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
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Contents
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:
- Interactions:
- Localization: secreted (with signal peptide), remains to some extent cell wall-associated PubMed
Database entries
- 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:
- 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:
Labs working on this gene/protein
Your additional remarks
References
Additional references: PubMed