A0A6G8ANN9 · A0A6G8ANN9_9ENTE

  • Protein
    UDP-N-acetylmuramyl-tripeptide synthetase
  • Gene
    murE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

150650100150200250300350400450500
TypeIDPosition(s)Description
Binding site46UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site124-130ATP (UniProtKB | ChEBI)
Binding site168-169UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site195UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site203UDP-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
      G7081_05755

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HDW17A
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Enterococcaceae > Vagococcus

Accessions

  • Primary accession
    A0A6G8ANN9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue237N6-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
Domain123-328Mur ligase central
Domain350-477Mur ligase C-terminal

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    506
  • Mass (Da)
    55,622
  • Last updated
    2020-08-12 v1
  • Checksum
    A953668CA36C1D82
MLSFNQMINLLTEHQLLKEYISNGVWHFTPTADLDDKTIKHITYDSRAVTEGSLFFCKGLAFKVDYLEQALAQGASFYVTEKNYELETDAIGIVVTDIKKAMAVISMAFYNYPQDDLKIIAYTGTKGKTTAAYFSKFILDVATQSKTALLSTMETILDGKTATKSLLTTPEAVDLYRMMAEAVSNGMTHLVMEVSSQAYKTQRVYGLDFDVAIFLNISEDHIGTIEHPDFDDYFYCKRQLMTHAKEVIINRNSDFVEIIEEVSQQAGANVTTYGDDSVEADYTFVSSAEGKGKFVVTSTQDSLNLSGDYQINLLGDFNQGNALSAMIATALVGATSESMITGLELAKVPGRMDTVTTNKGVPIYVDFAHNLLSLQTLLSFVKKEHADRRLVVVIGSTGGKGESRRKDFGNVLSELADVAILTSDDPGTESAKDIAAEIESYLSDRVERLTELNRAFAIKHALETATEKDVIVLAGKGSDKYQVIGTERTPYEGDLEIATKLIEGGL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP049886
EMBL· GenBank· DDBJ
QIL46616.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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