UgtP

• Description: UDP-glucose diacylglycerol glucosyltransferase, growth-rate dependent 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
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 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:

• Cofactors:

• 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:
  • GP1369 (ugtP::spc), available in Jörg Stülke's lab

• Expression vector:
  • pGP2571, for expression in B. subtilis (based on pBQ200, available in Jörg Stülke's lab
  • pGP2600, for expression/ purification from E. coli with N-terminal His-tag, in pWH844, available in Jörg Stülke's lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

An-Chun Chien, Norbert S Hill, Petra Anne Levin
Cell size control in bacteria.
Curr Biol: 2012, 22(9);R340-9
[PubMed:22575476] [WorldCat.org] [DOI] (I p)

David W Adams, Jeff Errington
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
Nat Rev Microbiol: 2009, 7(9);642-53
[PubMed:19680248] [WorldCat.org] [DOI] (I p)

Daisuke Shiomi, William Margolin
A sweet sensor for size-conscious bacteria.
Cell: 2007, 130(2);216-8
[PubMed:17662935] [WorldCat.org] [DOI] (P p)

Original Publications

Norbert S Hill, Paul J Buske, Yue Shi, Petra Anne Levin
A moonlighting enzyme links Escherichia coli cell size with central metabolism.
PLoS Genet: 2013, 9(7);e1003663
[PubMed:23935518] [WorldCat.org] [DOI] (I p)

An-Chun Chien, Shannon Kian Gharabiklou Zareh, Yan Mei Wang, Petra Anne Levin
Changes in the oligomerization potential of the division inhibitor UgtP co-ordinate Bacillus subtilis cell size with nutrient availability.
Mol Microbiol: 2012, 86(3);594-610
[PubMed:22931116] [WorldCat.org] [DOI] (I p)

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)

Vladimir Lazarevic, Blazenka Soldo, Noël Médico, Harold Pooley, Sierd Bron, Dimitri Karamata
Bacillus subtilis alpha-phosphoglucomutase is required for normal cell morphology and biofilm formation.
Appl Environ Microbiol: 2005, 71(1);39-45
[PubMed:15640167] [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)