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R7RNQ5 · R7RNQ5_9CLOT

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 site29UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site109-115ATP (UniProtKB | ChEBI)
Binding site151-152UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site178UDP-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 site376meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site400-403meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site452meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site456meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site588-594ATP (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
      TCEL_01741

Organism names

Accessions

  • Primary accession
    R7RNQ5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue218N6-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
Domain21-95Mur ligase N-terminal catalytic
Domain107-305Mur ligase central
Domain327-454Mur ligase C-terminal
Motif400-403Meso-diaminopimelate recognition motif
Domain504-575Mur ligase N-terminal catalytic
Domain586-771Mur ligase central
Domain794-914Mur 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
    930
  • Mass (Da)
    104,505
  • Last updated
    2013-07-24 v1
  • MD5 Checksum
    414A3ED7E4C00E49AD0B193F5010C5DB
MRLFDMLKGLDYVLIKGSDLEIEHITYSSREVVEGSLFFCIEGFKTDGHQFIQDAVNRGAKAIIVSKDVNVEEDVTIVKVKDTREAMAIVSSNFYGNPSKFFNVIGVTGTNGKTTSTFMIKSILDEYNRKTALLGTIYNIIGEKIEEAKRTTPESMDLQRLYSEMKNSGITDCIMEVSSHSLELKRVYGVEFKVGIFTNLTQDHLDFHKTMENYFNAKMKLFENSENCIINIDDEYGKRAAEMFKNKRVITYGIDNRADIMAENLKIDSDGSQFDLVINGVKRRVKLHLPGKFNVYNALGCIGAAIALNIPVDIAIKGLEKLQSVPGRSEKIVSHAGFTVVIDYAHTPDGIENILKAAREYTSGRLITLFGCGGDRDKGKRPLMGKAAGELSDFCIITSDNPRSEDPMAIINDIIPGIEQTGCKYIVIEDRKKAIEYAIKNAKKGDVIVVAGKGHEKYQILKDRTIEFDERKIVEGFLKEIITTDDIIKATCGKVFNLNENIIINKITTDSRKVEKGDVFIALKGEKFDGHDFLGEVKDKGAVCAVVSKFIPNVDIPQILVDDTLRAYKEIARYYRRRFDIPIVAITGSCGKTTTKEMIASVLSSRLNVHKTEKNFNNEIGLPMTILNLKSKHEASVVEMGMNHFGEIESLSYVALPKIAVITNIGTAHIENLGSRENILKAKMEITTYFNEENILVINSDDDMLSTVKTDKYKIIKFAINSDADYKAYDIIDLGQDGMEFKCNISGVERRFKVNLPGQHNIYNALSAIAVGDILGLQYEDIYNGILNFNPGSMRMNIVELKDDIKFIVDCYNANPDSMKAAIDVLNKFNGRRIAVLGDMFELGEFSKAMHKEVGNYLVDKCDVLIAIGEFAKEYYNEAMGKIECYYFINKEEALDFIKNFIKRDDVVLFKASRGMKLEYISDSLIEQRK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAVN010000091
EMBL· GenBank· DDBJ
CDF57827.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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