Difference between revisions of "Apt"

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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 510 bp, 170 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 510 bp, 170 aa  
 
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[relA]]'', ''[[yrvE]]''
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[relA]]'', ''[[recJ]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU27610 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU27610 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU27610 DNA_with_flanks]
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU27610 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU27610 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU27610 DNA_with_flanks]
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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =

Revision as of 08:48, 7 July 2015

Gene name apt
Synonyms
Essential no
Product adenine phosphoribosyltransferase
Function purine salvage and interconversion
Gene expression levels in SubtiExpress: apt
Metabolic function and regulation of this protein in SubtiPathways:
apt
MW, pI 18 kDa, 4.701
Gene length, protein length 510 bp, 170 aa
Immediate neighbours relA, recJ
Sequences Protein DNA DNA_with_flanks
Genetic context
Apt context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Apt expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, universally conserved proteins, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU27610

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate (according to Swiss-Prot)
  • Protein family: purine/pyrimidine phosphoribosyltransferase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylated on Arg-85 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2DY0 (from Escherichia coli k12, 56% identity, 66% similarity)
  • KEGG entry: [3]

Additional information

universally conserved protein

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1738 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1189 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1706 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

M Nickel, G Homuth, C Böhnisch, U Mäder, T Schweder
Cold induction of the Bacillus subtilis bkd operon is mediated by increased mRNA stability.
Mol Genet Genomics: 2004, 272(1);98-107
[PubMed:15241682] [WorldCat.org] [DOI] (P p)

H H Saxild, P Nygaard
Genetic and physiological characterization of Bacillus subtilis mutants resistant to purine analogs.
J Bacteriol: 1987, 169(7);2977-83
[PubMed:3110131] [WorldCat.org] [DOI] (P p)