[1]	PROTEIN SEQUENCE. TISSUE=Egg white; DOI=10.1021/bi00550a013; PubMed=7378374 [NCBI, ExPASy, EBI, Israel, Japan] Simpson R.J., Begg G.S., Dorow D.S., Morgan F.J.; "Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan."; Biochemistry 19:1814-1819(1980).
[2]	PROTEIN SEQUENCE OF 46-68 AND 95-111. DOI=10.1016/0006-291X(90)91922-F; PubMed=2302197 [NCBI, ExPASy, EBI, Israel, Japan] Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J.; "Internal amino acid sequencing of proteins by in situ cyanogen bromide cleavage in polyacrylamide gels."; Biochem. Biophys. Res. Commun. 166:139-145(1990).
[3]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1107/S0907444994009893; PubMed=15299299 [NCBI, ExPASy, EBI, Israel, Japan] Zao Z., Esnouf R., Isaacs N., Stuart D.; "A strategy for rapid and effective refinement applied to black swan lysozyme."; Acta Crystallogr. D 51:331-336(1995).
[4]	X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). DOI=10.1107/S0907444995008468; PubMed=15299731 [NCBI, ExPASy, EBI, Israel, Japan] Karlsen S., Hough E., Rao Z.H., Isaacs N.W.; "Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases."; Acta Crystallogr. D 52:105-114(1996).

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

A00872; LZWSG.

3D structure databases

PDB

1GBS; X-ray; 1.50 A; A=1-185.	[ExPASy / RCSB / EBI]
1LSP; X-ray; 2.45 A; A=1-185.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GBS; -.
1LSP; -.

ModBase

P00717.

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

P00717; -.

Other

LinkHub

P00717; -.

UniRef

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

Keywords

3D-structure; 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_0000193515`
`ACT_SITE`	`73 73`		`By similarity.`
`DISULFID`	`4 60`
`DISULFID`	`18 29`
`HELIX`	`8 10`	`3`
`HELIX`	`18 21`	`4`
`HELIX`	`22 24`	`3`
`HELIX`	`30 46`	`17`
`HELIX`	`49 59`	`11`
`HELIX`	`63 74`	`12`
`HELIX`	`75 77`	`3`
`TURN`	`92 95`	`4`
`TURN`	`98 100`	`3`
`HELIX`	`110 130`	`21`
`HELIX`	`136 149`	`14`
`HELIX`	`151 153`	`3`
`TURN`	`158 163`	`6`
`HELIX`	`165 167`	`3`
`HELIX`	`169 181`	`13`
`TURN`	`182 184`	`3`

Sequence information

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

Molecular weight: 20400 Da [This is the MW of the unprocessed precursor]

CRC64: 22358F632C98342A [This is a checksum on the sequence]

        10         20         30         40         50         60 
RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VPASKTIAER DLKAMDRYKT IIKKVGEKLC 

        70         80         90        100        110        120 
VEPAVIAGII SRESHAGKVL KNGWGDRGNG FGLMQVDKRS HKPQGTWNGE VHITQGTTIL 

       130        140        150        160        170        180 
TDFIKRIQKK FPSWTKDQQL KGGISAYNAG AGNVRSYARM DIGTTHDDYA NDVVARAQYY 


KQHGY

P00717 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