[1]	PROTEIN SEQUENCE. TISSUE=Egg white; PubMed=7075596 [NCBI, ExPASy, EBI, Israel, Japan] Schoentgen F., Jolles J., Jolles P.; "Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose-type lysozyme."; Eur. J. Biochem. 123:489-497(1982).
[2]	PROTEIN SEQUENCE OF 1-34. TISSUE=Egg white; DOI=10.1007/BF01732553; PubMed=904618 [NCBI, ExPASy, EBI, Israel, Japan] Jolles J., Perin J.-P., Jolles P.; "The ostrich (Struthio camelus) egg-white lysozyme."; Mol. Cell. Biochem. 17:39-44(1977).

Comments

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.
SUBCELLULAR LOCATION: Secreted.
MISCELLANEOUS: Shows preference for N-acetylmuramic acid residues that are substituted with a peptide moiety. It acts only as a glycanohydrolase.
SIMILARITY: Belongs to the glycosyl hydrolase 23 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

A00874; LZOSG.

3D structure databases

HSSP

P00718; 153L. [HSSP ENTRY / PDB]

SMR

P00719; 1-185.

ModBase

P00719.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
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

IPR002152; Glyco_hydro_23.
IPR008258; Lytic_TGlycosylase-like_cat.
Graphical view of domain structure.

Pfam

PF01464; SLT; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001065; Lysozyme_g; 1.

PR00749; LYSOZYMEG.

Phylogenomic databases

HOVERGEN

P00719; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 185`	`185`	`Lysozyme g.`	`PRO_0000193516`
`ACT_SITE`	`73 73`		`By similarity.`
`ACT_SITE`	`86 86`		`By similarity.`
`DISULFID`	`4 60`		`By similarity.`
`DISULFID`	`18 29`		`By similarity.`

Sequence information

Length: 185 AA [This is the length of the unprocessed precursor]

Molecular weight: 20563 Da [This is the MW of the unprocessed precursor]

CRC64: 02B78AF5D526B5DC [This is a checksum on the sequence]

        10         20         30         40         50         60 
RTGCYGDVNR VDTTGASCKS AKPEKLNYCG VAASRKIAER DLQSMDRYKA LIKKVGQKLC 

        70         80         90        100        110        120 
VDPAVIAGII SRESHAGKAL RNGWGDNGNG FGLMQVDRRS HKPVGEWNGE RHLMQGTEIL 

       130        140        150        160        170        180 
ISMIKAIQKK FPRWTKEQQL KGGISAYNAG PGNVRSYERM DIGTTHDDYA NDVVARAQYY 


KQHGY

P00719 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