P00700 (LYSC_COLVI) 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

Colinus virginianus (Bobwhite quail) (Tetrao virginianus)

Taxonomic identifier

9014 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Odontophoridae › Colinus

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
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.
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
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

Chain

1 – 129

129

Lysozyme C

PRO_0000208863

Sites

Active site

35

1

Active site

52

1

Amino acid modifications

Disulfide bond

6 ↔ 127

Ref.1

Disulfide bond

30 ↔ 115

Ref.1

Disulfide bond

64 ↔ 80

Ref.1

Disulfide bond

76 ↔ 94

Ref.1

Secondary structure

1

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129

Helix Strand Turn

Details...

Helix

5 – 14

10

Helix

25 – 36

12

Beta strand

43 – 45

3

Beta strand

51 – 53

3

Turn

54 – 57

4

Turn

60 – 63

4

Helix

80 – 84

5

Beta strand

85 – 87

3

Helix

89 – 99

11

Beta strand

101 – 103

3

Helix

104 – 107

4

Helix

109 – 114

6

Turn

115 – 117

3

Helix

120 – 124

5

Sequences

	Sequence		Length	Mass (Da)
	P00700 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 1C5797001951FF38	FASTA	129	14,271
	10 20 30 40 50 60 KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS TDYGVLQINS 70 80 90 100 110 120 RWWCNDGKTP GSRNLCNIPC SALLSSDITA TVNCAKKIVS DGNGMNAWVA WRNRCKGTDV QAWIRGCRL

References

[1]	"Amino acid sequence studies on bobwhite quail egg white lysozyme." Prager E.M., Arnheim N., Mross G.A., Wilson A.C. J. Biol. Chem. 247:2905-2916(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Egg white.
[2]	"Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment." Chacko S., Silverton E.W., Smith-Gill S.J., Davies D.R., Schick K.A., Xavier K.A., Willson R.C., Jeffrey P.D., Chang C.Y., Sieker L.C., Sheriff S. Proteins 26:55-65(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

PIR

LZQJEB. A00855.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BQL	X-ray	2.60	Y	1-129	[»]
1DKJ	X-ray	2.00	A	1-129	[»]
1DKK	X-ray	1.90	A/B	1-129	[»]

ProteinModelPortal

P00700.

SMR

P00700. Positions 1-129.

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDE

P00700.

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...

Other

EvolutionaryTrace

P00700.

Entry information

Entry name

LYSC_COLVI

Accession

Primary (citable) accession number: P00700

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program