YmdB
- Description: putative phosphatase/ phosphodiesterase
Gene name | ymdB |
Synonyms | |
Essential | no |
Product | putative phosphatase/ phosphodiesterase |
Function | unknown function |
MW, pI | 29,1 kDa, 6.50 |
Gene length, protein length | 792 bp, 264 amino acids |
Immediate neighbours | rny, spoVS |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag: BSU16970
Phenotypes of a mutant
strong overexpression of Hag
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, negative effector of the expression of hag and other members of the SigD regulon
- Protein family:
- Paralogous protein(s): similar to unknown proteins
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: O31775
- KEGG entry: [2]
- E.C. number:
Additional information
has a negative effect on hag expression
Expression and regulation
- Regulation: constitutive
- Regulatory mechanism:
- Additional information: there is a terminator between rny and ymdB, most transcripts terminate there
Biological materials
- Mutant: GP583 (spc), available in Stülke lab
- Expression vector:
- 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
Jason Zemansky, Benjamin C Kline, Joshua J Woodward, Jess H Leber, Hélène Marquis, Daniel A Portnoy
Development of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype.
J Bacteriol: 2009, 191(12);3950-64
[PubMed:19376879]
[WorldCat.org]
[DOI]
(I p)
Dong Hae Shin, Michael Proudfoot, Hyo Jin Lim, In-Kyu Choi, Hisao Yokota, Alexander F Yakunin, Rosalind Kim, Sung-Hou Kim
Structural and enzymatic characterization of DR1281: A calcineurin-like phosphoesterase from Deinococcus radiodurans.
Proteins: 2008, 70(3);1000-9
[PubMed:17847097]
[WorldCat.org]
[DOI]
(I p)