Difference between revisions of "StoA"
(→Extended information on the protein) |
|||
Line 79: | Line 79: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' forespore envelope {{PubMed|19919673}} | + | * '''[[Localization]]:''' |
+ | ** forespore envelope {{PubMed|19919673}} | ||
=== Database entries === | === Database entries === |
Revision as of 12:29, 10 August 2011
- Description: thiol-disulfide oxidoreductase, with thioredoxin-like domain, required for the synthesis of the endospore peptidoglycan cortex
Gene name | stoA |
Synonyms | spoIVH, ykvV |
Essential | no |
Product | thiol-disulfide oxidoreductase |
Function | spore cortex formation |
Interactions involving this protein in SubtInteract: StoA | |
MW, pI | 18 kDa, 5.297 |
Gene length, protein length | 495 bp, 165 aa |
Immediate neighbours | ykvU, zosA |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13840
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: reduction of intramolecular disulfide bonds in SpoVD PubMed
- Protein family: thioredoxin domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- forespore envelope PubMed
Database entries
- Structure: 3ERW
- UniProt: O31687
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Lars Hederstedt, University of Lund, Sweden Homepage
Your additional remarks
References
Reviews
Patrick Eichenberger
The red-ox status of a penicillin-binding protein is an on/off switch for spore peptidoglycan synthesis in Bacillus subtilis.
Mol Microbiol: 2010, 75(1);10-2
[PubMed:19919674]
[WorldCat.org]
[DOI]
(I p)
Original Publications