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A0A1D2SAW4 · A0A1D2SAW4_9BURK

  • Protein
    Multifunctional fusion protein
  • 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.
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.

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 site28UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site111-117ATP (UniProtKB | ChEBI)
Binding site160-161UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site187UDP-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 site392meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site416-419meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site467meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site471meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site614-620ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity
Molecular FunctionUDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity
Molecular FunctionUDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine 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
    Multifunctional fusion protein

Including 2 domains:

  • 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
  • Recommended name
    UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
  • EC number
  • Alternative names
    • D-alanyl-D-alanine-adding enzyme

Gene names

    • Name
      murE
    • Synonyms
      murF
    • ORF names
      ABS45_03510

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Comamonas

Accessions

  • Primary accession
    A0A1D2SAW4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue227N6-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

Family & Domains

Features

Showing features for domain, motif, region.

Type
IDPosition(s)Description
Domain24-68Mur ligase N-terminal catalytic
Domain109-317Mur ligase central
Domain340-469Mur ligase C-terminal
Motif416-419Meso-diaminopimelate recognition motif
Domain532-600Mur ligase N-terminal catalytic
Domain612-815Mur ligase central
Region750-772Disordered
Domain846-959Mur ligase C-terminal

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.
Belongs to the MurCDEF family. MurF subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    975
  • Mass (Da)
    102,308
  • Last updated
    2016-11-30 v1
  • MD5 Checksum
    DE14FC1D6EB0AF98259DB24D11056827
MTLQRLSSVDKALAFLRQRVGGQLRIDSRAVQPGDGFIALQGYHADGRAFVQDALARGAAACVVEVEGDAAGLVDDDRVAALAGLKAHAGALASLWLGEPSRHLKVLSVTGTNGKTSTAWWLAHALQKLSKQELLALDGCGLIGTLGVGIAPDLQATGLTTPNPLRLQQVLADFVRAGVGACAIEASSIGIAEQRLAGTQIDTALFTNLTQDHLDYHGSMQAYWEAKRALFDWPGLRAAVVNIDDEHGAALHRVLAARALDLWSVAVDAPARLRAVDLHHGATGLAFTVVEGGERVPLSTRLVGQYNVSNLLGVIAALRSLGVSLAAACGVCADLEAVPGRMQQVTEPGQPLAVVDYAHTPDALAKVLAALRPLAQGRGGRLWCVFGCGGDRDALKRPLMGAAAQQGADRVIVTSDNPRSEEAAAIVHQILQGMIASRHVQAELDRATAIAQALAQADARDVVLIAGKGHEPYQEIAGVRRPFSDLEQARLALARRAPQLHEMATLQQAWELIRARVPQARLVGDGALAFTRVHTDTRTLAPGDLFVALKGERFDAHDFLPQARSAGAAAAIAHGGLAAAGLAGIEVPDTLAALAALATGWRARFDWSLIAVTGSNGKTTVTQMIASILRAWQGDAALATSGNFNNAVGVPLTLLRLRAGHRAAVVELGMNHPGEIAELAAMAQPTVALVNNAQREHQEFMHGVEAVARENGAVLQALPPDGVAVFPAFDVFTPLWRELAGSRRCITFASPSLQPSPQRGEGRPAQGSDVHCPQAQWQGDAWAVQIVTPQGAFDTRLQIAGEHNLGNALAATACAVATGVPLAAVAEGLAQFRPVAGRSRAFTMRDGARELVVVDDTYNANPDSVRAAIDVLASLPAPRLLVLGDMGEVGSQGPEFHAEAGDYAKQHGVTRLYALGALTRHAVQSFGAGAEHFDAADALIAATRAALPTTGSVLVKGSRFMRMERVVRAIEEAAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MEDS01000005
EMBL· GenBank· DDBJ
ODS93273.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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