Difference between revisions of "SpeA"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
* no [[biofilm formation]] {{PubMed|20876533}}
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* no [[biofilm formation]] {{PubMed|24529384,20876533}}
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 18:03, 28 February 2014

Gene name speA
Synonyms cad
Essential no
Product arginine decarboxylase
Function spermidine, polyamine biosynthesis
Gene expression levels in SubtiExpress: speA
Metabolic function and regulation of this protein in SubtiPathways:
speA
MW, pI 53 kDa, 5.081
Gene length, protein length 1470 bp, 490 aa
Immediate neighbours sr1, yktA
Sequences Protein DNA DNA_with_flanks
Genetic context
SpeA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SpeA expression.png















Categories containing this gene/protein

miscellaneous metabolic pathways, biofilm formation

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU14630

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-arginine = agmatine + CO2 (according to Swiss-Prot)
  • Protein family: Orn/Lys/Arg decarboxylase class-I family (according to Swiss-Prot)
  • Paralogous protein(s): YaaO

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [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

Laura Hobley, Sok Ho Kim, Yukari Maezato, Susan Wyllie, Alan H Fairlamb, Nicola R Stanley-Wall, Anthony J Michael
Norspermidine is not a self-produced trigger for biofilm disassembly.
Cell: 2014, 156(4);844-54
[PubMed:24529384] [WorldCat.org] [DOI] (I p)

Matthew Burrell, Colin C Hanfrey, Ewan J Murray, Nicola R Stanley-Wall, Anthony J Michael
Evolution and multiplicity of arginine decarboxylases in polyamine biosynthesis and essential role in Bacillus subtilis biofilm formation.
J Biol Chem: 2010, 285(50);39224-38
[PubMed:20876533] [WorldCat.org] [DOI] (I p)

Xiao Yan Liu, Jian Lei, Xiang Liu, Xiao Dong Su, Lanfen Li
Preliminary X-ray crystallographic studies of Bacillus subtilis SpeA protein.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 3);282-4
[PubMed:19255484] [WorldCat.org] [DOI] (I p)

A Sekowska, P Bertin, A Danchin
Characterization of polyamine synthesis pathway in Bacillus subtilis 168.
Mol Microbiol: 1998, 29(3);851-8
[PubMed:9723923] [WorldCat.org] [DOI] (P p)