Difference between revisions of "UgtP"
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==Original Publications== | ==Original Publications== | ||
'''Additional publications:''' {{PubMed|22931116}} | '''Additional publications:''' {{PubMed|22931116}} | ||
− | <pubmed>9244290,18820022,17662947,9720862 22362028 </pubmed> | + | <pubmed>9244290,18820022,17662947,9720862 22362028 15640167 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 11:00, 19 September 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
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:
- 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:
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
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
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)