LytE

• Description: cell wall hydrolase (major autolysin) for cell elongation and separation, D,L-endopeptidase-type autolysin
  
  

Gene name	lytE
Synonyms	papQ, cwlF
Essential	no
Product	cell wall hydrolase (major autolysin),endopeptidase-type autolysin
Function	major autolysin, cell elongation and separation
Gene expression levels in SubtiExpress: lytE
MW, pI	37 kDa, 10.713
Gene length, protein length	1029 bp, 343 aa
Immediate neighbours	phoA, citR
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell wall degradation/ turnover, cell wall synthesis

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
• inactivation of lytE strongly restores beta-lactam resistance in a sigM mutant by delaying cell lysis PubMed
• a lytE mutation is synthetically lethal with ftsE and ftsX mutation (due to a lack of autolysin activity) PubMed
• a lytE mutation increases the cell separation defect of a lytF mutant PubMed
• cells are thinner (reduced diameter) as compared to the wild type 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): the C-terminal D,L-endopeptidase domains of LytE, LytF, CwlS, and CwlO exhibit strong sequence similarity

Extended information on the protein

• Kinetic information:

• Domains:
  • contains three N-acetylglucosamine-polymer-binding LysM domains PubMed
  • C-terminal D,L-endopeptidase domain PubMed

• Modification:

• Cofactors:

• Effectors of protein activity:
  • activity requires functional MreB and MreBH PubMed

• Interactions:
  • MreBH-LytE along the cylindrical part of the cell wall PubMed
  • FtsZ-LytE at the division septum PubMed
  • PbpB-LytE at the division septum PubMed

• Localization:
  • binds the cell wall PubMed
  • localizes to cell septa, poles and lateral sidewall of the cell (via the N-terminal domain) PubMed
  • localization to lateral cell wall depends on the interaction with MreBH PubMed

Database entries

• Structure:

• UniProt: P54421

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: lytE PubMed

• Expression browser: lytE PubMed

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

• Regulation:
  • repressed under conditions that trigger sporulation (Spo0A) PubMed
  • induced at high temperature (SigI, WalR) PubMed

• Regulatory mechanism:
  • WalR: transcription activation PubMed
  • Spo0A: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:
  • 1A790 ( lytE::cat), PubMed, available at BGSC
  • 1A792 ( lytE::cat), PubMed, available at BGSC
  • 1A1024 ( lytE::spec), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Waldemar Vollmer
Bacterial growth does require peptidoglycan hydrolases.
Mol Microbiol: 2012, 86(5);1031-5
[PubMed:23066944] [WorldCat.org] [DOI] (I p)

Girbe Buist, Anton Steen, Jan Kok, Oscar P Kuipers
LysM, a widely distributed protein motif for binding to (peptido)glycans.
Mol Microbiol: 2008, 68(4);838-47
[PubMed:18430080] [WorldCat.org] [DOI] (I p)