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A0A143P7I4 · A0A143P7I4_9STAP

  • Protein
    Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
  • Gene
    murT
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue.

Catalytic activity

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site202Zn2+ (UniProtKB | ChEBI)
Binding site205Zn2+ (UniProtKB | ChEBI)
Binding site224Zn2+ (UniProtKB | ChEBI)
Binding site226Zn2+ (UniProtKB | ChEBI)
Active site349

GO annotations

AspectTerm
Molecular Functionacid-amino acid ligase activity
Molecular FunctionATP binding
Molecular Functioncarbon-nitrogen ligase activity on lipid II
Molecular Functionzinc ion binding
Biological Processcell wall organization
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
  • EC number

Gene names

    • Name
      murT
    • ORF names
      EIG99_08495
      , I6J35_03300

Organism names

  • Taxonomic identifier
  • Strains
    • SA11
    • FDAARGOS_1205
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A143P7I4

Proteomes

Interaction

Subunit

Forms a heterodimer with GatD.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain53-274Mur ligase central
Domain313-421Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT C-terminal

Sequence similarities

Belongs to the MurCDEF family. MurT subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    438
  • Mass (Da)
    49,054
  • Last updated
    2016-06-08 v1
  • MD5 Checksum
    17A884AA6D4C6B5EA46A58343D02494E
MRQWTAINLAKLARKASRAVGKRGTDLPGQVARRIDKDILRNLAEKVDDVVFISGTNGKTTTSNLIGHTLKANNIDIIHNNEGANMAAGITSAFIVQSNPNTKIAVIEIDEGSIPRVLKEMTPTMMVFTNFFRDQMDRFGEIDIMVNNIAEAISHKGIKLILNADDPFVSRLKIASESNVYYGMKAHAHEFEQSTMNESKYCPNCGRLLAYDYIHYNQIGHYHCVCGFKREKPKYEVSKFTISPFIHLTIGDTTFDMKIAGDFNAYNAIAAYSVLRELGLNDASIKNGFETYTSDNGRMQYFKSGNKEAMINLAKNPAGMNASLSMGEQLEGKKVYVISLNDNPADGRDISWIYDADFEKLSNQDIETIIVTGSRAEELQLRLKLAEVNVAVVVEKDIYKATARTMDYSGKTVAIPNYTSLEPMLEQLNRSFEMRENQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP069567
EMBL· GenBank· DDBJ
QRP96166.1
EMBL· GenBank· DDBJ
Genomic DNA
RQTE01000155
EMBL· GenBank· DDBJ
RZI01584.1
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.
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