PgcA

• Description: alpha-phosphoglucomutase, required for UDP-glucose synthesis, inhibits FtsZ ring assembly (indirect effect due to a defect in UDP-glucose synthesis)
  
  

Gene name	pgcA
Synonyms	yhxB, gtaC, gtaE
Essential	no
Product	alpha-phosphoglucomutase
Function	interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate
Gene expression levels in SubtiExpress: pgcA
Metabolic function and regulation of this protein in SubtiPathways: pgcA
MW, pI	62 kDa, 4.913
Gene length, protein length	1695 bp, 565 aa
Immediate neighbours	glpD, yhcY
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell wall synthesis, lipid metabolism/ other, phosphoproteins

The gene

Basic information

• Locus tag: BSU09310

Phenotypes of a mutant

• the inactivation of pgcA suppresses the poor and filametous growth of the yvcL zapA double mutant PubMed

Database entries

• BsubCyc: BSU09310

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate (according to Swiss-Prot)

• Protein family: phosphohexose mutase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated on ser/ thr/ tyr PubMed, PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU09310

• Structure:

• UniProt: P18159

• KEGG entry: [2]

• E.C. number: 5.4.2.2

Additional information

PgcA inhibits FtsZ ring assembly (indirect effect due to a defect in UDP-glucose synthesis)PubMed

Expression and regulation

• Operon:

• Expression browser: pgcA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Katarina Surdova, Pamela Gamba, Dennis Claessen, Tjalling Siersma, Martijs J Jonker, Jeff Errington, Leendert W Hamoen
The conserved DNA-binding protein WhiA is involved in cell division in Bacillus subtilis.
J Bacteriol: 2013, 195(24);5450-60
[PubMed:24097947] [WorldCat.org] [DOI] (I p)

Norbert S Hill, Ryosuke Kadoya, Dhruba K Chattoraj, Petra Anne Levin
Cell size and the initiation of DNA replication in bacteria.
PLoS Genet: 2012, 8(3);e1002549
[PubMed:22396664] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Richard B Weart, Amy H Lee, An-Chun Chien, Daniel P Haeusser, Norbert S Hill, Petra Anne Levin
A metabolic sensor governing cell size in bacteria.
Cell: 2007, 130(2);335-47
[PubMed:17662947] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Vladimir Lazarevic, Blazenka Soldo, Noël Médico, Harold Pooley, Sierd Bron, Dimitri Karamata
Bacillus subtilis alpha-phosphoglucomutase is required for normal cell morphology and biofilm formation.
Appl Environ Microbiol: 2005, 71(1);39-45
[PubMed:15640167] [WorldCat.org] [DOI] (P p)

Steven S Branda, José Eduardo González-Pastor, Etienne Dervyn, S Dusko Ehrlich, Richard Losick, Roberto Kolter
Genes involved in formation of structured multicellular communities by Bacillus subtilis.
J Bacteriol: 2004, 186(12);3970-9
[PubMed:15175311] [WorldCat.org] [DOI] (P p)