GcaD

• Description: UDP-N-acetylglucosamine pyrophosphorylase
  
  

Gene name	gcaD
Synonyms	tms, tms26
Essential	yes PubMed
Product	UDP-N-acetylglucosamine pyrophosphorylase
Function	cell wall metabolism
Metabolic function and regulation of this protein in SubtiPathways: Nucleotides (regulation)
MW, pI	49 kDa, 5.65
Gene length, protein length	1368 bp, 456 aa
Immediate neighbours	spoVG, prs
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU00500

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P14192

• KEGG entry: [3]

• E.C. number: 2.7.7.23

Expression and regulation

• Operon: gcaD-prs-ctc PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)