Difference between revisions of "LytC"

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(Expression and regulation)
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** [[LytR]]: transcription repression {{PubMed|1357079,16306698}}  
 
** [[LytR]]: transcription repression {{PubMed|1357079,16306698}}  
 
** [[YvrHb]]: transcription repression  {{PubMed|16306698}}  
 
** [[YvrHb]]: transcription repression  {{PubMed|16306698}}  
 +
** [[SlrR]] (in complex with [[SinR]]: transcription repression  {{PubMed|20351052}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''
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=References=
 
=References=
  
<pubmed>19542270 ,10945275,14594841, 1357079 16306698, </pubmed>
+
<pubmed>19542270 ,10945275,14594841, 1357079 16306698, 20351052 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:37, 31 March 2010

  • Description: N-acetylmuramoyl-L-alanine amidase, required for flagellar function PubMed

Gene name lytC
Synonyms cwlB
Essential no
Product N-acetylmuramoyl-L-alanine amidase

(EC 3.5.1.28)

Function major autolysin, cell separation, wall turnover

lysis, motility and general cell lysis induced by sodium azide

MW, pI 52 kDa, 10.108
Gene length, protein length 1488 bp, 496 aa
Immediate neighbours tuaA, lytB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LytC context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU35620

Phenotypes of a mutant

impaired in motility, the phenotype is suppressed by mutations in lonA or smiA PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides (according to Swiss-Prot)
  • Protein family: N-acetylmuramoyl-L-alanine amidase 3 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: secreted (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

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)

Masakuni Serizawa, Keisuke Kodama, Hiroki Yamamoto, Kazuo Kobayashi, Naotake Ogasawara, Junichi Sekiguchi
Functional analysis of the YvrGHb two-component system of Bacillus subtilis: identification of the regulated genes by DNA microarray and northern blot analyses.
Biosci Biotechnol Biochem: 2005, 69(11);2155-69
[PubMed:16306698] [WorldCat.org] [DOI] (P 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)

T Shida, H Hattori, F Ise, J Sekiguchi
Overexpression, purification, and characterization of Bacillus subtilis N-acetylmuramoyl-L-alanine amidase CwlC.
Biosci Biotechnol Biochem: 2000, 64(7);1522-5
[PubMed:10945275] [WorldCat.org] [DOI] (P p)

V Lazarevic, P Margot, B Soldo, D Karamata
Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier.
J Gen Microbiol: 1992, 138(9);1949-61
[PubMed:1357079] [WorldCat.org] [DOI] (P p)