PbpX
- Description: penicillin-binding protein X
Gene name | pbpX |
Synonyms | |
Essential | no |
Product | penicillin-binding protein X |
Function | endopeptidase |
MW, pI | 43 kDa, 9.711 |
Gene length, protein length | 1173 bp, 391 aa |
Immediate neighbours | recA, rny |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
cell wall synthesis, cell envelope stress proteins (controlled by SigM, W, X, Y)
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU16950
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: extracellular (signal peptide) PubMed, localizes during sporulation to both asymmetric septa and the prespore Link to a summary
Database entries
- Structure:
- UniProt: O31773
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: pbpX PubMed
- 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
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
Min Cao, John D Helmann
The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.
J Bacteriol: 2004, 186(4);1136-46
[PubMed:14762009]
[WorldCat.org]
[DOI]
(P p)