Difference between revisions of "UgtP"

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(Original Publications)
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==Original Publications==
==Original Publications==
'''Additional publications:''' {{PubMed|22931116}}
'''Additional publications:''' {{PubMed|22931116}}
<pubmed>9244290,18820022,17662947,9720862 22362028 15640167 </pubmed>
<pubmed>9244290,18820022,17662947,9720862 22362028 15640167 22931116 </pubmed>
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 10:29, 30 October 2012

  • 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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
UgtP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
UgtP expression.png

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

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

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
  • 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:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks



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

Additional publications: PubMed

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)