Difference between revisions of "YmdB"
(→Database entries) |
|||
Line 91: | Line 91: | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId= | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=4B2O 4B2O] |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31775 O31775] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O31775 O31775] |
Revision as of 19:00, 31 July 2013
- Description: phosphodiesterase, controls bistable gene expression
Gene name | ymdB |
Synonyms | |
Essential | no |
Product | phosphodiesterase |
Function | control of bistable gene expression |
Gene expression levels in SubtiExpress: ymdB | |
MW, pI | 29,1 kDa, 6.50 |
Gene length, protein length | 792 bp, 264 amino acids |
Immediate neighbours | rny, spoVS |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU16970
Phenotypes of a mutant
- strong overexpression of hag PubMed
- defective in biofilm formation PubMed
- the phenotypes of the ymdB mutant can be suppressed by overexpression of slrR PubMed
- inactivation of ymdB restores beta-lactam resistance in a sigM mutant PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: phosphatase activity toward phosphoenolpyruvate and phosphodiesterase activity toward 2',3'-cAMP (the Deinococcus ortholog) PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 4B2O
- UniProt: O31775
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation: constitutive
- Regulatory mechanism:
- Additional information: there is a terminator between rny and ymdB, most transcripts terminate there PubMed
Biological materials
- Mutant:
- Expression vector:
- for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP1041, available in Stülke lab
- for expression/ purification from B. subtilis with C-terminal Strep-tag, for SPINE, in pGP382: pGP1919, available in Stülke lab
- for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP1040, available in Stülke lab
- for expression/ purification from E. coli with N-terminal Strep-tag, in pGP172: pGP1917, available in Stülke lab
- GP970 (ymdB-Strep (cat)), purification from B. subtilis, for SPINE, available in Stülke lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
Yun Luo, John D Helmann
Analysis of the role of Bacillus subtilis σ(M) in β-lactam resistance reveals an essential role for c-di-AMP in peptidoglycan homeostasis.
Mol Microbiol: 2012, 83(3);623-39
[PubMed:22211522]
[WorldCat.org]
[DOI]
(I p)
Eric R Pozsgai, Kris M Blair, Daniel B Kearns
Modified mariner transposons for random inducible-expression insertions and transcriptional reporter fusion insertions in Bacillus subtilis.
Appl Environ Microbiol: 2012, 78(3);778-85
[PubMed:22113911]
[WorldCat.org]
[DOI]
(I p)
Christine Diethmaier, Nico Pietack, Katrin Gunka, Christoph Wrede, Martin Lehnik-Habrink, Christina Herzberg, Sebastian Hübner, Jörg Stülke
A novel factor controlling bistability in Bacillus subtilis: the YmdB protein affects flagellin expression and biofilm formation.
J Bacteriol: 2011, 193(21);5997-6007
[PubMed:21856853]
[WorldCat.org]
[DOI]
(I p)
Functional and structural analysis of orthologs in other organisms