A0A2S6WZP5 · A0A2S6WZP5_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 site91UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site174-180ATP (UniProtKB | ChEBI)
Binding site215-216UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site242UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site250UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site444meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site468-471meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site524meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site528meso-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
      BZZ08_06346

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MH60
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A2S6WZP5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue282N6-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 compositional bias, region, domain, motif.

TypeIDPosition(s)Description
Compositional bias1-21Polar residues
Region1-59Disordered
Compositional bias34-49Polar residues
Domain83-158Mur ligase N-terminal catalytic
Domain172-372Mur ligase central
Domain395-526Mur ligase C-terminal
Motif468-471Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    555
  • Mass (Da)
    57,922
  • Last updated
    2018-07-18 v1
  • Checksum
    F2608449089A00E1
MTTITPDPGNQSASQGAPQPSLRREAGTAGTLTAVPHPDQSQTTQKGHPVTYPGPPRPVRISATPLAELADQLGVAAPDGSAEVTGITHDSRAVRPGDLYAALPGARLHGADFVTQAAGLGAVAVLTDPAGAERAAAAGLPALVVDDPRARMGELAATIYGHPGRDLLQIGITGTSGKTTTAYLVEGGLRTAKSTGLIGTVETRIGDERIKSERTTPEATDLQALFAVMRERGTEAVAMEVSSHALVLGRVDACVFDIAVFTNLSPEHMEFHSGMEDYFQAKAQLFTPRRSRLGVVNVDDEYGRRLANEATVPVVTYSAEGHPDADWRADEVEVGPLDSTFTVLGPKGERIAARSPLAGPFNVANTLAAIVALAAAGLDPQSAADGVAAVPGVPGRLERVDEGQPFFAVVDYAHKTDAVESVLRALRKVTEGRLHVVLGCGGDRDITKREPMGAAVARFADTAVLTSDNPRSEDPLAILATMLQGAASVPAHERGEVQVFEDRAAAIAAAVARARPGDTVLVAGKGHEQGQDIAGVVRPFDDRQVLREAIQKTQG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-21Polar residues
Compositional bias34-49Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MULI01000084
EMBL· GenBank· DDBJ
PPS79068.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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