A0A015W385 · A0A015W385_BACFG

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 site30UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site111-117ATP (UniProtKB | ChEBI)
Binding site153-154UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site180UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site186UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site188UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site378meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site402-405meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site455meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site459meso-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
      M125_0574

Organism names

Accessions

  • Primary accession
    A0A015W385

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue220N6-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
Domain22-97Mur ligase N-terminal catalytic
Domain109-305Mur ligase central
Domain327-457Mur ligase C-terminal
Motif402-405Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    485
  • Mass (Da)
    53,186
  • Last updated
    2014-06-11 v1
  • Checksum
    F4D56E3EB1D13AB7
MKLKEILTSIQPVKITGNQDIEITGVDIDSRQVESGHLFMAMRGTQTDGHAYIPAAVEKGATAILCEELPAELAEGVTYIQVADSEDAVGKAATTFYGNPSSKLELVGVTGTNGKTTIATLLYNTFRYFGYKVGLISTVCNYIDDEAIPTEHTTPDPITLNRLLGRMADEGCKYVFMEVSSHSIAQKRISGLKFAGGIFTNLTRDHLDYHKTVENYLKAKKKFFDDMPKNSFSLTNLDDKNGLVMTQNTKSKVYTYSLRSLSDFKGRVLESHFEGMLLDFNNHELAVQFIGKFNASNLLAVFGAAVLLGKKEEDVLVALSTLHPVAGRFDAIRSPQGYTAIVDYAHTPDALVNVLNAIHGVLEGKGKVITVVGAGGNRDKGKRPIMAKEAARASDRVIITSDNPRFEEPQDIINDMLAGLDTEDKKKTLSIADRKEAIRTACMLAEKGDVILVAGKGHENYQDIKGVKHHFDDKEVLKEIFSLTV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JGDB01000014
EMBL· GenBank· DDBJ
EXY92673.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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