A0A7W7DEZ0 · A0A7W7DEZ0_9ACTN

  • Protein
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
  • Gene
    murE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • 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.

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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site44UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site127-133ATP (UniProtKB | ChEBI)
Binding site169-170UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site196UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site204UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site398meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site422-425meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site478meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site482meso-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
      BJ982_006339

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 45784
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Streptosporangiaceae > Sphaerisporangium

Accessions

  • Primary accession
    A0A7W7DEZ0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue236N6-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 motif, domain.

TypeIDPosition(s)Description
Motif422-425Meso-diaminopimelate recognition motif
Domain441-505TRAM

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    510
  • Mass (Da)
    52,947
  • Last updated
    2021-06-02 v1
  • Checksum
    48FF13B7DE2AF710
MRPPSMRPAAGQVRPLSGLAALLGAPSGGGRAPLAAVTGVTIDSRQVRPGDLYVAVRGTSVHGAAFARAAAEAGAAAVLTDPAGRRDAVASGLPVLVVPEPRAVLGTVAAWVYERPSEGLLLLGVTGTSGKSTTSFLMEGGLRAAGHRTGLVGGVEIHVGDLRFTPTLTTPEASDLQGLFALMREQGVTAAAMEVSSHALALGRVDGTRYDVALFTNLSQDHLDFHRDLDDYFRAKARLFTPELSRVGVVNIDDAHGRELAGLAKIPVTTFSSGGAAEADWRAHDVRLGADGSTFRVVGPGGVEADVSVGLPGPFNVANTLGALVALVEAGVPLQTAVHGVGTVTGVPGRMERVPGAQGFQAIVDYSHKPGAVESVLRALREVTSGELIIVLGCGGDRDRGKRPMMGEAAARLADVAVLTSDNPRSEDPVRILFEMLQGVLRVPGRDRAHVIMEPDRAAAIGLAIGRARPGDVVVVAGKGHEQGQYVAGEVLPFDDRQVVAEAISRRERM

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACHND010000001
EMBL· GenBank· DDBJ
MBB4704795.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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