Difference between revisions of "UgtP"

From SubtiWiki
Jump to: navigation, search
Line 39: Line 39:
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
<br/><br/><br/><br/>
 
<br/><br/><br/><br/>
 
 
 
 
<br/><br/><br/><br/><br/><br/>
 
<br/><br/><br/><br/><br/><br/>
  
Line 78: Line 74:
 
=== Basic information/ Evolution ===
 
=== 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)  
+
* '''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|22931116}}
  
 
* '''Protein family:'''
 
* '''Protein family:'''
Line 95: Line 93:
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
 +
** oligomerization of [[UgtP]] is inhibited by UDP-Glc and by interaction with [[FtsZ]]  {{PubMed|22931116}}
  
 
* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
** [[EzrA]]-[[UgtP]] {{PubMed|17662947}}[[UgtP]]-[[UgtP]] {{PubMed|17662947}}
+
** [[EzrA]]-[[UgtP]] {{PubMed|17662947}}
 
+
** [[UgtP]]-[[UgtP]] {{PubMed|17662947}}, forms oligomers {{PubMed|22931116}}
* '''[[Localization]]:''' membrane-bound protein, self-assembles into tightly wound spirals ''in vitro'' {{PubMed|17662947}}
+
** [[UgtP]]-[[FtsZ]] (under nutrient rich conditions) {{PubMed|22931116}}
  
 +
* '''[[Localization]]:'''
 +
** membrane-bound protein, self-assembles into tightly wound spirals ''in vitro'' {{PubMed|17662947}}
 +
** 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|22931116}}
 +
** under nutrient poor conditions: forms punctate foci (oligomers), no interaction with [[FtsZ]]  {{PubMed|22931116}}
 
=== Database entries ===
 
=== Database entries ===
  
Line 151: Line 154:
  
 
==Original Publications==
 
==Original Publications==
 +
'''Additional publications:''' {{PubMed|22931116}}
 
<pubmed>9244290,18820022,17662947,9720862 22362028 </pubmed>
 
<pubmed>9244290,18820022,17662947,9720862 22362028 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:37, 31 August 2012

  • 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
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

References

Reviews


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)