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lytE [2017-05-24 13:20:23]
cell wall hydrolase (major autolysin) for cell elongation and separation, D,L-endopeptidase-type autolysin
Molecular weight
37.16 kDa
Function
major autolysin, cell elongation and separation
Product
cell wall hydrolase (major autolysin),endopeptidase-type autolysin
Genomic Context
Categories containing this gene/protein
Gene
Coordinates
1,018,998 → 1,020,002
Phenotypes of a mutant
a cwlO lytE mutant is not viable PubMedgrowth defect at high temperature PubMedinactivation of lytE strongly restores beta-lactam resistance in a sigM mutant by delaying cell lysis PubMeda lytE mutation is synthetically lethal with ftsE and ftsX mutation (due to a lack of autolysin activity) PubMeda lytE mutation increases the cell separation defect of a lytF mutant PubMedcells are thinner (reduced diameter) as compared to the wild type PubMed The protein
Catalyzed reaction/ biological activity
cleaves the peptide bond between D-Glu (position 2 in the peptioglycan peptide) and m-diamino pimelic acid (position 3) PubMed 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 Domains
Effectors of protein activity
Structure
4XCM (from Thermus thermophilus, 34% identity) Localization
binds the cell wall PubMedlocalizes to cell septa, poles and lateral sidewall of the cell (via the N-terminal domain) PubMedlocalization to lateral cell wall depends on the interaction with MreBH PubMed Expression and Regulation
Operons
Sigma factors
Regulatory mechanism
Regulation
expression is modulated in response to D,L-endopeptidase activity (increased two-fold to compensate for reduced activity in the absence of CwlO or FtsE-FtsX, decreased upon overexpression of LytE) (WalR) PubMedinduced at high temperature (SigI, WalR) PubMed view in new tabBiological materials
References
Reviews
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Original publications
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