Reviewed, UniProtKB/Swiss-Prot P00703 (LYSC_MELGA)

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

Meleagris gallopavo (Common turkey)

Taxonomic identifier

9103 [NCBI]

Taxonomic lineage

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

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)
None. [Check GOA]

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 18

18

Chain

19 – 147

129

Lysozyme C

Amino acid modifications

Disulfide bond

24 ↔ 145

Disulfide bond

48 ↔ 133

Disulfide bond

82 ↔ 98

Disulfide bond

94 ↔ 112

Secondary structure

1

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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 – 81

4

Beta strand

85 – 87

3

Helix

98 – 102

5

Helix

107 – 117

11

Helix

122 – 125

4

Helix

127 – 132

6

Turn

133 – 135

3

Helix

138 – 142

5

Sequences

	Sequence		Length	Mass (Da)
	P00703-1 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: 77C54CD70834583F	FASTA	147	16,135
	10 20 30 40 50 60 MRSLLILVLC FLPLAALGKV YGRCELAAAM KRLGLDNYRG YSLGNWVCAA KFESNFNTHA 70 80 90 100 110 120 TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCNIPCSA LLSSDITASV NCAKKIASGG 130 140 NGMNAWVAWR NRCKGTDVHA 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]	"Turkey egg white lysozyme. Preparation of the crystalline enzyme and investigation of the amino acid sequence." Larue J.N., Speck J.C. Jr. J. Biol. Chem. 245:1985-1991(1970) [PubMed: 5440837] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-147. Tissue: Egg white.
[3]	"Crystallographic study of turkey egg-white lysozyme and its complex with a disaccharide." Sarma R., Bott R. J. Mol. Biol. 113:555-565(1977) [PubMed: 886621] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS.
[4]	"Structure determination of turkey egg-white lysozyme using Laue diffraction data." Howell P.L., Almo S.C., Parsons M., Petsko G.A., Hajdu J. Acta Crystallogr. B 48:200-207(1992) [PubMed: 1515108] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]	"Structure of hexagonal turkey egg-white lysozyme at 1.65-A resolution." Howell P.L. Acta Crystallogr. D 51:654-662(1995) [PubMed: 15299795] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[6]	"1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme." Bartik K., Dobson C.M., Redfield C. Eur. J. Biochem. 215:255-266(1993) [PubMed: 8344294] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

PIR

LZTK. C92574.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
135L	X-ray	1.30	A	19-147	[»]
1DZB	X-ray	2.00	X/Y	19-147	[»]
1JEF	X-ray	1.77	A	19-147	[»]
1JSE	X-ray	1.12	A	19-147	[»]
1JTP	X-ray	1.90	L/M	19-147	[»]
1LJN	X-ray	1.19	A	19-147	[»]
1LZ2	X-ray	2.80	A	19-147	[»]
1LZY	X-ray	1.55	A	19-147	[»]
1TEW	X-ray	1.65	A	19-147	[»]
1UAC	X-ray	1.70	Y	19-147	[»]
1XFT	X-ray	3.35	A	19-147	[»]
2LZ2	X-ray	2.20	A	19-147	[»]
3LZ2	X-ray	2.50	A	19-147	[»]

DisProt

DP00259.

ModBase

Search...

Phylogenomic databases

HOVERGEN

P00703.

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]

ProDom

P00703.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

BindingDB

P00703.

LinkHub

P00703.

ProtoNet

Search...

Entry information

Entry name

LYSC_MELGA

Accession

Primary (citable) accession number: P00703

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	July 22, 2008
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)