Difference between revisions of "LytC"
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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 This image was kindly provided by SubtiList
|
Contents
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:
- UniProt: Q02114
- KEGG entry: [3]
- E.C. number: 3.5.1.28
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
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)