CpgA

• Description: activity stimulated by ribosomes
  
  

Gene name	cpgA
Synonyms	yloQ
Essential	no
Product	GTPase
Function	unknown
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	33 kDa, 4.743
Gene length, protein length	894 bp, 298 aa
Immediate neighbours	prkC, rpe
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU15780

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: engC GTPase domain (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on Ser/ Thr by PrkC, dephosphorylated by PrpC PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1T9H

• UniProt: O34530

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:
  • prpC-prkC-cpgA PubMed
  • cpgA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Tony Wilkinson, York University, U.K. homepage

References

Cédric Absalon, Michal Obuchowski, Edwige Madec, Delphine Delattre, I Barry Holland, Simone J Séror
CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 3);932-943
[PubMed:19246764] [WorldCat.org] [DOI] (P p)

Ishita M Shah, Maria-Halima Laaberki, David L Popham, Jonathan Dworkin
A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments.
Cell: 2008, 135(3);486-96
[PubMed:18984160] [WorldCat.org] [DOI] (I p)

Cédric Absalon, Kassem Hamze, Didier Blanot, Claude Frehel, Rut Carballido-Lopez, Barry I Holland, Jean van Heijenoort, Simone J Séror
The GTPase CpgA is implicated in the deposition of the peptidoglycan sacculus in Bacillus subtilis.
J Bacteriol: 2008, 190(10);3786-90
[PubMed:18344364] [WorldCat.org] [DOI] (I p)

Alison Hunt, Joy P Rawlins, Helena B Thomaides, Jeff Errington
Functional analysis of 11 putative essential genes in Bacillus subtilis.
Microbiology (Reading): 2006, 152(Pt 10);2895-2907
[PubMed:17005971] [WorldCat.org] [DOI] (P p)

Lionel Cladière, Kassem Hamze, Edwige Madec, Vladimir M Levdikov, Anthony J Wilkinson, I Barry Holland, Simone J Séror
The GTPase, CpgA(YloQ), a putative translation factor, is implicated in morphogenesis in Bacillus subtilis.
Mol Genet Genomics: 2006, 275(4);409-20
[PubMed:16485133] [WorldCat.org] [DOI] (P p)

Adam Iwanicki, Krzysztof Hinc, Simone Seror, Grzegorz Wegrzyn, Michal Obuchowski
Transcription in the prpC-yloQ region in Bacillus subtilis.
Arch Microbiol: 2005, 183(6);421-30
[PubMed:16025310] [WorldCat.org] [DOI] (P p)

Tracey L Campbell, Denis M Daigle, Eric D Brown
Characterization of the Bacillus subtilis GTPase YloQ and its role in ribosome function.
Biochem J: 2005, 389(Pt 3);843-52
[PubMed:15828870] [WorldCat.org] [DOI] (I p)

Vladimir M Levdikov, Elena V Blagova, James A Brannigan, Lionel Cladière, Alfred A Antson, Michail N Isupov, Simone J Séror, Anthony J Wilkinson
The crystal structure of YloQ, a circularly permuted GTPase essential for Bacillus subtilis viability.
J Mol Biol: 2004, 340(4);767-82
[PubMed:15223319] [WorldCat.org] [DOI] (P p)

Lionel Cladière, Elena Blagova, Vladimir M Levdikov, James A Brannigan, Simone J Séror, Anthony J Wilkinson
Crystallization of YloQ, a GTPase of unknown function essential for Bacillus subtilis viability.
Acta Crystallogr D Biol Crystallogr: 2004, 60(Pt 2);329-30
[PubMed:14747714] [WorldCat.org] [DOI] (P p)