Difference between revisions of "PlsX"
Line 1: | Line 1: | ||
− | * '''Description:''' acyl-acyl carrier protein (ACP):phosphate acyltransferase, catalyzes the synthesis of the intermediate fatty acyl-phosphate (acyl-PO4) <br/><br/> | + | * '''Description:''' acyl-acyl carrier protein (ACP):phosphate acyltransferase, catalyzes the synthesis of the intermediate fatty acyl-phosphate (acyl-PO4), coordinates membrane synthesis with [[cell division]] <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
Line 8: | Line 8: | ||
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ylpD '' | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ylpD '' | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Essential''' || yes | + | |style="background:#ABCDEF;" align="center"| '''Essential''' || yes {{PubMed|24224907,12682299}} |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''Product''' || acyl-acyl carrier protein (ACP):phosphate acyltransferase | |style="background:#ABCDEF;" align="center"| '''Product''' || acyl-acyl carrier protein (ACP):phosphate acyltransferase | ||
Line 39: | Line 39: | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
− | + | <br/><br/> | |
− | |||
− | |||
− | |||
− | |||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[cell division]]}}, | ||
{{SubtiWiki category|[[biosynthesis of lipids]]}}, | {{SubtiWiki category|[[biosynthesis of lipids]]}}, | ||
{{SubtiWiki category|[[essential genes]]}} | {{SubtiWiki category|[[essential genes]]}} | ||
Line 60: | Line 57: | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
− | ** essential | + | ** essential {{PubMed|24224907,12682299}} |
** depletion results in sporulation deficiency (via [[SpoIIR]]) {{PubMed|22111992}} | ** depletion results in sporulation deficiency (via [[SpoIIR]]) {{PubMed|22111992}} | ||
+ | ** a ts mutant forms an abberant Z-ring and has a [[cell division]] defect {{PubMed|24224907}} | ||
+ | |||
=== Database entries === | === Database entries === | ||
Line 86: | Line 85: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
− | ** [[PlsX]]-[[PlsY]] | + | ** [[PlsX]]-[[PlsY]] {{PubMed|19282621}} |
+ | ** [[PlsX]]-[[FtsA]] {{PubMed|24224907}} | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
+ | ** localizes to the cell division sites, colocalizes with the Z-ring {{PubMed|24224907}} | ||
=== Database entries === | === Database entries === | ||
Line 117: | Line 118: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=plsX_1662547_1663548_1 plsX] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=plsX_1662547_1663548_1 plsX] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigA]] {{PubMed|16932747}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|16932747}} |
* '''Regulation:''' | * '''Regulation:''' | ||
Line 149: | Line 150: | ||
=References= | =References= | ||
− | + | <pubmed>12737802, 19282621, 17645809, 17557823, 8759840 16932747 19850612 16091051 21383089 22111992 24224907</pubmed> | |
− | <pubmed>12737802, 19282621, 17645809, 17557823, 8759840 16932747 19850612 16091051 21383089</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:18, 12 January 2014
- Description: acyl-acyl carrier protein (ACP):phosphate acyltransferase, catalyzes the synthesis of the intermediate fatty acyl-phosphate (acyl-PO4), coordinates membrane synthesis with cell division
Gene name | plsX |
Synonyms | ylpD |
Essential | yes PubMed |
Product | acyl-acyl carrier protein (ACP):phosphate acyltransferase |
Function | biosynthesis of phospholipids |
Gene expression levels in SubtiExpress: plsX | |
Interactions involving this protein in SubtInteract: PlsX | |
Metabolic function and regulation of this protein in SubtiPathways: plsX | |
MW, pI | 35 kDa, 5.492 |
Gene length, protein length | 999 bp, 333 aa |
Immediate neighbours | fapR, fabD |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell division, biosynthesis of lipids, essential genes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15890
Phenotypes of a mutant
- essential PubMed
- depletion results in sporulation deficiency (via SpoIIR) PubMed
- a ts mutant forms an abberant Z-ring and has a cell division defect PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: catalyzes the synthesis of the intermediate fatty acyl-phosphate (acyl-PO4)
- Protein family: plsX family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization:
- localizes to the cell division sites, colocalizes with the Z-ring PubMed
Database entries
- Structure: 1VI1
- UniProt: P71018
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Matsumoto lab PubMed
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Hiraku Takada, Sanae Fukushima-Tanaka, Masato Morita, Yasuhiro Kasahara, Satoru Watanabe, Taku Chibazakura, Hiroshi Hara, Kouji Matsumoto, Hirofumi Yoshikawa
An essential enzyme for phospholipid synthesis associates with the Bacillus subtilis divisome.
Mol Microbiol: 2014, 91(2);242-55
[PubMed:24224907]
[WorldCat.org]
[DOI]
(I p)
Veronica Diez, Gustavo E Schujman, Frederico J Gueiros-Filho, Diego de Mendoza
Vectorial signalling mechanism required for cell-cell communication during sporulation in Bacillus subtilis.
Mol Microbiol: 2012, 83(2);261-74
[PubMed:22111992]
[WorldCat.org]
[DOI]
(I p)
Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089]
[WorldCat.org]
[DOI]
(I p)
Mariano A Martinez, Diego de Mendoza, Gustavo E Schujman
Transcriptional and functional characterization of the gene encoding acyl carrier protein in Bacillus subtilis.
Microbiology (Reading): 2010, 156(Pt 2);484-495
[PubMed:19850612]
[WorldCat.org]
[DOI]
(I p)
Yoshinori Hara, Masahide Seki, Satoshi Matsuoka, Hiroshi Hara, Atsushi Yamashita, Kouji Matsumoto
Involvement of PlsX and the acyl-phosphate dependent sn-glycerol-3-phosphate acyltransferase PlsY in the initial stage of glycerolipid synthesis in Bacillus subtilis.
Genes Genet Syst: 2008, 83(6);433-42
[PubMed:19282621]
[WorldCat.org]
[DOI]
(P p)
Mika Yoshimura, Taku Oshima, Naotake Ogasawara
Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli.
BMC Microbiol: 2007, 7;69
[PubMed:17645809]
[WorldCat.org]
[DOI]
(I e)
Luciana Paoletti, Ying-Jie Lu, Gustavo E Schujman, Diego de Mendoza, Charles O Rock
Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis.
J Bacteriol: 2007, 189(16);5816-24
[PubMed:17557823]
[WorldCat.org]
[DOI]
(P p)
Gustavo E Schujman, Marcelo Guerin, Alejandro Buschiazzo, Francis Schaeffer, Leticia I Llarrull, Georgina Reh, Alejandro J Vila, Pedro M Alzari, Diego de Mendoza
Structural basis of lipid biosynthesis regulation in Gram-positive bacteria.
EMBO J: 2006, 25(17);4074-83
[PubMed:16932747]
[WorldCat.org]
[DOI]
(P p)
Natalia Comella, Alan D Grossman
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis.
Mol Microbiol: 2005, 57(4);1159-74
[PubMed:16091051]
[WorldCat.org]
[DOI]
(P p)
Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis.
Dev Cell: 2003, 4(5);663-72
[PubMed:12737802]
[WorldCat.org]
[DOI]
(P p)
H R Morbidoni, D de Mendoza, J E Cronan
Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid biosynthesis genes.
J Bacteriol: 1996, 178(16);4794-800
[PubMed:8759840]
[WorldCat.org]
[DOI]
(P p)