Difference between revisions of "PlsY"
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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of phospholipids | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of phospholipids | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU18070 plsY] | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=PlsY PlsY] | ||
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=plsY plsY]''' | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 20 kDa, 10.408 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 20 kDa, 10.408 | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yneR]]'', ''[[yneT]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yneR]]'', ''[[yneT]]'' | ||
|- | |- | ||
− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU18070 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU18070 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU18070 DNA_with_flanks] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:yneS_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:yneS_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
+ | |- | ||
+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=plsY_1931920_1932501_-1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:plsY_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU18070]] | ||
|- | |- | ||
|} | |} | ||
__TOC__ | __TOC__ | ||
+ | <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/> | ||
+ | |||
+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[biosynthesis of lipids]]}}, | ||
+ | {{SubtiWiki category|[[essential genes]]}}, | ||
+ | {{SubtiWiki category|[[membrane proteins]]}} | ||
+ | |||
+ | = This gene is a member of the following [[regulons]] = | ||
− | |||
=The gene= | =The gene= | ||
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=== Basic information === | === Basic information === | ||
− | * ''' | + | * '''Locus tag:''' BSU18070 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
Line 42: | Line 64: | ||
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU18070&redirect=T BSU18070] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
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=== Additional information=== | === Additional information=== | ||
+ | |||
+ | |||
Line 54: | Line 79: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' Acyl-phosphate + sn-glycerol 3-phosphate = acyl-sn-glycerol 3-phosphate + phosphate (according to UniProt) |
* '''Protein family:''' UPF0078 family (according to Swiss-Prot) | * '''Protein family:''' UPF0078 family (according to Swiss-Prot) | ||
Line 72: | Line 97: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
+ | ** [[PlsY]]-[[PlsX]] {{PubMed|19282621}} | ||
− | * '''Localization:''' cell membrane | + | * '''[[Localization]]:''' cell membrane {{PubMed|19820159}} |
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU18070&redirect=T BSU18070] | ||
* '''Structure:''' | * '''Structure:''' | ||
− | * ''' | + | * '''UniProt:''' [http://www.uniprot.org/uniprot/Q45064 Q45064] |
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU18070] |
* '''E.C. number:''' | * '''E.C. number:''' | ||
Line 92: | Line 119: | ||
* '''Operon:''' | * '''Operon:''' | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=plsY_1931920_1932501_-1 plsY] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' | ||
* '''Regulation:''' | * '''Regulation:''' | ||
Line 98: | Line 127: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = | ||
Line 110: | Line 139: | ||
* '''GFP fusion:''' | * '''GFP fusion:''' | ||
− | * '''two-hybrid system:''' | + | * '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in Matsumoto lab {{PubMed|19282621}} |
* '''Antibody:''' | * '''Antibody:''' | ||
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=References= | =References= | ||
+ | ==Reviews== | ||
+ | <pubmed> 15952903 17919287</pubmed> | ||
+ | ==Original Publications== | ||
+ | <pubmed> 19282621, 17005971, 17557823, 19820159, </pubmed> | ||
− | + | [[Category:Protein-coding genes]] | |
− | |||
− |
Latest revision as of 13:51, 2 April 2014
- Description: acylphosphate:glycerol-phosphate acyltransferase
Gene name | plsY |
Synonyms | yneS |
Essential | yes PubMed |
Product | acylphosphate:glycerol-phosphate acyltransferase |
Function | biosynthesis of phospholipids |
Gene expression levels in SubtiExpress: plsY | |
Interactions involving this protein in SubtInteract: PlsY | |
Metabolic function and regulation of this protein in SubtiPathways: plsY | |
MW, pI | 20 kDa, 10.408 |
Gene length, protein length | 579 bp, 193 aa |
Immediate neighbours | yneR, yneT |
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
biosynthesis of lipids, essential genes, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU18070
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU18070
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Acyl-phosphate + sn-glycerol 3-phosphate = acyl-sn-glycerol 3-phosphate + phosphate (according to UniProt)
- Protein family: UPF0078 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane PubMed
Database entries
- BsubCyc: BSU18070
- Structure:
- UniProt: Q45064
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- 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
Reviews
Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287]
[WorldCat.org]
[DOI]
(P p)
Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903]
[WorldCat.org]
[DOI]
(P p)
Original Publications
Jessica C Zweers, Thomas Wiegert, Jan Maarten van Dijl
Stress-responsive systems set specific limits to the overproduction of membrane proteins in Bacillus subtilis.
Appl Environ Microbiol: 2009, 75(23);7356-64
[PubMed:19820159]
[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)
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)
Alison Hunt, Joy P Rawlins, Helena B Thomaides, Jeff Errington
Functional analysis of 11 putative essential genes in Bacillus subtilis.
Microbiology (Reading): 2006, 152(Pt 10);2895-2907
[PubMed:17005971]
[WorldCat.org]
[DOI]
(P p)