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A0A9X4Y850 · A0A9X4Y850_9GAMM

  • Protein
    Membrane-bound lytic murein transglycosylase F
  • Gene
    mltF
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

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

  • 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 site308

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

Names & Taxonomy

Protein names

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

Gene names

    • Name
      mltF
    • ORF names
      GLW01_00060

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 22507_15_FS
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Vreelandella

Accessions

  • Primary accession
    A0A9X4Y850

Proteomes

Subcellular Location

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

Keywords

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain37-261Solute-binding protein family 3/N-terminal
Region262-461LT domain

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

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    461
  • Mass (Da)
    53,333
  • Last updated
    2023-11-08 v1
  • MD5 Checksum
    11424679AEA912CF684AB9D014BFDC70
MYRVRRIVFLAAIVAVVGCTNDQGQARTLQAIKEEGTLVVLTRNAPTTWYLGRDGKPTGPEYDMVEAFASHLGVDVSYNIKPSIRSIIEGIENGEGDLAAAGLTITPKRQERFRFGPPYQDVTQQVVCRRDNVQPESVEELVGLELTVIADSSYVERLEALKESHPELEWQTVDNRSTEQLLYDVWQREIDCTIADSNIVDHNRRYFPELIAPFNLNRSESLGWMMAQPRKDLESAVASWLESFRKSGRLEVVKEHYYGYFEVFDYVDTRRLIRRVDERYPKYRSYFETAAEQYDLPYILLSAQGYQESHWRARARSPTGVRGIMMLTLNTAKEVGVDNRLDPKQSIFGGAKYLAKLKNERFSDKVEEPDRTWLALAAYNVGRGHLHDAQRLAREQDLNPHRWGDVKQVLPLLSKKFIYQNLKYGYARGYEPVRYVQRIREYQHILENEIEVLSVEPPDPE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WMEX01000001
EMBL· GenBank· DDBJ
MYL25176.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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