Difference between revisions of "LytE"
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* '''[[Domains]]:''' | * '''[[Domains]]:''' | ||
+ | ** contains four N-acetylglucosamine-polymer-binding [[LysM domain]]s {{PubMed|18430080}} | ||
** C-terminal D,L-endopeptidase domain {{PubMed|22139507}} | ** C-terminal D,L-endopeptidase domain {{PubMed|22139507}} | ||
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=References= | =References= | ||
− | == Reviews == | + | == Reviews== |
− | <pubmed>23066944</pubmed> | + | <pubmed>18430080 23066944</pubmed> |
== Original publications == | == Original publications == | ||
<pubmed>21261835,22211522 16950129,17581128,14594841,9457885,9573210,10322020, 24125693 20059685,14651647, 23869552 21541672 22139507 23855774</pubmed> | <pubmed>21261835,22211522 16950129,17581128,14594841,9457885,9573210,10322020, 24125693 20059685,14651647, 23869552 21541672 22139507 23855774</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:46, 27 December 2013
- 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 |
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
- cells are thinner (reduced diameter) as compared to the wild type 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:
- contains four N-acetylglucosamine-polymer-binding LysM domains PubMed
- C-terminal D,L-endopeptidase domain PubMed
- Modification:
Database entries
- Structure:
- UniProt: P54421
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: lytE PubMed
- Regulation:
- 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
Original publications