Difference between revisions of "MprF"
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|style="background:#ABCDEF;" align="center"|'''Function''' || lysyl-phosphatidylglycerol lipid biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || lysyl-phosphatidylglycerol lipid biosynthesis | ||
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| + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU08425 mprF] | ||
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|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_synthesis.html Lipid synthesis]''' | |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_synthesis.html Lipid synthesis]''' | ||
Revision as of 16:04, 6 August 2012
| Gene name | mprF |
| Synonyms | yfiW, yfiX |
| Essential | no |
| Product | lysyl-phosphatidylglycerol synthase |
| Function | lysyl-phosphatidylglycerol lipid biosynthesis |
| Gene expression levels in SubtiExpress: mprF | |
| Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis | |
| MW, pI | 96 kDa, 9.498 |
| Gene length, protein length | 2568 bp, 856 aa |
| Immediate neighbours | yfiV, yfiY |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
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Contents
Categories containing this gene/protein
biosynthesis of lipids, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU08425
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
Additional information
Gene was re-assembled due to sequencing error in original sequence (it encompasses the genes annotated as yfiX and yfiW in SubtiList) PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane at the septum PubMed
Database entries
- Structure:
- UniProt: C0H3X7
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon: mprF (according to DBTBS)
- Sigma factor:
- 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
Hervé Roy, Michael Ibba
Broad range amino acid specificity of RNA-dependent lipid remodeling by multiple peptide resistance factors.
J Biol Chem: 2009, 284(43);29677-83
[PubMed:19734140]
[WorldCat.org]
[DOI]
(I p)
Anna-Barbara Hachmann, Esther R Angert, John D Helmann
Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin.
Antimicrob Agents Chemother: 2009, 53(4);1598-609
[PubMed:19164152]
[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)
Hervé Roy, Michael Ibba
RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors.
Proc Natl Acad Sci U S A: 2008, 105(12);4667-72
[PubMed:18305156]
[WorldCat.org]
[DOI]
(I p)
Ayako Nishibori, Jin Kusaka, Hiroshi Hara, Masato Umeda, Kouji Matsumoto
Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes.
J Bacteriol: 2005, 187(6);2163-74
[PubMed:15743965]
[WorldCat.org]
[DOI]
(P p)
Petra Staubitz, Andreas Peschel
MprF-mediated lysinylation of phospholipids in Bacillus subtilis--protection against bacteriocins in terrestrial habitats?
Microbiology (Reading): 2002, 148(Pt 11);3331-3332
[PubMed:12427923]
[WorldCat.org]
[DOI]
(P p)
