Difference between revisions of "LytE"
Line 39: | Line 39: | ||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
− | {{SubtiWiki category|[[cell wall degradation/ turnover]]}} | + | {{SubtiWiki category|[[cell wall degradation/ turnover]]}}, |
+ | {{SubtiWiki category|[[cell wall synthesis]]}} | ||
+ | |||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
Line 57: | Line 59: | ||
* growth defect at high temperature {{PubMed|21541672}} | * growth defect at high temperature {{PubMed|21541672}} | ||
* inactivation of ''[[lytE]]'' strongly restores beta-lactam resistance in a ''[[sigM]]'' mutant by delaying cell lysis {{PubMed|22211522}} | * inactivation of ''[[lytE]]'' strongly restores beta-lactam resistance in a ''[[sigM]]'' mutant by delaying cell lysis {{PubMed|22211522}} | ||
+ | * a ''[[lytE]]'' mutation is synthetically lethal with ''[[ftsE]]'' and ''[[ftsX]]'' mutation (due to a lack of autolysin activity) {{PubMed|xxx}} | ||
+ | * a ''[[lytE]]'' mutation increases the cell separation defect of a ''[[lytF]]'' mutant {{PubMed|xxx}} | ||
=== Database entries === | === Database entries === | ||
Line 118: | Line 122: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=lytE_1018998_1020002_1 lytE] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=lytE_1018998_1020002_1 lytE] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigA]] {{PubMed|9573210}}, [[SigH]] {{PubMed|9573210}}, [[SigI]] {{PubMed|21541672}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|9573210}}, [[SigH]] {{PubMed|9573210}}, [[SigI]] {{PubMed|21541672}} |
* '''Regulation:''' | * '''Regulation:''' |
Revision as of 12:33, 16 July 2013
- Description: cell wall hydrolase (major autolysin), 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 separation, cell proliferation |
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 |
Contents
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
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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:
- C-terminal D,L-endopeptidase domain PubMed
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P54421
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: lytE PubMed
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Additional reviews: PubMed
Original publications
Additional publications: PubMed