[1]	PROTEIN SEQUENCE. STRAIN=Embden breed; TISSUE=Egg white; Simpson R.J., Morgan F.J.; "Complete amino acid sequence of Embden goose (Anser anser) egg-white lysozyme."; Biochim. Biophys. Acta 744:349-351(1983).
[2]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). DOI=10.1038/303828a0; PubMed=6866082 [NCBI, ExPASy, EBI, Israel, Japan] Gruetter M.G., Weaver L.H., Matthews B.W.; "Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?"; Nature 303:828-831(1983).
[3]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). DOI=10.1016/S0022-2836(95)80038-7; PubMed=7823320 [NCBI, ExPASy, EBI, Israel, Japan] Weaver L.H., Gruetter M.G., Matthews B.W.; "The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the 'goose-type' lysozymes lack a catalytic aspartate residue."; J. Mol. Biol. 245:54-68(1995).

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

A00873; LZGSG.

3D structure databases

PDB

153L; X-ray; 1.60 A; A=1-185.	[ExPASy / RCSB / EBI]
154L; X-ray; 1.60 A; A=1-185.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

153L; -.
154L; -.

ModBase

P00718.

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

P00718; -.

Other

LinkHub

P00718; -.

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_0000193513`
`ACT_SITE`	`73 73`
`ACT_SITE`	`86 86`
`DISULFID`	`4 60`
`DISULFID`	`18 29`
`HELIX`	`8 10`	`3`
`HELIX`	`18 21`	`4`
`HELIX`	`22 24`	`3`
`HELIX`	`31 40`	`10`
`HELIX`	`42 46`	`5`
`HELIX`	`49 59`	`11`
`HELIX`	`63 74`	`12`
`TURN`	`75 79`	`5`
`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`	`169 182`	`14`

Sequence information

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

Molecular weight: 20373 Da [This is the MW of the unprocessed precursor]

CRC64: 0B2F0C9B2A66C324 [This is a checksum on the sequence]

        10         20         30         40         50         60 
RTDCYGNVNR IDTTGASCKT AKPEGLSYCG VSASKKIAER DLQAMDRYKT IIKKVGEKLC 

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

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


KQHGY

P00718 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