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A0KJ50 · MLTF_AERHH

Function

function

Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.

Catalytic activity

  • Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
    EC:4.2.2.n1 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site316

GO annotations

AspectTerm
Cellular Componentcell outer membrane
Molecular Functionlytic transglycosylase activity
Biological Processcell wall macromolecule catabolic process
Biological Processcell wall organization
Biological Processpeptidoglycan catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Membrane-bound lytic murein transglycosylase F
  • EC number
  • Alternative names
    • Murein lyase F

Gene names

    • Name
      mltF
    • Ordered locus names
      AHA_1765

Organism names

Accessions

  • Primary accession
    A0KJ50

Proteomes

Subcellular Location

Cell outer membrane ; Peripheral membrane protein
Note: Attached to the inner leaflet of the outer membrane.

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-31
ChainPRO_000035391732-496Membrane-bound lytic murein transglycosylase F

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region32-271Non-LT domain
Region273-496LT domain
Compositional bias464-478Basic and acidic residues
Region464-486Disordered

Domain

The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.

Sequence similarities

In the N-terminal section; belongs to the bacterial solute-binding protein 3 family.
In the C-terminal section; belongs to the transglycosylase Slt family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    496
  • Mass (Da)
    56,811
  • Last updated
    2006-12-12 v1
  • MD5 Checksum
    D6DC950C03A245CBD28855A4C1AEB003
MPIFSTRVLTYLRCIFRLFIGLTLLLTLVGCDFYTPSSQLEQIRQRGEIRVGTIYGPTSYYQRDDTAQGFDYELAQSYADWLGVKLTIVPVYSTAELVELLRKGKLDLAAAAIVVTPERRQLFRFGPGFYQVSPKLVYRNGSPKPKDIGDLKGNIVVPAGSTGEDLLKELAKQYPNLKWSTNRDADVEELLKQVADGKIDYTVVQDTVLARTQRYYPELTEGMTLAKNQTVAWAMTKLPDDSLYASIIDFFGQRFMDGAIAKLDEKYFGHVQNFDFVDTRTFLQRAKSLLPKYQDLFKTHANVVDWRLLAAISYQESHWDPEARSYTGVRGMMMLTEPTAKAMGVNNRLHPEESIKGGARYLEQMMEKVPASVPDDEKVWFALTAYNIGYGHMMDARRLTKELGKNPDAWSDVKEVLPLLQQSRWHRKVRYGYARGGEARNYVNNVRQYYQSLLWLDNEQQKAHRREELDDDDSSEPPSAERPTVIAEVVKQITLR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias464-478Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000462
EMBL· GenBank· DDBJ
ABK38788.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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