PROTEIN SEQUENCE.
TISSUE=Egg white;
PubMed=1368578 [NCBI, ExPASy, EBI, Israel, Japan]
Araki T., Kuramoto M., Torikata T.;
"The amino acid sequence of Lady Amherst's pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes.";
Agric. Biol. Chem. 54:2299-2308(1990).

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

JH0211; JH0211.

3D structure databases

HSSP

P00698; 1UIB. [HSSP ENTRY / PDB]

SMR

P22910; 1-129.

ModBase

P22910.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0003796;	Molecular function: lysozyme activity (inferred from electronic annotation from InterPro).
GO:0016998;	Biological process: cell wall catabolic process (inferred from electronic annotation from InterPro).
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

P22910; -.

Other

ProtoNet

P22910.

UniRef

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

Keywords

Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing; Glycosidase; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 129`	`129`	`Lysozyme C.`	`PRO_0000208861`
`ACT_SITE`	`35 35`		`By similarity.`
`ACT_SITE`	`52 52`		`By similarity.`
`DISULFID`	`6 127`		`By similarity.`
`DISULFID`	`30 115`		`By similarity.`
`DISULFID`	`64 80`		`By similarity.`
`DISULFID`	`76 94`		`By similarity.`

Sequence information

Length: 129 AA [This is the length of the unprocessed precursor]

Molecular weight: 14311 Da [This is the MW of the unprocessed precursor]

CRC64: E0A6D33123F39CF2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
KVYGRCELAA AMKRLGLDNY RGYSLGNWVC AAKFESNFNT HATNRNTDGS TDYGILQINS 

        70         80         90        100        110        120 
RWWCNDGRTP GSRNLCHIPC SALLSSDITA SVNCAKKIVS DGNGMNAWVA WRNRCKGTDV 


NAWTRGCRL

P22910 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