PcrB

• Description: heptaprenylglyceryl phosphate synthase
  
  

Gene name	pcrB
Synonyms	yerE
Essential	no
Product	heptaprenylglyceryl phosphate synthase
Function	unknown
MW, pI	24 kDa, 4.204
Gene length, protein length	684 bp, 228 aa
Immediate neighbours	yerD, pcrA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

lipid metabolism/ other

The gene

Basic information

• Locus tag: BSU06600

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: GGGP synthase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • forms dimers PubMed

• Localization:

Database entries

• Structure: 1VIZ

• UniProt: O34790

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: pcrB-pcrA-ligA-yerH PubMed

• Expression browser: pcrB PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

David Peterhoff, Hermann Zellner, Harald Guldan, Rainer Merkl, Reinhard Sterner, Patrick Babinger
Dimerization determines substrate specificity of a bacterial prenyltransferase.
Chembiochem: 2012, 13(9);1297-303
[PubMed:22614947] [WorldCat.org] [DOI] (I p)

Harald Guldan, Frank-Michael Matysik, Marco Bocola, Reinhard Sterner, Patrick Babinger
Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria.
Angew Chem Int Ed Engl: 2011, 50(35);8188-91
[PubMed:21761520] [WorldCat.org] [DOI] (I p)

Harald Guldan, Reinhard Sterner, Patrick Babinger
Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.
Biochemistry: 2008, 47(28);7376-84
[PubMed:18558723] [WorldCat.org] [DOI] (I p)

M A Petit, E Dervyn, M Rose, K D Entian, S McGovern, S D Ehrlich, C Bruand
PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication.
Mol Microbiol: 1998, 29(1);261-73
[PubMed:9701819] [WorldCat.org] [DOI] (P p)