V8QNH3 · V8QNH3_9BURK

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 site21UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site23UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site111-117ATP (UniProtKB | ChEBI)
Binding site154-155UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site181UDP-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 site189UDP-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 site465meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site469meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site580-586ATP (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
      murF
    • Synonyms
      murE
    • ORF names
      W822_21245

Organism names

Accessions

  • Primary accession
    V8QNH3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue221N6-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
Domain20-97Mur ligase N-terminal catalytic
Domain109-311Mur ligase central
Domain351-467Mur ligase C-terminal
Motif416-419Meso-diaminopimelate recognition motif
Domain499-543Mur ligase N-terminal catalytic
Domain578-768Mur ligase central
Domain790-907Mur ligase C-terminal

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    931
  • Mass (Da)
    98,927
  • Last updated
    2014-02-19 v1
  • Checksum
    59A7F4A727D38F69
MTGTISEWLLGHVTDKADLKLDSRDIQKGDVFVACTGSVVNGLAYIADAVKNGAAAVLAEVASDAESQAFDDSGYDVPVLPVVNLRMQLGQIADAWYGHPSEAVSVIAVTGTNGKTSCVTWIAEALNAVGKACATIGTLGTVLPDGTNLGGYLTTPDVLTLHRQIAQMRDAGVQYVAMEASSIGIEQGRMNGLRVKVAAFTNLTLDHLDYHQTMARYEAAKAALFAWPGLSHAIVNLDDEAGQRIFEHSSAQARAGYSLRASPLAAYTAVEHEFHDYGLVFTLRTPGGDAQLTTRLLGEHSISNILLVVAVLDALGIHLQQSAGLISLLKPVPGRLQTVTAIGADPGSKLPLVVVDYSHTPDSLERALQALRPVATARGGHLACVFGCGGDRDKTKRPLMGQLAARLADQVLVTSDNPRTEVPGDILNDILKGMPDDARAEPDRGCAIIEVILKASPADVVLIAGKGHETYQEINHVRQPFDDIEWSRLGLLLRGQPAISTDSRQIPENGLFIAIRGEQHDAHDFIADAQQAGAAAALVSSRDPAVSLPQILVADTTQALMSMGHAWRRQFSFPLIAVAGSNGKTTTKEMISSILAAAVGAAHRFATEGNLNNQWGVPRSLLRLTCDHQLAVLELGMNHPGEIEQLAVLVEPDIAVVTNAQREHQEFMHTVEAVAIENGQVFRSLSTAGTAVFPADEPYADLWRDLAGGRRVLTFGQNDSADFYAESVVQDSQGISFVMKSPVGEIDIRLAIAGQHNVRNSLAAAACAHAAGISLADIRAGLQAFAPVKGRMRSHTLSGGLTLVDDSYNANPDSVIAAIDVLAALPAPTVLVLGDMAEVGENGPQMHEEVGQYARSKGITYVFTYGNASALTARACGAAAEHMTDIHEIANRVVARQPASILVKGSRSMRMERVVQDLLSWSEQKEAGHAV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AYXT01000013
EMBL· GenBank· DDBJ
ETF00888.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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