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O69557 · MURE_MYCLE

  • 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 site52UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site139-145ATP (UniProtKB | ChEBI)
Binding site181-182UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site208UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site216UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site410meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site434-437meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site488meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site492meso-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
    • ORF names
      MLCB268.07c
    • Ordered locus names
      ML0909

Organism names

Accessions

  • Primary accession
    O69557

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00001019121-530UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
Modified residue248N6-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
Motif434-437Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    530
  • Mass (Da)
    54,808
  • Last updated
    1998-08-01 v1
  • MD5 Checksum
    22B9FA457FB5FD54439707FF763E030C
MTEVVAVPVRLRPSATAGVRLPELVAQVGAVLADGPGQAATVPDIPVTGVTLRAQEVLSGDLFAALAGASTHGARYAGVALERGAVAVLTDVAGVAELTAQASSVPILIHPEPRSVLGGLAAAAYGHPSNRMTVVGITGTSGKTTTTYMVEAGLRAGGRVVGLVGTIGIRIDGADIPSFLTTPEAPALQAMLAAMVERGVETVVMEVSSHALSLGRVEGTQFAVAGFTNLSRDHLDFHPDMEEYFEAKAVLFDPHSLLRARTVVVCIDDDAGRATAARAGDAITVSALGQPASWRATDIRSPGVGAQEFTAVDPAGVQHRVGIRLPGRYNVANCLVALAILDVVGVSPEQASLGFRDIRIPGRLERIDCGQDFLALVDYAHKPGALHSVLTALLQPDHRLAVVFGAGGERDPGKRAPMGEIAAELADLVVVTDDNPRGEDPAAIRRDILTGTVAAGGAAQVVEIGDRRAAIQYAVAWAGPDDVVLVAGKGHETGQRGAAETCPFDDRVELARALQVRDARLLPAPGRACQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL022602
EMBL· GenBank· DDBJ
CAA18673.1
EMBL· GenBank· DDBJ
Genomic DNA
AL583920
EMBL· GenBank· DDBJ
CAC31290.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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