Difference between revisions of "SpoVD"
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+ | = Categories containing this gene/protein = | ||
+ | {{SubtiWiki category|[[cell wall synthesis]]}}, | ||
+ | {{SubtiWiki category|[[sporulation proteins]]}}, | ||
+ | {{SubtiWiki category|[[membrane proteins]]}} | ||
=The protein= | =The protein= | ||
Revision as of 20:12, 30 November 2010
- Description: mother-cell specific penicillin-binding protein (spore cortex)
Gene name | spoVD |
Synonyms | |
Essential | no |
Product | penicillin-binding protein (spore cortex) |
Function | spore morphogenesis |
MW, pI | 71 kDa, 8.85 |
Gene length, protein length | 1935 bp, 645 aa |
Immediate neighbours | pbpB, murE |
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: BSU15170
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
Categories containing this gene/protein
cell wall synthesis, sporulation proteins, membrane proteins
The protein
Basic information/ Evolution
- Protein family:
- Paralogous protein(s): PbpB
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: intramolecular disulfide bonds between two Cys residues are reduced by StoA, this is rquired for activity of SpoVD PubMed
- Localization: intermembrane space that separates forespores from mother cells PubMed
Database entries
- Structure:
- UniProt: Q03524
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and 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
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