Difference between revisions of "GlmM"
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+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[cell wall synthesis]]}}, | ||
+ | {{SubtiWiki category|[[biosynthesis of cell wall components]]}}, | ||
+ | {{SubtiWiki category|[[essential genes]]}}, | ||
+ | {{SubtiWiki category|[[phosphoproteins]]}} | ||
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+ | = This gene is a member of the following [[regulons]] = | ||
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=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 16:06, 8 December 2010
- Description: phosphoglucosamine mutase, required for cell wall synthesis
Gene name | glmM |
Synonyms | ybbT |
Essential | yes PubMed |
Product | phosphoglucosamine mutase, required for cell wall synthesis |
Function | cell wall synthesis |
MW, pI | 48 kDa, 4.677 |
Gene length, protein length | 1344 bp, 448 aa |
Immediate neighbours | ybbR, glmS |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
cell wall synthesis, biosynthesis of cell wall components, essential genes, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU01770
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate (according to Swiss-Prot)
- Protein family: phosphohexose mutase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 3I3W (from Francisella tularensis, 39% identity, 58% similarity)
- UniProt: O34824
- KEGG entry: [2]
- E.C. number: 5.4.2.10
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- pGP400: (expression in B. subtilis in pBQ200), available in Stülke lab
- pGP1401: (expression, purification in E. coli with N-terminal His-tag, in pWH844), available in Stülke lab
- pGP1402: (cloning vector for glmM (GlmM S100A) in E. coli, in pBlueskript KS), available in Stülke lab
- pGP1403: (expression of GlmM (S100A) in B. subtilis in pBQ200), available in Stülke lab
- pGP1405: (expression, purification of GlmM (S100A) in E. coli with N-terminal His-tag, in pWH844), available in Stülke lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Sebastian R Schmidl, Katrin Gronau, Nico Pietack, Michael Hecker, Dörte Becher, Jörg Stülke
The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases.
Mol Cell Proteomics: 2010, 9(6);1228-42
[PubMed:20097688]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
L Jolly, F Pompeo, J van Heijenoort, F Fassy, D Mengin-Lecreulx
Autophosphorylation of phosphoglucosamine mutase from Escherichia coli.
J Bacteriol: 2000, 182(5);1280-5
[PubMed:10671448]
[WorldCat.org]
[DOI]
(P p)
L Jolly, P Ferrari, D Blanot, J Van Heijenoort, F Fassy, D Mengin-Lecreulx
Reaction mechanism of phosphoglucosamine mutase from Escherichia coli.
Eur J Biochem: 1999, 262(1);202-10
[PubMed:10231382]
[WorldCat.org]
[DOI]
(P p)
D Mengin-Lecreulx, J van Heijenoort
Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli.
J Biol Chem: 1996, 271(1);32-9
[PubMed:8550580]
[WorldCat.org]
[DOI]
(P p)