GlmM

• 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
Gene expression levels in SubtiExpress: glmM
Metabolic function and regulation of this protein in SubtiPathways: glmM
MW, pI	48 kDa, 4.677
Gene length, protein length	1344 bp, 448 aa
Immediate neighbours	cdaR, glmS
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes, phosphoproteins

The gene

Basic information

• Locus tag: BSU01770

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU01770

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Modification: phosphorylation on Ser-100 PubMed, this is an autophosphorylation PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU01770

• Structure: 3PDK (from B. anthracis) PubMed

• UniProt: O34824

• KEGG entry: [2]

• E.C. number: 5.4.2.10

Expression and regulation

• Operon: cdaA-cdaR-glmM-glmS PubMed

• Expression browser: glmM PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • A ncRNA is predicted between glmM and glmS PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1353 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2093 PubMed

Biological materials

• Mutant:

• Expression vector:
  • pGP400: (expression in B. subtilis in pBQ200), available in Jörg Stülke's lab
  • pGP1401: (expression, purification in E. coli with N-terminal His-tag, in pWH844), available in Jörg Stülke's lab
  • pGP1402: (cloning vector for glmM (GlmM S100A) in E. coli, in pBlueskript KS), available in Jörg Stülke's lab
  • pGP1403: (expression of GlmM (S100A) in B. subtilis in pBQ200), available in Jörg Stülke's lab
  • pGP1405: (expression, purification of GlmM (S100A) in E. coli with N-terminal His-tag, in pWH844), available in Jörg Stülke's lab

• lacZ fusion:
  • GP1340 (cat) based on pAC6, available in Jörg Stülke's lab

• GFP fusion:
  • GP1382 glmM-gfp ermC (based on pGP1080), available in Jörg Stülke's lab

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• FLAG-tag construct:
  • GP1380 lacA::cdaR-Strep aphA3 glmM-3xFLAG ermC (based on pGP1460 and pGP1087), available in Jörg Stülke's lab

• Strep-tag construct:
  • GP1388 lacA::glmM-Strep aphA3 cdaA-3xFLAG ermC (based on pGP1460 and pGP1087), available in Jörg Stülke's lab

• Antibody: available in Jörg Stülke's lab

References

Jan Gundlach, Felix M P Mehne, Christina Herzberg, Jan Kampf, Oliver Valerius, Volkhard Kaever, Jörg Stülke
An Essential Poison: Synthesis and Degradation of Cyclic Di-AMP in Bacillus subtilis.
J Bacteriol: 2015, 197(20);3265-74
[PubMed:26240071] [WorldCat.org] [DOI] (I p)

Felix M P Mehne, Katrin Gunka, Hinnerk Eilers, Christina Herzberg, Volkhard Kaever, Jörg Stülke
Cyclic di-AMP homeostasis in bacillus subtilis: both lack and high level accumulation of the nucleotide are detrimental for cell growth.
J Biol Chem: 2013, 288(3);2004-17
[PubMed:23192352] [WorldCat.org] [DOI] (I p)

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)

Ritcha Mehra-Chaudhary, Jacob Mick, Lesa J Beamer
Crystal structure of Bacillus anthracis phosphoglucosamine mutase, an enzyme in the peptidoglycan biosynthetic pathway.
J Bacteriol: 2011, 193(16);4081-7
[PubMed:21685296] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

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)