A0A1E7G5W9 · A0A1E7G5W9_LACLC

Function

function

Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

148350100150200250300350400450
TypeIDPosition(s)Description
Binding site43UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site116-122ATP (UniProtKB | ChEBI)
Binding site160-161UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site187UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site195UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionacid-amino acid ligase activity
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Biological Processcell division
Biological Processcell wall organization
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UDP-N-acetylmuramyl-tripeptide synthetase
  • EC number
  • Alternative names
    • UDP-MurNAc-tripeptide synthetase

Gene names

    • Name
      murE
    • ORF names
      AJ89_03705

Organism names

Accessions

  • Primary accession
    A0A1E7G5W9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue229N6-carboxylysine

Post-translational modification

Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain115-310Mur ligase central
Domain332-458Mur ligase C-terminal

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    483
  • Mass (Da)
    54,112
  • Last updated
    2017-02-15 v1
  • Checksum
    8BE769D398430CA7
MIKLEQVVEILKKDNNFREISSAGEYYFNWPKEVNFDQLSYDSRKSTKDTLFFAKGLNFKKEYLTDLEAAFYVSEFDYEVALPAIIVTDVKRAMALIAANFYEFPQNKLKTLALTGTKGKTTSAYFAKAILDKMNGGKTALLSTAQTTLDGQNYFKSELTTPESLDLLEMMAKALENGMTHLVMEVSSQAYKTERVYGLTFDVGVFLNISPDHIGPVEHPTLEDYFYCKRQLLKNSRYFVANAEMNHFAIIKEELNERKIPHAFYGADSENKIIESKGLHFVTDGSVSGEFDIRLLGRFNQENALATALATKALGASFENIRQGLASAIVPGRMELLTAKNGAHIYIDYAHNGLSLENLVEVVEDHHAGQLFLVLGSTGNKGESRRKDFGQVIENHPRLNVILTTDDSNRENPKTIADEIASFVSRELDFELDRKFAIKKAISKTQNSDDAVIIAGKGADMFQLKDGKREPYIGDSPAAQKYL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JMMZ01000008
EMBL· GenBank· DDBJ
OEU40354.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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