Difference between revisions of "UgtP"
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|style="background:#ABCDEF;" align="center"|'''Function''' || synthesis of glycolipids and anchoring of lipoteichoic <br/>acid, inhibition of [[FtsZ]] assembly | |style="background:#ABCDEF;" align="center"|'''Function''' || synthesis of glycolipids and anchoring of lipoteichoic <br/>acid, inhibition of [[FtsZ]] assembly | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_syn.html Lipid synthesis]''' | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 43 kDa, 8.398 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 43 kDa, 8.398 |
Revision as of 13:41, 16 February 2010
- 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 |
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
|
Contents
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)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot), membrane-bound protein, self-assembles into tightly wound spirals in vitro 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
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)
Original Publications