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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 PRU00680


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00680
General rule information [?]

Accession PRU00680
Dates 18-DEC-2007 (Created)
19-NOV-2022 (Last updated, Version 13)
Data class Domain;
Predictors PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2
Name Glycosyl hydrolases family 22 (GH22) domain
Function Alpha-lactalbumin, a regulatory protein in milk, and lysozyme (EC 3.2.1.17) C (chicken type), which acts as a bacteriolytic enzyme, belong to a family of proteins with eight conserved cysteines that form four disulfide bonds. Alpha-lactalbumin lacks the enzymatic activity and the corresponding Glu and Asp residues. Alpha-lactalbumin binds a calcium ion, while most lysozyme C do not bind calcium.
Scope(s) Eukaryota
Metazoa
Example(s) Q659U0;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1>
Protein name + AltName: Full=lysozyme C;
                 EC=3.2.1.17;
AltName: Full=1,4-beta-N-acetylmuramidase C;

Comments [?]

FUNCTIONLysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
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.

Keywords [?]

case <FTGroup:1>
Antimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
end case
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
Calcium
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
end case
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
GO:0005509; Molecular function:calcium ion binding
end case

Cross-references [?]

PROSITE PS00128; GLYCOSYL_HYDROL_F22_1; 1;

Features [?]

From: PS51348
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="C-type lysozyme #"
ACT_SITE 35 35 E 1
ACT_SITE 52 52 D 1
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
BINDING 82 82 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 binds [HCUEDKQNMYWSTRX]
BINDING 85 85 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 binds [HCUEDKQNMYWSTRX]
BINDING 87 87 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 binds [HCUEDKQNMYWSTRX]
BINDING 90 90 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 binds [HCUEDKQNMYWSTRX]
BINDING 91 91 /ligand="Ca(2+)"
/ligand_id="ChEBI:CHEBI:29108"
/ligand_label="#1"		 binds [HCUEDKQNMYWSTRX]
end case
DISULFID 6 125 disulf C-x*-C
DISULFID 30 114 disulf C-x*-C
DISULFID 64 80 disulf C-x*-C
DISULFID 76 94 disulf C-x*-C

Additional information [?]

Size range 110-140 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 [?]