Difference between revisions of "SpeB"
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=Expression and regulation= | =Expression and regulation= | ||
+ | * '''Operon:''' ''[[speE]]-[[speB]]'' {{PubMed|9723923}} | ||
− | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|9723923}} | |
− | |||
− | * '''[[Sigma factor]]:''' [[SigA]] | ||
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
− | + | <pubmed> 9723923 </pubmed> | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 20:09, 3 February 2010
- Description: agmatinase
Gene name | speB |
Synonyms | ywhG |
Essential | no |
Product | agmatinase |
Function | spermidine, polyamine biosynthesis |
Metabolic function and regulation of this protein in SubtiPathways: Cys, Met & Sulfate assimilation | |
MW, pI | 32 kDa, 4.768 |
Gene length, protein length | 870 bp, 290 aa |
Immediate neighbours | ywhH, speE |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU37490
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Agmatine + H2O = putrescine + urea (according to Swiss-Prot)
- Protein family: Agmatinase subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: P70999
- KEGG entry: [3]
- E.C. number: 3.5.3.11
Additional information
Expression and regulation
- 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
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)