A0A353NKH3 · A0A353NKH3_9BACT

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 site40UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site125-131ATP (UniProtKB | ChEBI)
Binding site172-173UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site199UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site205UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site207UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site414meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site438-441meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site506meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site510meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site649-655ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functiontetrahydrofolylpolyglutamate synthase activity
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
      murE
    • Synonyms
      murF
    • ORF names
      DDY32_17530

Organism names

  • Taxonomic identifier
  • Strain
    • UBA9573
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfobulbia > Desulfobulbales > Desulfobulbaceae

Accessions

  • Primary accession
    A0A353NKH3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue239N6-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.

TypeIDPosition(s)Description
Domain33-111Mur ligase N-terminal catalytic
Domain123-337Mur ligase central
Domain375-508Mur ligase C-terminal
Motif438-441Meso-diaminopimelate recognition motif
Domain647-848Mur ligase central
Domain871-1001Mur ligase C-terminal

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,014
  • Mass (Da)
    108,774
  • Last updated
    2018-11-07 v1
  • Checksum
    F24B7B12425907AE
MSIRNTHHTLASLLRGVNCRVVGSSGSLKEKGVTSVTSDSRTVTPESLFVALSGTGTDGHKYLENAIGNGCTAVLCEAGRVSEDLLQKLQAVVIETPDTNKAYAAVAANFYERPAEKLTLVGVTGTNGKTTVTYLLEQVLLQAGHGVGVIGTVNNRYTLADGTKKIIGTRFTTPEAMLLQQLLREMIDCGVEYVVMEVSSHALAQRRVGELSFAVVAFTNLTRDHLDYHLDMDDYFRAKTKLFTEYLVEGGRAVLPVAEARPESPAWLATLHEICAQAGKKVVSWGEGENASVSLVNHTAGLTRTDLVLQTPSGQHRFSTPLVGRFNIDNILTVVAMSCALGIDEAQSCKALAVANGAPGRLERVSLGDDWPVQAPAVFVDYAHTPDALEKVLTTAAALPHRQLIGVFGCGGDRDKGKRPVMGEIATRLCDIAIVTDDNPRTEDPEAIVEQILAGIQNRTEYVKDSSWLAGRKPMDRGCTVIRDRKTAIASAIKSGGPDDIVVIAGKGHEPYQLTIQGKRFFDDRMEAGNVLLSWTDTLAAEAVHGTLLPGSGSGRLLGSVITDSRLASEKGLFVALRGEKHDAHEFAGQAVANGATCLMVERMPSSTADTGVSHILVPDSQKALGDLAAFRRRRLARMTTQVVIGITGSCGKTTVKEMIAAILARKWPEGPDNPIGCVLKTRGNFNNIIGLPISLLPLDLSHRAAVMEMGMNMPGELTRLAEIADPDISIITNIHGAHLLGLGTIEGVARAKEELFAGTKQSGTLVINLDDLWVRQFAGKYPQRKVTFAVRKEDHASPPDFWASDVVQDNGGAIIFTMHYRQETAEIHLFTAGLHNVANALAAAATAATAGASLAEIAAGLADFRPADKRMEILYPKAGFILINDTYNANPASMAAGLRTLKQMARKSTTAIIGDMRELGEASAQAHFDIGRLIAELAIDRVGVVGDFRDDVQRGAIAHGCPAESIRTFADKDAAVSWIKEMIATKRIGKDDLILIKASRGLRFETIVAKLVE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DNSP01000212
EMBL· GenBank· DDBJ
HBG21009.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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