A0A011QFU7 · A0A011QFU7_9PROT

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 site29UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site117-123ATP (UniProtKB | ChEBI)
Binding site156-157UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site183UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site191UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site391meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site415-418meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site463meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site467meso-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
      AW10_03552

Organism names

Accessions

  • Primary accession
    A0A011QFU7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue223N6-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.

TypeIDPosition(s)Description
Domain28-102Mur ligase N-terminal catalytic
Domain115-316Mur ligase central
Domain339-465Mur ligase C-terminal
Motif415-418Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    497
  • Mass (Da)
    52,050
  • Last updated
    2014-06-11 v1
  • Checksum
    7F5CF68B5A1E48AD
MLNAESAARATLARLAALGVQPSGASDDSRQLLAGDLFLAYPGALADGRSHIAAAISAGACAVLWEASTAATDSFSWNADWRIANLPVSGLRSLCGPLAHAVYGRPSERLSLIAVTGTNGKTSVTQWLAACHPRRCATVGTLGAGFPGALVETGFTTPEATTLMRSLARFADDDAQACALEASSIGIAEGRLDGARVDVAVFTNLTHDHLDYHGSLEAYAQAKAELFTWPRLRLAVCNLDDPFGRQLAALSSATKVVGYTQQEAPDGRQGTLRAEGVEETSNGLRFRLCAPNGRALVETGLLGRYNVANLLAVAAVLIDAGMTPKAVAERFAQLRSPAGRLETIGGHNEPLVVVDYAHTPDALDSALGALRAVATARGASLVVIFGCGGDRDRGKRPLMGAIAAKRADRVVLTSDNPRGEDAQRILDEIHSAAPAAEVLVDRGQAIERTILGAHPADVVLIAGKGHETYQEICGVRRPFSDAAQARAALTARQEMVE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JEMX01000093
EMBL· GenBank· DDBJ
EXI77694.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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