Difference between revisions of "SpeA"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 15:49, 25 February 2014
- Description: arginine decarboxylase, required for biofilm formation
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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P21885
- KEGG entry: [2]
- E.C. number: 4.1.1.19
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)