A0A4P6TTL2 · A0A4P6TTL2_STRSO

  • Protein
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
  • Gene
    murE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site94UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site177-183ATP (UniProtKB | ChEBI)
Binding site219-220UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site246UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site254UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site448meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site472-475meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site528meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site532meso-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
      D0Z67_07275

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KCTC 9819
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A4P6TTL2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue286N6-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 region, compositional bias, domain, motif.

TypeIDPosition(s)Description
Region1-57Disordered
Compositional bias26-51Polar residues
Domain87-161Mur ligase N-terminal catalytic
Domain175-376Mur ligase central
Domain399-530Mur ligase C-terminal
Motif472-475Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    559
  • Mass (Da)
    57,871
  • Last updated
    2019-07-31 v1
  • Checksum
    CE56FFF55330624E
MTTITPDDGNRGTHRTGREPRFSSGAGTPGTLTAVPHADQSQTTQKGASVTNPGPPRPVQVSAIFLAELAGQLGTAAPAETAEPVGVTGITHDSRAVRPGDVYAALSGARLHGADFATQAAGLGAVAVLTDPAGADRAAATGLPVLVVEDPRAEMGELAATIYGHPGRDMLQIGITGTSGKTTTAYLIEGGLRAAGRATGLVGTVETRIGDERIKSERTTPEATDLQALFAVMRERGTDAVAMEVSSHALVLGRVDGCVFDIAVFNNLSPEHMEFHSGMEDYFQAKASLFTPERSRLGVVNADDEYGRRLVTEAGVPVVTFSAEGHPDADWRAEDVQTGPMDSTFTALGPNGERVHARSPLPGPFNVANTLAALAALAAAGIDPQTAADGIAAVPGVPGRLERVDAGQPYLAVVDYAHKTDAVESVLKALRKVTKGRVHLVLGCGGDRDRTKRGPMGAAAARYADTAVLTSDNPRSEDPLAILATMLEGAASVPTHERGEVLLFEERAAAIAAAVGRAAAGDTVLVAGKGHEQGQDIAGVIRPFDDRQVLREAIQNTQG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias26-51Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP032229
EMBL· GenBank· DDBJ
QBJ90127.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp