Reviewed, UniProtKB/Swiss-Prot Q7LZQ1 (LYSC_TRISI)

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

Trionyx sinensis (Chinese softshell turtle) (Pelodiscus sinensis)

Taxonomic identifier

13735 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Testudines › Cryptodira › Trionychoidea › Trionychidae › Pelodiscus

Protein attributes

Sequence length	131 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
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. Ref.2
Subunit structure	Monomer By similarity.
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.
biophysicochemical properties	pH dependence: Optimum pH is 6.0. Temperature dependence: Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
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
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 – 131

131

Lysozyme C

PRO_0000208876

Sites

Active site

36

1

By similarity

Active site

54

1

By similarity

Amino acid modifications

Disulfide bond

7 ↔ 129

Disulfide bond

31 ↔ 117

Disulfide bond

66 ↔ 82

Disulfide bond

78 ↔ 96

Experimental info

Sequence conflict

128

1

D → G AA sequence Ref.1

Secondary structure

1

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131

Helix Strand Turn

Details...

Helix

6 – 15

10

Helix

21 – 23

3

Helix

26 – 37

12

Beta strand

44 – 47

4

Turn

48 – 51

4

Beta strand

52 – 55

4

Turn

56 – 59

4

Turn

62 – 65

4

Helix

82 – 86

5

Helix

91 – 102

12

Helix

106 – 109

4

Helix

111 – 116

6

Turn

117 – 119

3

Helix

123 – 125

3

Turn

126 – 128

3

Sequences

	Sequence		Length	Mass (Da)
	Q7LZQ1-1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: D59A7793A75E6AA1	FASTA	131	14,790
	10 20 30 40 50 60 GKIYEQCELA REFKRHGMDG YHGYSLGDWV CTAKHESNFN TAATNYNRGD QSTDYGILQI 70 80 90 100 110 120 NSRWWCNDGK TPKAKNACGI ECSELLKADI TAAVNCAKRI VRDPNGMGAW VAWTKYCKGK 130 DVSQWIKDCK L

References

[1]	Araki T., Yamamoto T., Torikata T. Submitted (JUN-1997) to the PIR data bank Cited for: PROTEIN SEQUENCE.
[2]	"Complete amino acid sequence of three reptile lysozymes." Sompong T., Sakda D., Jisnuson S., Tomohiro A. Submitted (NOV-2007) to UniProtKB Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Egg white.
[3]	"The structure of the orthorhombic form of soft-shelled turtle lysozyme at 1.9 angstroms resolution." Siritapetawee J., Thammasirirak S., Yuvaniyama J., Robinson R.C. Submitted (MAY-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Cross-references

Sequence databases

PIR

JC5493.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GV0	X-ray	1.90	A	1-131	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Phylogenomic databases

HOVERGEN

Q7LZQ1.

Enzyme and pathway databases

BRENDA

3.2.1.17. 39406.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
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...

Entry information

Entry name

LYSC_TRISI

Accession

Primary (citable) accession number: Q7LZQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	January 15, 2008
Last modified:	June 16, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)