Difference between revisions of "Sat"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
| − | {{SubtiWiki category|[[sulfur metabolism]]}} | + | {{SubtiWiki category|[[sulfur metabolism]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sat_1632208_1633356_1 sat] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sat_1632208_1633356_1 sat] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' [[SigA]] {{PubMed|11004190}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|11004190}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
| − | <pubmed>16267287,11004190,12107147, 18039762 </pubmed> | + | <pubmed>16267287,11004190,12107147, 18039762 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:16, 5 March 2014
- Description: sulfate adenylyltransferase
| Gene name | sat |
| Synonyms | ylnB |
| Essential | no |
| Product | sulfate adenylyltransferase |
| Function | sulfate activation |
| Gene expression levels in SubtiExpress: sat | |
| Metabolic function and regulation of this protein in SubtiPathways: sat | |
| MW, pI | 42 kDa, 5.646 |
| Gene length, protein length | 1146 bp, 382 aa |
| Immediate neighbours | cysP, cysC |
| 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
sulfur metabolism, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15590
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + sulfate = diphosphate + adenylyl sulfate (according to Swiss-Prot)
- Protein family: sulfate adenylyltransferase family (according to Swiss-Prot)
- Paralogous protein(s): YitA
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O34764
- KEGG entry: [3]
- E.C. number: 2.7.7.4
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
- CymR: transcription repression
- Additional information:
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Isabelle Martin-Verstraete, Institute Pasteur, Paris, France
Your additional remarks
References
Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762]
[WorldCat.org]
[DOI]
(I p)
Daniela Albanesi, Maria Cecilia Mansilla, Gustavo E Schujman, Diego de Mendoza
Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation.
J Bacteriol: 2005, 187(22);7631-8
[PubMed:16267287]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)
M C Mansilla, D Albanesi, D de Mendoza
Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in L-cysteine biosynthesis in Bacillus subtilis.
J Bacteriol: 2000, 182(20);5885-92
[PubMed:11004190]
[WorldCat.org]
[DOI]
(P p)
