NagZ

• 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 This image was kindly provided by SubtiList

Categories containing this gene/protein

cell wall degradation/ turnover

The gene

Basic information

• Locus tag: BSU01660

Phenotypes of a mutant

increased autolysis PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization:
  • secreted (with signal peptide), remains to some extent cell wall-associated PubMed

Database entries

• Structure: 3CQM PubMed

• UniProt: P40406

• 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:

• Expression browser: nagZ PubMed

• Sigma factor:

• Regulation:
  • expressed in late exponential and early stationary phase PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: available in Christoph Mayer's lab PubMed

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)