P00702 (LYSC_PHACO) Reviewed, UniProtKB/Swiss-Prot

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

Phasianus colchicus colchicus (Ring-necked pheasant)

Taxonomic identifier

9057 [NCBI]

Taxonomic lineage

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

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.
Subcellular location	Secreted.
Post-translational modification	By an evolutionary shift in the site of proteolytic cleavage of prelysozyme, Gly-18 became the N-terminal residue of the mature protein instead of being the C-terminal residue of the signal sequence as in other birds.
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
Cellular component	Secreted
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule 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: UniProtKB-SubCell
Molecular function	lysozyme activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.2

Chain

18 – 147

130

Lysozyme C

PRO_0000018499

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

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 – 80

3

Beta strand

85 – 87

3

Helix

98 – 102

5

Beta strand

103 – 105

3

Helix

107 – 117

11

Turn

118 – 121

4

Helix

122 – 125

4

Helix

127 – 132

6

Turn

133 – 135

3

Helix

138 – 142

5

Sequences

	Sequence		Length	Mass (Da)
	P00702 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 7A0EF8CCFD6B8249	FASTA	147	16,166
	10 20 30 40 50 60 MRSLLILVLC FLPLAAPGKV YGRCELAAAM KRMGLDNYRG YSLGNWVCAA KFESNFNTGA 70 80 90 100 110 120 TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCHIPCSA LLSSDITASV NCAKKIVSDG 130 140 NGMNAWVAWR KHCKGTDVNV 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]	"Amino acid sequence of pheasant lysozyme. Evolutionary change affecting processing of prelysozyme." Jolles J., Ibrahimi I.M., Prager E.M., Schoentgen F., Jolles P., Wilson A.C. Biochemistry 18:2744-2752(1979) [PubMed: 476049] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-147.
[3]	"Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex." Chitarra V., Alzari P.M., Bentley G.A., Bhat T.N., Eisele J.L., Houdusse A., Lescar J., Souchon H., Poljak R.J. Proc. Natl. Acad. Sci. U.S.A. 90:7711-7715(1993) [PubMed: 8356074] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]	"Crystal structures of pheasant and guinea fowl egg-white lysozymes." Lescar J., Souchon H., Alzari P.M. Protein Sci. 3:788-798(1994) [PubMed: 8061608] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 121.
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GHL	X-ray	2.10	A/B	18-147	[»]
1JHL	X-ray	2.40	A	19-147	[»]

ProteinModelPortal

P00702.

SMR

P00702. Positions 18-147.

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG052297.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

SUPFAM

SSF53955. SSF53955. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

LYSC_PHACO

Accession

Primary (citable) accession number: P00702

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 1, 1994
Last modified:	April 5, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program