LytE

• Description: cell wall hydrolase (major autolysin),endopeptidase-type autolysin
  
  

Gene name	lytE
Synonyms	papQ, cwlF
Essential	no
Product	cell wall hydrolase (major autolysin),endopeptidase-type autolysin
Function	major autolysin, cell separation, cell lysis
MW, pI	37 kDa, 10.713
Gene length, protein length	1029 bp, 343 aa
Immediate neighbours	phoA, citR
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

This gene is a member of the following regulons

SigH regulon, SigI regulon, Spo0A regulon, WalR regulon

The gene

Basic information

• Locus tag: BSU09420

Phenotypes of a mutant

• • a cwlO lytE mutant is not viable PubMed
  • growth defect at high temperature PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: nlpC/p60 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • MreBH-LytE PubMed

• Localization: secreted (according to Swiss-Prot), binds the cell wall PubMed

Database entries

• Structure:

• UniProt: P54421

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: lytE PubMed

• Sigma factor: SigA PubMed, SigH PubMed, SigI PubMed

• Regulation:
  • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • induced at high temperature (SigI) PubMed
• Regulatory mechanism:
  • WalR: transcription activation PubMed
  • Spo0A: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

Chi-Ling Tseng, Jung-Tze Chen, Ju-Hui Lin, Wan-Zhen Huang, Gwo-Chyuan Shaw
Genetic evidence for involvement of the alternative sigma factor SigI in controlling expression of the cell wall hydrolase gene lytE and contribution of LytE to heat survival of Bacillus subtilis.
Arch Microbiol: 2011, 193(9);677-85
[PubMed:21541672] [WorldCat.org] [DOI] (I p)

Paola Bisicchia, David Noone, Efthimia Lioliou, Alistair Howell, Sarah Quigley, Thomas Jensen, Hanne Jarmer, Kevin M Devine
The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis.
Mol Microbiol: 2007, 65(1);180-200
[PubMed:17581128] [WorldCat.org] [DOI] (P p)

Rut Carballido-López, Alex Formstone, Ying Li, S Dusko Ehrlich, Philippe Noirot, Jeff Errington
Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE.
Dev Cell: 2006, 11(3);399-409
[PubMed:16950129] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Hiroki Yamamoto, Shin-ichirou Kurosawa, Junichi Sekiguchi
Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases.
J Bacteriol: 2003, 185(22);6666-77
[PubMed:14594841] [WorldCat.org] [DOI] (P p)

R Ohnishi, S Ishikawa, J Sekiguchi
Peptidoglycan hydrolase LytF plays a role in cell separation with CwlF during vegetative growth of Bacillus subtilis.
J Bacteriol: 1999, 181(10);3178-84
[PubMed:10322020] [WorldCat.org] [DOI] (P p)

S Ishikawa, Y Hara, R Ohnishi, J Sekiguchi
Regulation of a new cell wall hydrolase gene, cwlF, which affects cell separation in Bacillus subtilis.
J Bacteriol: 1998, 180(9);2549-55
[PubMed:9573210] [WorldCat.org] [DOI] (P p)

P Margot, M Wahlen, A Gholamhoseinian, P Piggot, D Karamata
The lytE gene of Bacillus subtilis 168 encodes a cell wall hydrolase.
J Bacteriol: 1998, 180(3);749-52
[PubMed:9457885] [WorldCat.org] [DOI] (P p)