Difference between revisions of "Sat"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[cysP]]'', ''[[cysC]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[cysP]]'', ''[[cysC]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15590 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15590 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15590 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15590 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15590 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15590 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:sat_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:sat_context.gif]]

Revision as of 10:11, 14 May 2013

  • 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:
Cys, Met & Sulfate assimilation
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
Sat context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Sat expression.png




























Categories containing this gene/protein

sulfur metabolism

This gene is a member of the following regulons

CymR regulon, S-box

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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed by casamino acids PubMed
    • repressed in the presence of cysteine (CymR)
    • induced by methionine starvation (S-box) PubMed
  • Regulatory mechanism:
    • S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
    • CymR: transcription repression
  • Additional information:

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)

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)