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Literature summary extracted from

  • Zheng, Y.; Struck, D.K.; Bernhardt, T.G.; Young, R.
    Genetic analysis of MraY inhibition by the {varphi}X174 protein E (2008), Genetics, 180, 1459-1466.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.13 in medium-copy plasmid pBAD30 for complementation studies in Escherichia coli K-12 mutant strain RY3321 lacking endogenous MraY Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.8.13 D231N catalytically inactive, overexpression does not rescue bacteria from protein E-induced lysis Bacillus subtilis
2.7.8.13 D267N enzymatically inactive, overexpression rescues bacteria from protein E-induced lysis Escherichia coli
2.7.8.13 deltaL172 single-codon deletion in putative transmembrane domain TMD5, mediates PhiX174-resistancy only in catalytically active form and at high culture densitiy Escherichia coli
2.7.8.13 F288L missense mutation in putative transmembrane domain TMD9, mediates PhiX174-resistancy only in catalytically active form Escherichia coli
2.7.8.13 G168S mediates PhiX174-resistancy only at high culture densitiy, similar to wild-type Escherichia coli
2.7.8.13 P170L mediates PhiX174-resistancy only in catalytically active form and at high culture densitiy, interacts with Epos gene product more strongly than with protein E Escherichia coli
2.7.8.13 V291M mediates PhiX174-resistancy only at high culture densitiy, similar to wild-type Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.8.13 protein E lysis protein of bacteriophage PhiX174, (strong) binding to MraY leads to cell lysis, overexpression of MraY wild-type rescues bacteria from protein E-induced lysis Bacillus subtilis
2.7.8.13 protein E lysis protein of bacteriophage PhiX174, binding to MraY leads to cell lysis, overexpression of MraY wild-type rescues bacteria from protein E-induced lysis Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenyl phosphate Escherichia coli Lipid I precursor synthesis, murein biosynthesis UMP + MurNAc-pentapeptide-diphosphoundecaprenol
-
 ?
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenyl phosphate Bacillus subtilis Lipid I precursor synthesis, murein biosynthesis UMP + MurNAc-pentapeptide-diphosphoundecaprenol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.13 Bacillus subtilis Q03521
-
-
2.7.8.13 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenyl phosphate Lipid I precursor synthesis, murein biosynthesis Escherichia coli UMP + MurNAc-pentapeptide-diphosphoundecaprenol
-
 ?
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenyl phosphate Lipid I precursor synthesis, murein biosynthesis Bacillus subtilis UMP + MurNAc-pentapeptide-diphosphoundecaprenol
-
 ?
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenyl phosphate efficient complementation of enzymatic activity in bacterial strain lacking endogenous MraY Bacillus subtilis UMP + MurNAc-pentapeptide-diphosphoundecaprenol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.8.13 MraY
-
 Escherichia coli
2.7.8.13 MraY
-
 Bacillus subtilis
2.7.8.13 phospho-MurNAc-pentapeptide translocase
-
 Escherichia coli
2.7.8.13 phospho-MurNAc-pentapeptide translocase
-
 Bacillus subtilis
2.7.8.13 translocase I
-
 Escherichia coli
2.7.8.13 translocase I
-
 Bacillus subtilis