J9W627 · J9W627_LENBU

Function

function

Catalyzes the addition of L-lysine 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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site38UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site114-120ATP (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)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine 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--L-lysine ligase
  • EC number
  • Alternative names
    • L-lysine-adding enzyme
    • UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase
    • UDP-MurNAc-tripeptide synthetase
    • UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

    • Name
      mure3
    • Synonyms
      murE
    • ORF names
      LBUCD034_1364

Organism names

Accessions

  • Primary accession
    J9W627

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue229N6-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.

Type
IDPosition(s)Description
Domain113-332Mur ligase central
Domain355-483Mur ligase C-terminal
Motif429-432L-lysine recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    511
  • Mass (Da)
    55,843
  • Last updated
    2012-11-28 v1
  • Checksum
    F8C19730DA071CDB
MAQITVAEVLVLLKEHNLLLESQLSSSSHPFDQIAYNSKLVTDNCLFFCKGNFKSAYLDDARQNGATAYMSEKTYQNAGIPGIIVKNIQKAMSLVSAAFFGFPQDQLPTIAYTGTKGKTTSAYFTKAILDQTYQRKVALSSTINTVVGLKPEDVVKSNLTTPESLDLFTMMRKAADNGMSHLVMEVSSQAYKKNRVYGLHYDVGVFLNISPDHIGRNEHPTFADYLHCKEQLLVNSDVCVLNADGTHLTDIFYTAKATTQPENIFIYGRAGQNQETEFPVDVEYRSLKDSLTENQIQVTARTAKAKQLNIDGVYRIGIPGDYNEGNAVAAAITSALMGAKPTEIAYGLANTTVPGRMEIYQTHDHGTIYVDYAHNYGSLHSVLDFLKKQAPNGKVTVITGSTGDKGIDRREGLGKAINEAADQAYLTTDDPATEDPQQIAKEIAAHIDTSKVATTYIPDRKQAITKAVSESQKGDLVVVAGKGHDQYQKINGKNVPYEGDAAIVKNLVKGL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003043
EMBL· GenBank· DDBJ
AFS00400.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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