Difference between revisions of "PurL"

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** subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
 
** subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 3495 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 10654 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 10:44, 17 April 2014

  • Description: phosphoribosylformylglycinamidine synthase

Gene name purL
Synonyms
Essential no
Product phosphoribosylformylglycinamidine synthase
Function purine biosynthesis
Gene expression levels in SubtiExpress: purL
Interactions involving this protein in SubtInteract: PurL
Metabolic function and regulation of this protein in SubtiPathways:
purL
MW, pI 80 kDa, 4.554
Gene length, protein length 2226 bp, 742 aa
Immediate neighbours purQ, purF
Sequences Protein DNA DNA_with_flanks
Genetic context
PurL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PurL expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, membrane proteins, most abundant proteins

This gene is a member of the following regulons

G-box, PurR regulon

The gene

Basic information

  • Locus tag: BSU06480

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate (according to Swiss-Prot)
  • Protein family: FGAMS family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 3D54 (from Thermotoga maritima, 39% identity, 58% similarity) PubMed
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • repressed in the presence of purine nucleotides (PurR) PubMed
    • repressed in the presence of adenine or adenosine(PurR) PubMed
    • repressed in the presence of guanine(G-box) PubMed
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 3495 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 10654 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Yanfei Xia, Shanshan Xie, Xin Ma, Huijun Wu, Xuan Wang, Xuewen Gao
The purL gene of Bacillus subtilis is associated with nematicidal activity.
FEMS Microbiol Lett: 2011, 322(2);99-107
[PubMed:21671997] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I 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)

Aaron A Hoskins, Ruchi Anand, Steven E Ealick, JoAnne Stubbe
The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation.
Biochemistry: 2004, 43(32);10314-27
[PubMed:15301530] [WorldCat.org] [DOI] (P p)

Lars Engholm Johansen, Per Nygaard, Catharina Lassen, Yvonne Agersø, Hans H Saxild
Definition of a second Bacillus subtilis pur regulon comprising the pur and xpt-pbuX operons plus pbuG, nupG (yxjA), and pbuE (ydhL).
J Bacteriol: 2003, 185(17);5200-9
[PubMed:12923093] [WorldCat.org] [DOI] (P p)

M Weng, P L Nagy, H Zalkin
Identification of the Bacillus subtilis pur operon repressor.
Proc Natl Acad Sci U S A: 1995, 92(16);7455-9
[PubMed:7638212] [WorldCat.org] [DOI] (P p)

D J Ebbole, H Zalkin
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis.
J Biol Chem: 1987, 262(17);8274-87
[PubMed:3036807] [WorldCat.org] (P p)