Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00701 (LYSC_COTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme C

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene names
Name:LYZ
OrganismCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Taxonomic identifier93934 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePerdicinaeCoturnix

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lysozymes 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

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. Ref.3

Subunit structure

Monomer.

Subcellular location

Secreted.

Miscellaneous

Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell wall macromolecule catabolic process

Inferred from electronic annotation. Source: InterPro

cytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2 Ref.3
Chain19 – 147129Lysozyme C
PRO_0000018496

Sites

Active site531
Active site701

Amino acid modifications

Disulfide bond24 ↔ 145
Disulfide bond48 ↔ 133
Disulfide bond82 ↔ 98
Disulfide bond94 ↔ 112

Experimental info

Sequence conflict391Q → LK AA sequence Ref.3

Secondary structure

........................ 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00701 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: B1D03EDA0E85DED3

FASTA14716,278
        10         20         30         40         50         60 
MRSLLVLVLC FLPLAALGKV YGRCELAAAM KRHGLDKYQG YSLGNWVCAA KFESNFNTQA 

        70         80         90        100        110        120 
TNRNTDGSTD YGILQINSRW WCNDGRTPGS RNLCNIPCSA LLSSDITASV NCAKKIVSDV 

       130        140 
HGMNAWVAWR NRCKGTDVNA WIRGCRL 

« Hide

References

[1]"Evolutionary shift in the site of cleavage of prelysozyme."
Weisman L.S., Krummel B.M., Wilson A.C.
J. Biol. Chem. 261:2309-2313(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-18.
[2]"The amino acid sequence of quail lysozyme."
Kaneda M., Kato I., Tominaga N., Titani K., Narita K.
J. Biochem. 66:747-749(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-147.
[3]"Quail lysozyme II."
Thammasirirak S., Preecharram S., Phonkham P., Daduang S., Araki T., Svasti J.
Submitted (SEP-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 19-147, CATALYTIC ACTIVITY.
Tissue: Egg white.
[4]Houdusse A., Bentley G.A., Poljak R.J., Souchon H., Zhang Z.
Submitted (JUN-1993) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 19-147.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRLZQJE. A91922.
JU0237.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IHLX-ray1.40A19-147[»]
ProteinModelPortalP00701.
SMRP00701. Positions 19-147.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEP00701.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052297.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00701.

Entry information

Entry nameLYSC_COTJA
AccessionPrimary (citable) accession number: P00701
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: October 16, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries