lytE

lytE
168

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

Locus
BSU_09420
Molecular weight
37.16 kDa
Isoelectric point
10.71
Protein length
334 aaSequenceBlast
Gene length
1005 bpSequenceBlast
Function
major autolysin, cell elongation and separation
Product
cell wall hydrolase (major autolysin),endopeptidase-type autolysin
Essential
no
E.C.
3.4.-.-
Synonyms
lytE, papQ, cwlF
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG1388 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,018,998  1,020,002
Phenotypes of a mutant
cell chain formation PubMed
a ''cwlO lytE'' mutant is not viable PubMed
a ugtP lytE double mutant has a severe cell shape defect, thi can be suppressed by mutations resulting in reduced expression or activity of PbpA PubMed
growth defect at high temperature PubMed
inactivation of ''lytE strongly restores beta-lactam resistance in a sigM'' mutant by delaying cell lysis PubMed
synthetically lethal with  ''ftsE and ftsX'' mutation (due to a lack of autolysin activity) PubMed
synthetically lethal with sweC and sweD, this can be suppressed by point mutations in ftsE or ftsX 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
reduced colony size with accumulation of dead cells in the colonies 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
degradation of gamma-polyglutamic acid PubMed
Protein family
Peptidase C40 family (according to UniProt)
Domains
contains three N-acetylglucosamine-polymer-binding LysM domains PubMed
C-terminal D,L-endopeptidase domain (NlpC/P60 domain) PubMed
3 LysM domains (aa 26-69, aa 86-129, aa 149-192) (according to UniProt)
Structure
4XCM (PDB) (from Thermus thermophilus, 34% identity) PubMed
P54421 (AlphaFold)
Effectors of protein activity
activity requires functional MreB and MreBH PubMed
both enzymatic activities are inhibited by interaction with IseA PubMed
activity is inhibited by Mg2+ 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
Expression and Regulation
Operons
Genes
lytE
Description
PubMed
Regulation
induced at high temperature (SigI, WalR) PubMed
Regulatory mechanism
WalR: activation, PubMed, in walR regulon
Spo0A: repression, PubMed, in spo0A regulon
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
SigH: sigma factor, PubMed, in sigH regulon
SigI: sigma factor, PubMed, in sigI regulon
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lytE

2025-03-30 05:40:14

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Additional information
expression and/ or activity of LytE is controlled by the length of lipoteichoic acid PubMed
Biological materials
Mutant
1A790 ( lytE::cat), PubMed, available at BGSC
1A792 ( lytE::cat), PubMed, available at BGSC
1A1024 ( lytE::spec), PubMed, available at BGSC
BKE09420 (lytE::erm  trpC2) available at BGSC and in Jörg Stülke's lab,  PubMed, upstream reverse: _UP1_CATATTTTCCTCCCCAAATG,  downstream forward: _UP4_TAATTTTTAGAGAAAACCCG
BKK09420 (lytE::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATATTTTCCTCCCCAAATG,  downstream forward: _UP4_TAATTTTTAGAGAAAACCCG
FLAG-tag construct
GP2020 lytE-3xFLAG spec (based on pGP1331), available in Jörg Stülke's lab
References
Reviews
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Original Publications
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Page visits: 9926

Time of last update: 2025-04-06 05:35:15

Author of last update: Jstuelk