Reviewed, UniProtKB/Swiss-Prot P00701 (LYSC_COTJA)

Names and origin

Protein names

Recommended name:
    Lysozyme C
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C

Gene names

Name:

LYZ

Organism

Coturnix coturnix japonica (Japanese quail)

Taxonomic identifier

93934 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Perdicinae › Coturnix

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	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.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	lysozyme activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Chain

19 – 147

129

Lysozyme C

PRO_0000018496

Sites

Active site

53

1

Active site

70

1

Amino acid modifications

Disulfide bond

24 ↔ 145

Disulfide bond

48 ↔ 133

Disulfide bond

82 ↔ 98

Disulfide bond

94 ↔ 112

Experimental info

Sequence conflict

39

1

Q → LK AA sequence Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

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147

Helix Strand Turn

Details...

Helix

23 – 32

10

Helix

43 – 54

12

Beta strand

61 – 63

3

Beta strand

69 – 71

3

Turn

72 – 75

4

Turn

78 – 80

3

Helix

98 – 102

5

Beta strand

103 – 105

3

Helix

107 – 116

10

Helix

122 – 125

4

Helix

127 – 132

6

Turn

133 – 135

3

Helix

138 – 142

5

Sequences

	Sequence		Length	Mass (Da)
	P00701-1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: B1D03EDA0E85DED3	FASTA	147	16,278
	10 20 30 40 50 60 MRSLLVLVLC FLPLAALGKV YGRCELAAAM KRHGLDKYQG YSLGNWVCAA KFESNFNTQA 70 80 90 100 110 120 TNRNTDGSTD YGILQINSRW WCNDGRTPGS RNLCNIPCSA LLSSDITASV NCAKKIVSDV 130 140 HGMNAWVAWR NRCKGTDVNA WIRGCRL

References

[1]	"Evolutionary shift in the site of cleavage of prelysozyme." Weisman L.S., Krummel B.M., Wilson A.C. J. Biol. Chem. 261:2309-2313(1986) [PubMed: 3511061] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-18.
[2]	"The amino acid sequence of quail lysozyme." Kaneda M., Kato I., Tominaga N., Titani K., Narita K. J. Biochem. 66:747-749(1969) [PubMed: 5358633] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-147.
[3]	"Quail lysozyme II." Thammasirirak S., Preecharram S., Phonkham P., Daduang S., Araki T., Svasti J. Submitted (SEP-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 19-147, CATALYTIC ACTIVITY. Tissue: Egg white.
[4]	Houdusse A., Bentley G.A., Poljak R.J., Souchon H., Zhang Z. Submitted (JUN-1993) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 19-147.

Cross-references

Sequence databases

PIR

LZQJE. A91922.
JU0237.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IHL	X-ray	1.40	A	19-147	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P00701.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

PROSITE

PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P00701.

Entry information

Entry name

LYSC_COTJA

Accession

Primary (citable) accession number: P00701

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 15, 1998
Last modified:	November 25, 2008
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)