[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Stomach; PubMed=7815930 [NCBI, ExPASy, EBI, Israel, Japan] Kornegay J.R., Schilling J.W., Wilson A.C.; "Molecular adaptation of a leaf-eating bird: stomach lysozyme of the hoatzin."; Mol. Biol. Evol. 11:921-928(1994).

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

EMBL

L36032; AAA73935.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55241; A55241.

3D structure databases

HSSP

P37156; 1JUG. [HSSP ENTRY / PDB]

ModBase

Q91159.

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

Q91159; -.

Other

ProtoNet

Q91159.

UniRef

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

Keywords

Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`CHAIN`	`20 145`	`126`	`Lysozyme C.`	`PRO_0000018498`
`ACT_SITE`	`53 53`		`By similarity.`
`ACT_SITE`	`70 70`		`By similarity.`
`DISULFID`	`25 145`		`By similarity.`
`DISULFID`	`49 133`		`By similarity.`
`DISULFID`	`82 98`		`By similarity.`
`DISULFID`	`94 112`		`By similarity.`
`VARIANT`	`23 23`	`1`	`P -> S (in 50% of the molecules).`

Sequence information

Length: 145 AA [This is the length of the unprocessed precursor]

Molecular weight: 16268 Da [This is the MW of the unprocessed precursor]

CRC64: FCDA921A2CAE7E94 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLFFGFLLAF LSAVPGTEGE IIPRCELVKI LREHGFEGFE GTTIADWICL VQHESDYNTE 

        70         80         90        100        110        120 
AYNNNGPSRD YGIFQINSKY WCNDGKTSGA VDGCHISCSE LMTNDLEDDI KCAKKIARDA 

       130        140 
HGLTPWYGWK NHCEGRDLSS YVKGC

Q91159 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