PROSITE logo
Black ribbon
We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU01257


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01257
General rule information [?]

Accession PRU01257
Dates 03-OCT-2019 (Created)
22-NOV-2019 (Last updated, Version 3)
Data class Domain;
Predictors PROSITE; PS51909; LYSOZYME_I
Name Invertebrate (I)-type lysozyme domain
Function I-type lysozymes have been identified in phylogenetically diverse organisms, including mollusca, nematoda, annelida, arthropoda and echinodermata. I-type lysozymes play an important role in immunity and digestion in invertebrates and are usually regarded as the first barrier against pathogens. I-type lysozymes exert multiple activities, such as muramidase, isopeptidase, chitinase, and non-enzymatic antibacterial activities.
Scope(s) Eukaryota
Metazoa
Example(s) Q8IU26;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1>
Protein name + RecName: EC=3.2.1.17;

Comments [?]

CATALYTIC ACTIVITY Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17;
end case
SIMILARITYBelongs to the glycosyl hydrolase 22 family. Type-I lysozyme subfamily.
case <FTGroup:1>

Keywords [?]

Antimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
Antibiotic
end case
case <FTTag:disulf>
Disulfide bond
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0003824; Molecular function:catalytic activity
GO:0019835; Biological process:cytolysis
GO:0042742; Biological process:defense response to bacterium
GO:0016798; Molecular function:hydrolase activity, acting on glycosyl bonds
GO:0008152; Biological process:metabolic process
GO:0016787; Molecular function:hydrolase activity

Features [?]

From: PS51909
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="I-type lysozyme #"
ACT_SITE 16 16 /note="Proton donor" E 1
ACT_SITE 26 26 /note="Nucleophile" D 1
DISULFID 8 91 disulf C-x*-C
DISULFID 11 123 disulf C-x*-C
DISULFID 13 19 disulf C-x*-C
DISULFID 23 32 disulf C-x*-C
DISULFID 45 73 disulf C-x*-C
DISULFID 63 69 disulf C-x*-C
DISULFID 87 105 disulf C-x*-C

Additional information [?]

Size range 110-130 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

UniProtKB rule member sequences [?]