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}} | + | * no [[biofilm formation]] {{PubMed|24529384,20876533}} |
=== Database entries === | === Database entries === | ||
Revision as of 18:03, 28 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
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Expression at a glance PubMed
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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)
