A0A2Y1SX98 · A0A2Y1SX98_STAAU

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

Function

function

Catalyzes the addition of L-lysine 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 site30UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site110-116ATP (UniProtKB | ChEBI)
Binding site151UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site152-153UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site179UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site187UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine 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--L-lysine ligase
  • EC number
  • Alternative names
    • L-lysine-adding enzyme
    • UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase
    • UDP-MurNAc-tripeptide synthetase
    • UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

    • Name
      murE
    • ORF names
      DQV00_13050
      , E1948_04840
      , E1948_11415
      , G0Z31_12335
      , G6Y24_06305
      , GQX52_12290
      , M1K003_1680
      , SAMEA4008601_02642
      , SAMEA4008627_00441
      , SAMEA70153168_01629

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • M1K003
    • Pt061.1
    • pt061.1
    • Lr2
    • UP89
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A2Y1SX98
  • Secondary accessions
    • A0A4U0B7Y1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue219N6-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
Domain108-311Mur ligase central
Domain334-458Mur ligase C-terminal
Motif406-409L-lysine recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    54,233
  • Last updated
    2018-09-12 v1
  • Checksum
    B5BD224B23DA5A13
MDASTLFKKVKVKRVLGSLEQQIDDITTDSRTAREGSIFVASVGYTVDSHKFCQNVADQGCKLVVVNKEQSLPANVTQVVVPDTLRVASILAHTLYDYPSHQLVTFGVTGTNGKTSIATMIHLIQRKLQKNSAYLGTNGFQINETKTKGANTTPETVSLTKKIKEAVDAGAESMTLEVSSHGLVLGRLRGVEFDVAIFSNLTQDHLDFHGTMEAYGHAKSLLFSQLGEDLSKEKYVVLNNDDSFSEYLRTVTPYEVFSYGIDEEAQFMAKNIQESLQGVSFDFVTPFGTYPVKSPYVGKFNISNIMAAMIAVWSKGTSLETIIKAVENLEPVEGRLEVLDPSLPIDLIIDYAHTADGMNKLIDAVQPFVKQKLIFLVGMAGERDLTKTPEMGRVACRADYVIFTPDNPANDDPKMLTAELAKGATHQNYIEFDDRAEGIKHAIDIAEPGDTVVLASKGREPYQIMPGHIKVPHRDDLIGLEAAYKKFGGGPVDQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAIGYB010000021
EMBL· GenBank· DDBJ
CAC5894423.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIGYX010000001
EMBL· GenBank· DDBJ
CAC5918387.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIIGN010000005
EMBL· GenBank· DDBJ
CAC8238328.1
EMBL· GenBank· DDBJ
Genomic DNA
BDVT01000007
EMBL· GenBank· DDBJ
GBV20686.1
EMBL· GenBank· DDBJ
Genomic DNA
JAIGOF010000017
EMBL· GenBank· DDBJ
MBX8595199.1
EMBL· GenBank· DDBJ
Genomic DNA
JAAJIY010000054
EMBL· GenBank· DDBJ
NGK22276.1
EMBL· GenBank· DDBJ
Genomic DNA
JAALTR010000170
EMBL· GenBank· DDBJ
NGW67107.1
EMBL· GenBank· DDBJ
Genomic DNA
JAANDN010000108
EMBL· GenBank· DDBJ
NUY69397.1
EMBL· GenBank· DDBJ
Genomic DNA
CP038850
EMBL· GenBank· DDBJ
QCT56790.1
EMBL· GenBank· DDBJ
Genomic DNA
QNXM01000003
EMBL· GenBank· DDBJ
TXL50549.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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