Difference between revisions of "YmdB"
(→Biological materials) |
|||
Line 1: | Line 1: | ||
− | * '''Description:''' | + | * '''Description:''' putative phosphatase/ phosphodiesterase <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
Line 10: | Line 10: | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || putative phosphatase/ phosphodiesterase |
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown function | |style="background:#ABCDEF;" align="center"|'''Function''' || unknown function | ||
Line 53: | Line 53: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' negative effector of the expression of ''[[hag]]'' and other members of the [[SigD]] regulon | + | * '''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:''' | * '''Protein family:''' | ||
Line 77: | Line 77: | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=1T70 1T70] {{PubMed|17847097}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O31775 O31775] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O31775 O31775] | ||
Line 127: | Line 127: | ||
=References= | =References= | ||
− | <pubmed> 19376879 </pubmed> | + | <pubmed> 19376879 17847097 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:02, 30 April 2010
- 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
|
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)