NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0167-4781(01)00248-2; PubMed=11470157 [NCBI, ExPASy, EBI, Israel, Japan]
Hikima J., Minagawa S., Hirono I., Aoki T.;
"Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein.";
Biochim. Biophys. Acta 1520:35-44(2001).

Comments

FUNCTION: Possesses lytic activity against M.lysodeikticus and several fish pathogenic bacteria.
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.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 6.0;
Temperature dependence: Optimum temperature is 25 degrees Celsius;
TISSUE SPECIFICITY: Ubiquitous.
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

EMBL

AB050591; BAB62407.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050590; BAB62406.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00718; 153L. [HSSP ENTRY / PDB]

ModBase

Q90VZ3.

Ontologies

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).
GO:0009253;	Biological process: peptidoglycan catabolic process (inferred from electronic annotation from InterPro).
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.

PRINTS

PR00749; LYSOZYMEG.

ProtoNet

Q90VZ3.

Phylogenomic databases

HOVERGEN

Q90VZ3; -.

Other

UniRef

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

Keywords

Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 195`	`195`	`Lysozyme g.`	`PRO_0000193520`
`ACT_SITE`	`71 71`		`By similarity.`
`ACT_SITE`	`84 84`		`By similarity.`

Sequence information

Length: 195 AA [This is the length of the unprocessed precursor]

Molecular weight: 21385 Da [This is the MW of the unprocessed precursor]

CRC64: 511DAF31876F662F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYGQIRLVE TSGASGATSQ QDNLGYSGVK ASHKMAEIDS GRMSKYKSKI NKVGQSYGIE 

        70         80         90        100        110        120 
PALIAAIISR ESRAGNQLKD GWGDWNPQRQ AYNAWGLMQV DVNPNGGGHT AVGGWDSEDH 

       130        140        150        160        170        180 
LRQATGILVT FIERIRTKFP GWSKEKQLKG GIAAYNMGDK NVHSYEGVDE NTTGRDYSND 

       190 
VTARAQWYRD NGYSG

Q90VZ3 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