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P00708 (LYSC_COLLI) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

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
OrganismColumba livia (Domestic pigeon)
Taxonomic identifier8932 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Columbiformes › Columbidae › Columba

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
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.

Cofactor

Binds 1 calcium ion per subunit.

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
   LigandCalcium
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Lysozyme C
PRO_0000208862

Regions

Calcium binding81 – 9212 By similarity

Sites

Active site351 By similarity
Active site521 By similarity

Amino acid modifications

Disulfide bond6 ↔ 127 By similarity
Disulfide bond30 ↔ 115 By similarity
Disulfide bond64 ↔ 80 By similarity
Disulfide bond76 ↔ 94 By similarity

Sequences

Sequence LengthMass (Da)Tools
P00708-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 96D3BAFDFD934DD8

FASTA12714,452
        10         20         30         40         50         60 
KDIPRCELVK ILRRHGFEGF VGKTVANWVC LVKHESGYRT TAFNNNGPNS RDYGIFQINS 

        70         80         90        100        110        120 
KYWCNDGKTR GSKNACNINC SKLRDDNIAD DIQCAKKIAR EARGLTPWVA WKKYCQGKDL 


SSYVRGC

« Hide

References

[1]"Amino acid sequence of pigeon egg-white lysozyme."
Rodriguez R., Menendez-Arias L., Gonzalez de Buitrago G., Gavilanes J.G.
Biochem. Int. 11:841-843(1985) [PubMed: 4091856] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Egg white.
[2]"Calcium-binding lysozymes."
Nitta K., Tsuge H., Shimazaki K., Sugai S.
Biol. Chem. Hoppe-Seyler 369:671-675(1988) [PubMed: 3214551] [Abstract]
Cited for: CALCIUM-BINDING DATA.
[3]"Crystallization and preliminary X-ray structure analysis of pigeon egg-white lysozyme."
Yao M., Tanaka I., Hikichi K., Nitta K.
J. Biochem. 111:1-3(1992) [PubMed: 1607355] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

PIRLZPY. A00863.

3D structure databases

ProteinModelPortalP00708.
SMRP00708. Positions 1-124.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Phylogenomic databases

HOVERGENHBG052297.

Enzyme and pathway databases

BRENDA3.2.1.17. 3625.

Family and domain databases

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

Entry information

Entry nameLYSC_COLLI
AccessionPrimary (citable) accession number: P00708
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: August 10, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents