Difference between revisions of "LytE"

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(Basic information/ Evolution)
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* '''Description:''' cell wall hydrolase (major autolysin),endopeptidase-type autolysin <br/><br/>
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* '''Description:''' cell wall hydrolase (major autolysin), D,L-endopeptidase-type autolysin <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || cell wall hydrolase (major autolysin),endopeptidase-type autolysin
 
|style="background:#ABCDEF;" align="center"| '''Product''' || cell wall hydrolase (major autolysin),endopeptidase-type autolysin
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || major autolysin, cell separation, cell lysis
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|style="background:#ABCDEF;" align="center"|'''Function''' || major autolysin, cell separation, cell proliferation
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 37 kDa, 10.713   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 37 kDa, 10.713   
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
** a ''[[cwlO]] [[lytE]]'' mutant is not viable {{PubMed|17581128}}
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** a ''[[cwlO]] [[lytE]]'' mutant is not viable {{PubMed|17581128,22139507}}
 
** growth defect at high temperature {{PubMed|21541672}}
 
** growth defect at high temperature {{PubMed|21541672}}
  
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* '''Domains:'''  
 
* '''Domains:'''  
 +
** C-terminal D,L-endopeptidase domain {{PubMed|22139507}}
  
 
* '''Modification:'''
 
* '''Modification:'''
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** [[MreBH]]-[[LytE]] {{PubMed|16950129}}
 
** [[MreBH]]-[[LytE]] {{PubMed|16950129}}
  
* '''[[Localization]]:''' secreted (according to Swiss-Prot), binds the cell wall {{PubMed|21261835}}
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* '''[[Localization]]:'''  
 +
** secreted (according to Swiss-Prot)
 +
** binds the cell wall {{PubMed|21261835}}
 +
** localizes to cell septa, poles and lateral sidewall of the cell (via the N-terminal domain) {{PubMed|22139507}}
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 11:58, 8 December 2011

  • 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
MW, pI 37 kDa, 10.713
Gene length, protein length 1029 bp, 343 aa
Immediate neighbours phoA, citR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LytE context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell wall degradation/ turnover

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

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:
  • Localization:
    • secreted (according to Swiss-Prot)
    • binds the cell wall PubMed
    • localizes to cell septa, poles and lateral sidewall of the cell (via the N-terminal domain) PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

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

Additional publications: PubMed