Difference between revisions of "SpeA"
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|style="background:#ABCDEF;" align="center"|'''Function''' || spermidine, polyamine biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || spermidine, polyamine biosynthesis | ||
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| + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU14630 speA] | ||
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/cys_meth_and_sulfate_assimilation.html Cys, Met & Sulfate assimilation]''' | ||
Revision as of 09:12, 7 August 2012
- 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: Cys, Met & Sulfate assimilation | |
| MW, pI | 53 kDa, 5.081 |
| Gene length, protein length | 1470 bp, 490 aa |
| Immediate neighbours | sr1, yktA |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
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
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)
