Difference between revisions of "YaaO"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === |
Revision as of 20:56, 19 December 2011
- Description: similar to arginine decarboxylase, but without enzymatic activity
Gene name | yaaO |
Synonyms | |
Essential | no |
Product | putative arginine decarboxylase |
Function | unknown |
Metabolic function and regulation of this protein in SubtiPathways: Nucleotides (regulation) | |
MW, pI | 52 kDa, 5.713 |
Gene length, protein length | 1440 bp, 480 aa |
Immediate neighbours | yaaN, tmk |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
poorly characterized/ putative enzymes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU00270
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: Orn/Lys/Arg decarboxylase class-I family (according to Swiss-Prot)
- Paralogous protein(s): SpeA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P37536
- KEGG entry: [2]
- E.C. number:
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
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)