Protein
- UniProt accession
- A5X378 [UniProt]
- Protein name
- Lysozyme
- PhaLP type
-
endolysin
evidence: ML prediction
probability: 99 % (predicted by ML model)
- Protein sequence
-
MTIKKGIAATVTGAALMLASPLIEEIEGVKYKPYKDIAGIWTVCHGITGNDVILGKEYTRRECDALLAKHMKFAADAVDKAVKVEIPLSMRAALYSFTFNAGTGAFRKSTMLKKIP
- Physico‐chemical
properties -
protein length: 116 AA molecular weight: 12593,00000 Da isoelectric point: 9,42065 aromaticity: 0,07759 hydropathy: 0,14569
Domains
Domains [InterPro]
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Enterobacteria phage A5 [NCBI] |
387264 | Drexlerviridae > Tunavirus > |
Host | No host information |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
ABF71471.1
[NCBI]
Genbank nucleotide accession
DQ525628
[NCBI]
CDS location
range 67 -> 417
strand +
strand +
CDS
ATGACAATCAAGAAAGGTATAGCCGCCACCGTCACAGGGGCGGCTTTAATGTTGGCATCGCCTTTGATTGAAGAAATTGAAGGCGTAAAGTATAAGCCTTACAAGGATATTGCTGGTATCTGGACGGTATGTCACGGCATCACAGGAAATGATGTGATTCTTGGAAAGGAATATACCAGGCGAGAATGTGACGCGCTATTAGCAAAGCACATGAAATTTGCGGCTGACGCTGTTGATAAGGCGGTTAAGGTTGAAATTCCTTTATCAATGCGAGCGGCTCTATACTCATTCACATTCAACGCCGGAACAGGTGCATTCAGGAAATCAACCATGCTTAAAAAGATCCCATAA
Gene Ontology
Description | Category | Evidence (source) | |
---|---|---|---|
GO:0003796 | lysozyme activity | Molecular function | Inferred from Electronic Annotation (UniProt) |
GO:0009253 | peptidoglycan catabolic process | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0016998 | cell wall macromolecule catabolic process | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0031640 | killing of cells of another organism | Biological process | Inferred from Electronic Annotation (UniProt) |
GO:0042742 | defense response to bacterium | Biological process | Inferred from Electronic Annotation (UniProt) |
Enzymatic activity
EC Number | Entry Name | Reaction Catalyzed | Classification | Evidence | Source |
---|---|---|---|---|---|
3.2.1.17 |
lysozyme
aka muramidase |
D-glucosamine residues in chitodextrins |
Hydrolases
Glycosylases
Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
|
match to sequence model evidence used in automatic assertion
ECO:0000256 |
RuleBase:RU003788 |
Tertiary structure
No tertiary structures available.