NagZ

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  • Description: N-acetylglucosaminidase

Gene name nagZ
Synonyms yzbA, ybbD
Essential no
Product N-acetylglucosaminidase
Function cell wall recycling
Metabolic function and regulation of this protein in SubtiPathways:
Murein recycling
MW, pI 70 kDa, 9.76
Gene length, protein length 1926 bp, 642 aa
Immediate neighbours ybbC, amiE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YbbD context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell wall degradation/ turnover

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU01660

Phenotypes of a mutant

increased autolysis PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: cleaves muropeptides derived from peptidoglycan, but not peptidoglycan itself PubMed
  • Protein family: glycosyl hydrolase 3 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • secreted (with signal peptide), remains to some extent cell wall-associated PubMed

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

The gene is mis-annotated in KEGG as an ortholog of beta-N-acetylhexosaminidase EC 3.2.1.52. It is marked in MetaCyc as “similar to beta-hexosaminidase”. No EC annotation is available in Swiss-ProtSwiss-Prot.supporting the annotation is available. PubMed

Expression and regulation

  • Operon:
  • Regulation:
    • expressed in late exponential and early stationary phase PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Additional references: PubMed

Silke Litzinger, Amanda Duckworth, Katja Nitzsche, Christian Risinger, Valentin Wittmann, Christoph Mayer
Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.
J Bacteriol: 2010, 192(12);3132-43
[PubMed:20400549] [WorldCat.org] [DOI] (I p)

Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040] [WorldCat.org] [DOI] (P p)

R C Berkeley, S J Brewer, J M Ortiz, J B Gillespie
An exo- -N-acetylglucosaminidase from Bacillus subtilis B; characterization.
Biochim Biophys Acta: 1973, 309(1);157-68
[PubMed:4196675] [WorldCat.org] [DOI] (P p)

J M Ortiz, J B Gillespie, R C Berkeley
An exo- -N-acetylglucosaminidase from Bacillus subtilis B; extraction and purification.
Biochim Biophys Acta: 1972, 289(1);174-86
[PubMed:4628806] [WorldCat.org] [DOI] (P p)