Difference between revisions of "GcaD"

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(Biological materials)
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU00500&redirect=T BSU00500]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gcaD-prs-ctc.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gcaD-prs-ctc.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU00500&redirect=T BSU00500]
  
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=1hm9 1HM9] (from ''Streptococcus pneumoniae'', 49% identity) {{PubMed|11118459}}
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=1hm9 1HM9] (from ''Streptococcus pneumoniae'', 49% identity) {{PubMed|11118459}}

Revision as of 12:46, 2 April 2014

  • Description: bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase

Gene name gcaD
Synonyms tms, tms26
Essential yes PubMed
Product bifunctional N-acetylglucosamine-1-phosphate

uridyltransferase/glucosamine-1-phosphate acetyltransferase

Function cell wall metabolism
Gene expression levels in SubtiExpress: gcaD
Metabolic function and regulation of this protein in SubtiPathways:
gcaD
MW, pI 49 kDa, 5.65
Gene length, protein length 1368 bp, 456 aa
Immediate neighbours spoVG, prs
Sequences Protein DNA DNA_with_flanks
Genetic context
GcaD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GcaD expression.png




























Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU00500

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 1HM9 (from Streptococcus pneumoniae, 49% identity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
    • pGP2596: (IPTG inducible expression, purification in E. coli with N-terminal His-tag, in pWH844), available in Jörg Stülke's lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Ludek Sojka, Tomás Kouba, Ivan Barvík, Hana Sanderová, Zdenka Maderová, Jirí Jonák, Libor Krásny
Rapid changes in gene expression: DNA determinants of promoter regulation by the concentration of the transcription initiating NTP in Bacillus subtilis.
Nucleic Acids Res: 2011, 39(11);4598-611
[PubMed:21303765] [WorldCat.org] [DOI] (I p)

G Sulzenbacher, L Gal, C Peneff, F Fassy, Y Bourne
Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
J Biol Chem: 2001, 276(15);11844-51
[PubMed:11118459] [WorldCat.org] [DOI] (P p)

I Hilden, B N Krath, B Hove-Jensen
Tricistronic operon expression of the genes gcaD (tms), which encodes N-acetylglucosamine 1-phosphate uridyltransferase, prs, which encodes phosphoribosyl diphosphate synthetase, and ctc in vegetative cells of Bacillus subtilis.
J Bacteriol: 1995, 177(24);7280-4
[PubMed:8522540] [WorldCat.org] [DOI] (P p)

B Hove-Jensen
Identification of tms-26 as an allele of the gcaD gene, which encodes N-acetylglucosamine 1-phosphate uridyltransferase in Bacillus subtilis.
J Bacteriol: 1992, 174(21);6852-6
[PubMed:1328164] [WorldCat.org] [DOI] (P p)