[1]	PROTEIN SEQUENCE OF 1-18. PubMed=3511061 [NCBI, ExPASy, EBI, Israel, Japan] Weisman L.S., Krummel B.M., Wilson A.C.; "Evolutionary shift in the site of cleavage of prelysozyme."; J. Biol. Chem. 261:2309-2313(1986).
[2]	PROTEIN SEQUENCE OF 19-147. TISSUE=Egg white; PubMed=5440837 [NCBI, ExPASy, EBI, Israel, Japan] Larue J.N., Speck J.C. Jr.; "Turkey egg white lysozyme. Preparation of the crystalline enzyme and investigation of the amino acid sequence."; J. Biol. Chem. 245:1985-1991(1970).
[3]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BONDS. DOI=10.1016/0022-2836(77)90238-8; PubMed=886621 [NCBI, ExPASy, EBI, Israel, Japan] Sarma R., Bott R.; "Crystallographic study of turkey egg-white lysozyme and its complex with a disaccharide."; J. Mol. Biol. 113:555-565(1977).
[4]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1107/S0108768191012466; PubMed=1515108 [NCBI, ExPASy, EBI, Israel, Japan] Howell P.L., Almo S.C., Parsons M., Petsko G.A., Hajdu J.; "Structure determination of turkey egg-white lysozyme using Laue diffraction data."; Acta Crystallogr. B 48:200-207(1992).
[5]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). DOI=10.1107/S0907444994013612; PubMed=15299795 [NCBI, ExPASy, EBI, Israel, Japan] Howell P.L.; "Structure of hexagonal turkey egg-white lysozyme at 1.65-A resolution."; Acta Crystallogr. D 51:654-662(1995).
[6]	STRUCTURE BY NMR. PubMed=8344294 [NCBI, ExPASy, EBI, Israel, Japan] Bartik K., Dobson C.M., Redfield C.; "1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme."; Eur. J. Biochem. 215:255-266(1993).

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.
SUBUNIT: Monomer.
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.
SIMILARITY: Belongs to the glycosyl hydrolase 22 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

C92574; LZTK.

3D structure databases

PDB

135L; X-ray; 1.30 A; A=19-147.	[ExPASy / RCSB / EBI]
1DZB; X-ray; 2.00 A; X/Y=19-147.	[ExPASy / RCSB / EBI]
1JEF; X-ray; 1.77 A; A=19-147.	[ExPASy / RCSB / EBI]
1JSE; X-ray; 1.12 A; A=19-147.	[ExPASy / RCSB / EBI]
1JTP; X-ray; 1.90 A; L/M=19-147.	[ExPASy / RCSB / EBI]
1LJN; X-ray; 1.19 A; A=19-147.	[ExPASy / RCSB / EBI]
1LZ2; X-ray; 2.80 A; A=19-147.	[ExPASy / RCSB / EBI]
1LZY; X-ray; 1.55 A; A=19-147.	[ExPASy / RCSB / EBI]
1TEW; X-ray; 1.65 A; A=19-147.	[ExPASy / RCSB / EBI]
1UAC; X-ray; 1.70 A; Y=19-147.	[ExPASy / RCSB / EBI]
1XFT; X-ray; 3.35 A; A=19-147.	[ExPASy / RCSB / EBI]
2LZ2; X-ray; 2.20 A; A=19-147.	[ExPASy / RCSB / EBI]
3LZ2; X-ray; 2.50 A; A=19-147.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

135L; -.
1DZB; -.
1JEF; -.
1JSE; -.
1JTP; -.
1LJN; -.
1LZ2; -.
1LZY; -.
1TEW; -.
1UAC; -.
1XFT; -.
2LZ2; -.
3LZ2; -.

DisProt

DP00259; -.

ModBase

P00703.

Ontologies

GO:0019835;	Biological process: cytolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0042742;	Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001916; Glyco_hydro_22.
IPR000974; Glyco_hydro_22_lys.
Graphical view of domain structure.

Pfam

PF00062; Lys; 1.
Pfam graphical view of domain structure.

PRINTS

PR00137; LYSOZYME.
PR00135; LYZLACT.

SMART

SM00263; LYZ1; 1.
SMART graphical view of domain structure.

PROSITE

PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

P00703; -.

Other

BindingDB

P00703; -.

LinkHub

P00703; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing; Glycosidase; Hydrolase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`CHAIN`	`19 147`	`129`	`Lysozyme C.`	`PRO_0000018497`
`DISULFID`	`24 145`
`DISULFID`	`48 133`
`DISULFID`	`82 98`
`DISULFID`	`94 112`
`HELIX`	`23 32`	`10`
`HELIX`	`43 54`	`12`
`STRAND`	`61 63`	`3`
`STRAND`	`69 71`	`3`
`TURN`	`72 75`	`4`
`TURN`	`78 81`	`4`
`STRAND`	`85 87`	`3`
`HELIX`	`98 102`	`5`
`HELIX`	`107 117`	`11`
`HELIX`	`122 125`	`4`
`HELIX`	`127 132`	`6`
`TURN`	`133 135`	`3`
`HELIX`	`138 142`	`5`

Sequence information

Length: 147 AA [This is the length of the unprocessed precursor]

Molecular weight: 16135 Da [This is the MW of the unprocessed precursor]

CRC64: 77C54CD70834583F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRSLLILVLC FLPLAALGKV YGRCELAAAM KRLGLDNYRG YSLGNWVCAA KFESNFNTHA 

        70         80         90        100        110        120 
TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCNIPCSA LLSSDITASV NCAKKIASGG 

       130        140 
NGMNAWVAWR NRCKGTDVHA WIRGCRL

P00703 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools