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A0A5R9CXI5 · A0A5R9CXI5_9LACO

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.
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 site41UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site117-123ATP (UniProtKB | ChEBI)
Binding site163-164UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site190UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site198UDP-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
      murE
    • ORF names
      FEZ41_02285

Organism names

Accessions

  • Primary accession
    A0A5R9CXI5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue232N6-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 domain, motif.

Type
IDPosition(s)Description
Domain116-335Mur ligase central
Domain358-486Mur ligase C-terminal
Motif432-435L-lysine recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    514
  • Mass (Da)
    56,521
  • Last updated
    2020-02-26 v1
  • MD5 Checksum
    A8E8584E3734FB33B8E315CFB092A80F
MHILAQITVDEILTLLDEHHLLIRSQFDNSQQRFQSIAYNSKVVSQGCLFFCKGNFRAEYLADAQKRGATGYVSEQEYGHVTIPGIIVSNIQKAMSLLSAAFFGFPQNNLPTIAYTGTKGKTTSAYFTKSILDRMYDKKVGLFSTINTVVGDRPEDVTKSSLTTPESLDLFTNMNRVVQNGMTHLVMEVSSQAYKKNRVYNLHYDIGVFLNISPDHIGRNEHPTFADYLHCKEQLLVNSRTCVINADSDHMVDVYYAAKATSQPEDIFVYHRKGSTKNPELPEDFMYESLADSLTENIIEISAVSPKAHRLGIDGTYHISIPGDYNEGNAVAAAITSGLMKADKKAIAYGLSHTVVPGRMEIYPTHEHGTVYVDYAHNYGSLHAVLDFLKQQSPAGKVIVITGSTGDKGIDRREGLGKAINESANVAYLTTDDPATEDPKVIADEIAAHIDQKRIAVQYIADRKTAISKAIEASHPGDVVVVAGKGHDAFQKINGQNVPYQGDAPIVSKLVKGL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VBSX01000004
EMBL· GenBank· DDBJ
TLQ20564.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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