Q81WC7 · MURE_BACAN

  • Protein
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
  • Gene
    murE
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

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

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site30UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site108-114ATP (UniProtKB | ChEBI)
Binding site149UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site150-151UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site177UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site185UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site383meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site407-410meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site457meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site461meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity
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-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
  • EC number
  • Alternative names
    • Meso-A2pm-adding enzyme
    • Meso-diaminopimelate-adding enzyme
    • UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    • UDP-MurNAc-tripeptide synthetase
    • UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

    • Name
      murE
    • Ordered locus names
      BA_4053, GBAA_4053, BAS3765

Organism names

  • Taxonomic identifier
  • Strains
    • Ames / isolate Porton
    • Ames ancestor
    • Sterne
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group

Accessions

  • Primary accession
    Q81WC7
  • Secondary accessions
    • Q6HUH2
    • Q6KNQ8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001018631-491UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
Modified residue217N6-carboxylysine

Post-translational modification

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

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif407-410Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    491
  • Mass (Da)
    53,705
  • Last updated
    2003-06-01 v1
  • Checksum
    7E2193B06F881669
MKLHTLVSCLHDFPVVPKENPEITSIEADSRKVKEGSLFVCMKGYTVDSHDFAKQAAAQGAAAIVAERPIDVDVPVVLVKNTFRSLAVLADYFYGQPTHKLHLIGITGTNGKTTTSHIMDEIMRAHGHKTGLIGTINMKIGDETFEVKNTTPDALTLQQTFAKMVEHGVDSTVMEVSSHALDLGRVHGCDYDVAVFTNLTQDHLDYHKTMEEYKHAKGLLFAQLGNSYNHNREKYAVLNNDDAVTVEYMRSTAATVVTYGIDTTSDVMAKDIAMTSGGTTFTLVTPYESVNVTMKLIGKFNVYNVLAATAAGLVSGVSLETIIDVIKELAGVPGRFEVVDGGQNYTVIVDYAHTPDSLENVLKTAKQFAKGDVYCIVGCGGDRDRTKRPIMASVATQYATHAIYTSDNPRSEDPAAILDDMVHGANGNNYEVIIDRKEAIHHAITKAKADDIIIIAGKGHETYQIIGKDVHHFDDREVAKEAITERLNNEE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016879
EMBL· GenBank· DDBJ
AAP27779.1
EMBL· GenBank· DDBJ
Genomic DNA
AE017334
EMBL· GenBank· DDBJ
AAT33170.1
EMBL· GenBank· DDBJ
Genomic DNA
AE017225
EMBL· GenBank· DDBJ
AAT56067.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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