TagB

• Description: putative CDP-glycerol:glycerol phosphate glycerophosphotransferase
  
  

Gene name	tagB
Synonyms
Essential	yes PubMed
Product	putative CDP-glycerol:glycerol phosphate glycerophosphotransferase
Function	biosynthesis of teichoic acid
MW, pI	44 kDa, 8.925
Gene length, protein length	1143 bp, 381 aa
Immediate neighbours	tagA, tagC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes, membrane proteins

This gene is a member of the following regulons

PhoP regulon, WalR regulon

The gene

Basic information

• Locus tag: BSU35760

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: adds a single glycerol phosphate residue to the non-reducing end of the undecaprenol-phosphate-linked N-acetylmannosamine-β(1,4)-N-acetylglucosamine-1-phosphate PubMed

• Protein family: CDP-glycerol glycerophosphotransferase 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:
  • cell membrane PubMed

Database entries

• Structure:

• UniProt: P27621

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tagA-tagB PubMed

• Expression browser: tagB PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed when phosphate is available (PhoP) PubMed

• Regulatory mechanism:
  • PhoP: transcription repression PubMed
  • WalR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Alex Formstone, Rut Carballido-López, Philippe Noirot, Jeffery Errington, Dirk-Jan Scheffers
Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis.
J Bacteriol: 2008, 190(5);1812-21
[PubMed:18156271] [WorldCat.org] [DOI] (I p)

Amit P Bhavsar, Michael A D'Elia, Tiffany D Sahakian, Eric D Brown
The Amino terminus of Bacillus subtilis TagB possesses separable localization and functional properties.
J Bacteriol: 2007, 189(19);6816-23
[PubMed:17660278] [WorldCat.org] [DOI] (P p)

Amit P Bhavsar, Ray Truant, Eric D Brown
The TagB protein in Bacillus subtilis 168 is an intracellular peripheral membrane protein that can incorporate glycerol phosphate onto a membrane-bound acceptor in vitro.
J Biol Chem: 2005, 280(44);36691-700
[PubMed:16150696] [WorldCat.org] [DOI] (P p)

Amit P Bhavsar, Laura K Erdman, Jeffrey W Schertzer, Eric D Brown
Teichoic acid is an essential polymer in Bacillus subtilis that is functionally distinct from teichuronic acid.
J Bacteriol: 2004, 186(23);7865-73
[PubMed:15547257] [WorldCat.org] [DOI] (P p)

Alistair Howell, Sarah Dubrac, Kasper Krogh Andersen, David Noone, Juliette Fert, Tarek Msadek, Kevin Devine
Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach.
Mol Microbiol: 2003, 49(6);1639-55
[PubMed:12950927] [WorldCat.org] [DOI] (P p)

W Liu, S Eder, F M Hulett
Analysis of Bacillus subtilis tagAB and tagDEF expression during phosphate starvation identifies a repressor role for PhoP-P.
J Bacteriol: 1998, 180(3);753-8
[PubMed:9457886] [WorldCat.org] [DOI] (P p)

C Mauël, A Bauduret, C Chervet, S Beggah, D Karamata
In Bacillus subtilis 168, teichoic acid of the cross-wall may be different from that of the cylinder: a hypothesis based on transcription analysis of tag genes.
Microbiology (Reading): 1995, 141 ( Pt 10);2379-89
[PubMed:7581998] [WorldCat.org] [DOI] (P p)

C Mauël, M Young, A Monsutti-Grecescu, S A Marriott, D Karamata
Analysis of Bacillus subtilis tag gene expression using transcriptional fusions.
Microbiology (Reading): 1994, 140 ( Pt 9);2279-88
[PubMed:7952180] [WorldCat.org] [DOI] (P p)