UgtP

• Description: UDP-glucose diacylglycerol glucosyltransferase, growth-rate dpendent inhibitor of cell division
  
  

Gene name	ugtP
Synonyms	ypfP
Essential	no
Product	UDP-glucose diacylglycerol glucosyltransferase
Function	synthesis of glycolipids and anchoring of lipoteichoic acid, inhibition of FtsZ assembly
Gene expression levels in SubtiExpress: ugtP
Interactions involving this protein in SubtInteract: UgtP
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis
MW, pI	43 kDa, 8.398
Gene length, protein length	1146 bp, 382 aa
Immediate neighbours	metA, cspD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell division, lipid metabolism/ other, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

• Locus tag: BSU21920

Phenotypes of a mutant

• • cells are bent and distended PubMed
  • increased expression of the SigM, SigV, and SigX regulons PubMed
  • altered localization of MreB (irregular clusters instead of helical dots) PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • UDP-glucose + 1,2-diacylglycerol = UDP + 1,2-diacyl-3-(O-beta-D-glucopyranosyl)-sn-glycerol (according to Swiss-Prot)
  • the interaction with FtsZ results in inhibition of cell division and an increase of cell size PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:
  • oligomerization of UgtP is inhibited by UDP-Glc and by interaction with FtsZ PubMed

• Interactions:
  • EzrA-UgtP PubMed
  • UgtP-UgtP PubMed, forms oligomers PubMed
  • UgtP-FtsZ (under nutrient rich conditions) PubMed

• Localization:
  • membrane-bound protein, self-assembles into tightly wound spirals in vitro PubMed
  • under nutrient rich conditions (increased concentration of UDP-Glc): throughout the cell, concentrated at the cell poles and/or the cytokinetic ring, interaction with FtsZ PubMed
  • under nutrient poor conditions: forms punctate foci (oligomers), no interaction with FtsZ PubMed

Database entries

• Structure:

• UniProt: P54166

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: ugtP PubMed

• Sigma factor: SigM PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

Additional publications: PubMed

Satoshi Matsuoka, Minako Chiba, Yu Tanimura, Michihiro Hashimoto, Hiroshi Hara, Kouji Matsumoto
Abnormal morphology of Bacillus subtilis ugtP mutant cells lacking glucolipids.
Genes Genet Syst: 2011, 86(5);295-304
[PubMed:22362028] [WorldCat.org] [DOI] (I p)

Letal I Salzberg, John D Helmann
Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition.
J Bacteriol: 2008, 190(23);7797-807
[PubMed:18820022] [WorldCat.org] [DOI] (I p)

Richard B Weart, Amy H Lee, An-Chun Chien, Daniel P Haeusser, Norbert S Hill, Petra Anne Levin
A metabolic sensor governing cell size in bacteria.
Cell: 2007, 130(2);335-47
[PubMed:17662947] [WorldCat.org] [DOI] (P p)

P Jorasch, F P Wolter, U Zähringer, E Heinz
A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products.
Mol Microbiol: 1998, 29(2);419-30
[PubMed:9720862] [WorldCat.org] [DOI] (P p)

K D Price, S Roels, R Losick
A Bacillus subtilis gene encoding a protein similar to nucleotide sugar transferases influences cell shape and viability.
J Bacteriol: 1997, 179(15);4959-61
[PubMed:9244290] [WorldCat.org] [DOI] (P p)