Protein
- UniProt accession
- F1BUQ2 [UniProt]
- Protein name
- Lysozyme
- PhaLP type
-
endolysin
evidence: ML prediction
probability: 99 % (predicted by ML model)
- Protein sequence
-
MRVERVIDACMRNDMPQPVYDAVVSWAFNVGTYAACRSTLGAHINRGEWRSACLQLPRWVFVKGVFSQGLQNRRDRELAWCLKGAA
- Physico‐chemical
properties -
protein length: 86 AA molecular weight: 9801,00000 Da isoelectric point: 9,49189 aromaticity: 0,10465 hydropathy: -0,17209
Domains
Domains [InterPro]
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Erwinia phage ENT90 [NCBI] |
947843 | Peduoviridae > Entnonagintavirus > Entnonagintavirus ENT90 |
Host |
Erwinia amylovora [NCBI] |
552 | Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Erwinia |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
ADX32457.1
[NCBI]
Genbank nucleotide accession
HQ110084
[NCBI]
CDS location
range 6193 -> 6453
strand -
strand -
CDS
ATGCGCGTGGAGCGCGTGATTGATGCCTGTATGCGCAACGACATGCCGCAGCCGGTCTATGACGCGGTGGTGTCGTGGGCGTTTAACGTCGGCACCTACGCCGCCTGCCGCTCCACGCTCGGCGCTCACATCAACCGGGGCGAGTGGCGCAGCGCCTGCCTGCAGCTGCCGCGCTGGGTATTTGTGAAAGGCGTATTCAGCCAGGGGCTGCAGAACCGCCGCGACCGGGAACTGGCCTGGTGCCTGAAGGGGGCTGCATGA
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.