Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.8.13 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
Search for more literature for 2.7.8.13

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
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
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)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q03521
-
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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