Difference between revisions of "LytF"

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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''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}}
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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=References=
 
=References=
 +
== Reviews==
 +
<pubmed>18430080</pubmed>
 +
== Original publications ==
 
<pubmed> 20351052,10322020,10206711,14594841,18761696, 19542270 22139507 23855774 23091053</pubmed>
 
<pubmed> 20351052,10322020,10206711,14594841,18761696, 19542270 22139507 23855774 23091053</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:46, 27 December 2013

  • Description: gamma-D-glutamate-meso-diaminopimelate muropeptidase (major autolysin)

Gene name lytF
Synonyms cwlE, yhdD
Essential no
Product gamma-D-glutamate-meso-diaminopimelate muropeptidase (major autolysin)
Function cell separation
Gene expression levels in SubtiExpress: lytF
Interactions involving this protein in SubtInteract: LytF
MW, pI 51 kDa, 10.41
Gene length, protein length 1464 bp, 488 aa
Immediate neighbours yhdC, nsrR
Sequences Protein DNA DNA_with_flanks
Genetic context
LytF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LytF expression.png















Categories containing this gene/protein

cell wall degradation/ turnover

This gene is a member of the following regulons

SigD regulon, SlrR regulon

The gene

Basic information

  • Locus tag: BSU09370

Phenotypes of a mutant

  • cell separation defect, this is increased by a lytE mutation 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:
  • Modification:
  • Effectors of protein activity:
  • Localization:
    • secreted (according to Swiss-Prot)
    • localizes to cell septa and poles PubMed

Database entries

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

Additional information

Expression and regulation

  • 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

Girbe Buist, Anton Steen, Jan Kok, Oscar P Kuipers
LysM, a widely distributed protein motif for binding to (peptido)glycans.
Mol Microbiol: 2008, 68(4);838-47
[PubMed:18430080] [WorldCat.org] [DOI] (I p)

Original publications

Jeffrey Meisner, Paula Montero Llopis, Lok-To Sham, Ethan Garner, Thomas G Bernhardt, David Z Rudner
FtsEX is required for CwlO peptidoglycan hydrolase activity during cell wall elongation in Bacillus subtilis.
Mol Microbiol: 2013, 89(6);1069-83
[PubMed:23855774] [WorldCat.org] [DOI] (I p)

Ryoichi Arai, Sadaharu Fukui, Naoya Kobayashi, Junichi Sekiguchi
Solution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilis, reveals a novel fold with a characteristic inhibitory loop.
J Biol Chem: 2012, 287(53);44736-48
[PubMed:23091053] [WorldCat.org] [DOI] (I p)

Masayuki Hashimoto, Seika Ooiwa, Junichi Sekiguchi
Synthetic lethality of the lytE cwlO genotype in Bacillus subtilis is caused by lack of D,L-endopeptidase activity at the lateral cell wall.
J Bacteriol: 2012, 194(4);796-803
[PubMed:22139507] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Thomas Norman, Roberto Kolter, Richard Losick
An epigenetic switch governing daughter cell separation in Bacillus subtilis.
Genes Dev: 2010, 24(8);754-65
[PubMed:20351052] [WorldCat.org] [DOI] (I p)

Rui Chen, Sarah B Guttenplan, Kris M Blair, Daniel B Kearns
Role of the sigmaD-dependent autolysins in Bacillus subtilis population heterogeneity.
J Bacteriol: 2009, 191(18);5775-84
[PubMed:19542270] [WorldCat.org] [DOI] (I p)

Hiroki Yamamoto, Yukiko Miyake, Miharu Hisaoka, Shin-Ichirou Kurosawa, Junichi Sekiguchi
The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis.
Mol Microbiol: 2008, 70(2);297-310
[PubMed:18761696] [WorldCat.org] [DOI] (I p)

Hiroki Yamamoto, Shin-ichirou Kurosawa, Junichi Sekiguchi
Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases.
J Bacteriol: 2003, 185(22);6666-77
[PubMed:14594841] [WorldCat.org] [DOI] (P p)

R Ohnishi, S Ishikawa, J Sekiguchi
Peptidoglycan hydrolase LytF plays a role in cell separation with CwlF during vegetative growth of Bacillus subtilis.
J Bacteriol: 1999, 181(10);3178-84
[PubMed:10322020] [WorldCat.org] [DOI] (P p)

Philippe Margot, Marco Pagni, Dimitri Karamata
Bacillus subtilis 168 gene lytF encodes a gamma-D-glutamate-meso-diaminopimelate muropeptidase expressed by the alternative vegetative sigma factor, sigmaD.
Microbiology (Reading): 1999, 145 ( Pt 1);57-65
[PubMed:10206711] [WorldCat.org] [DOI] (P p)