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Literature summary extracted from

  • Coker, O.; Palittapongarnpim, P.
    Current understanding of de novo synthesis of bacterial lipid carrier (undecaprenyl phosphate): More enzymes to be discovered (2011), Afr. J. Microbiol. Res., 5, 2555-2565.
No PubMed abstract available

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.27 membrane inner cytoplasmic membrane Bacillus subtilis 16020
-
3.6.1.27 membrane inner cytoplasmic membrane Escherichia coli 16020
-

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.27 Bacillus subtilis P94571
-
-
3.6.1.27 Escherichia coli P60932
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.27 undecaprenyl diphosphate + H2O
-
 Bacillus subtilis undecaprenyl phosphate + phosphate
-
 ?
3.6.1.27 undecaprenyl diphosphate + H2O
-
 Escherichia coli undecaprenyl phosphate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.27 bacA
-
 Escherichia coli
3.6.1.27 BcrC
-
 Bacillus subtilis
3.6.1.27 Und-pp phosphatase
-
 Bacillus subtilis
3.6.1.27 Und-pp phosphatase
-
 Escherichia coli
3.6.1.27 undecaprenyl pyrophosphate phosphatase
-
 Bacillus subtilis
3.6.1.27 undecaprenyl pyrophosphate phosphatase
-
 Escherichia coli
3.6.1.27 Upp-P
-
 Bacillus subtilis
3.6.1.27 Upp-P
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
3.6.1.27 malfunction an undecaprenyl pyrophosphate phosphatase null mutant does not show any significant growth or morphological defect, neither is its sensitivity to bacitracin affected. However, the enzyme activity in the mutant is reduced by 75% Escherichia coli
3.6.1.27 physiological function the enzyme confers resistance to bacitracin Bacillus subtilis