldCat.org] [DOI] (I p)

Muriel Gondry, Ludovic Sauguet, Pascal Belin, Robert Thai, Rachel Amouroux, Carine Tellier, Karine Tuphile, Mickaël Jacquet, Sandrine Braud, Marie Courçon, Cédric Masson, Steven Dubois, Sylvie Lautru, Alain Lecoq, Shin-ichi Hashimoto, Roger Genet, Jean-Luc Pernodet
Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes.
Nat Chem Biol: 2009, 5(6);414-20
[PubMed:19430487] [WorldCat.org] [DOI] (I p)

S H Harrison
The surgical management of the arthritic hand.
Ann R Coll Surg Engl: 1979, 61(1);17-28
[PubMed:420491] [WorldCat.org] (P p)

additional paper