Difference between revisions of "TagU"
| Line 103: | Line 103: | ||
* '''Operon:''' ''lytR'' {{PubMed|1357079}} | * '''Operon:''' ''lytR'' {{PubMed|1357079}} | ||
| − | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=lytR_3663281_3664201_1 tagU] {{PubMed|22383849}} |
| + | |||
| + | * '''Sigma factor:''' [[SigA]] {{PubMed|1357079,9636707}}, [[SigX]] {{PubMed|1357079,9636707}} | ||
* '''Regulation:''' | * '''Regulation:''' | ||
| Line 110: | Line 112: | ||
** [[LytR]]: autorepression {{PubMed|1357079}} | ** [[LytR]]: autorepression {{PubMed|1357079}} | ||
| − | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = | ||
Revision as of 07:44, 17 April 2012
- Description: phosphotransferase, attaches teichoic acid, teichuronic acid, or acidic capsular polysaccharide to cell wall peptidoglycan via phosphodiester linkage to N-acteylmuramic acid
| Gene name | tagU |
| Synonyms | lytR |
| Essential | no |
| Product | phosphotransferase, responsible for attachment of anionic polymers to peptidoglycan |
| Function | transfer of anionic cell wall polymers from lipid-linked precursors to peptidoglycan |
| Interactions involving this protein in SubtInteract: TagU | |
| MW, pI | 34 kDa, 9.527 |
| Gene length, protein length | 918 bp, 306 aa |
| Immediate neighbours | lytA, mnaA |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
cell wall synthesis, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU35650
Phenotypes of a mutant
- a tagU mutant has no phenoype, the triple tagT tagU tagV mutant is unable to grow under normal conditions PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: LytR-Cps2a-Psr family PubMed
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): Mg(2+) PubMed
- Effectors of protein activity:
- Localization:
- cytoplasmic membrane (with extracytoplasmic catalaytic domain) PubMed
Database entries
- UniProt: Q02115
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: lytR 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
Yoshikazu Kawai, Jon Marles-Wright, Robert M Cleverley, Robyn Emmins, Shu Ishikawa, Masayoshi Kuwano, Nadja Heinz, Nhat Khai Bui, Christopher N Hoyland, Naotake Ogasawara, Richard J Lewis, Waldemar Vollmer, Richard A Daniel, Jeff Errington
A widespread family of bacterial cell wall assembly proteins.
EMBO J: 2011, 30(24);4931-41
[PubMed:21964069]
[WorldCat.org]
[DOI]
(I e)
Judith Hübscher, Lucas Lüthy, Brigitte Berger-Bächi, Patricia Stutzmann Meier
Phylogenetic distribution and membrane topology of the LytR-CpsA-Psr protein family.
BMC Genomics: 2008, 9;617
[PubMed:19099556]
[WorldCat.org]
[DOI]
(I e)
X Huang, J D Helmann
Identification of target promoters for the Bacillus subtilis sigma X factor using a consensus-directed search.
J Mol Biol: 1998, 279(1);165-73
[PubMed:9636707]
[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)
