P85345 (LYSC_AMYCA) 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
Asiatic softshell turtle lysozyme C
Short name=ASTL

Gene names

Name:

LYZ

Organism

Amyda cartilaginea (Asiatic softshell turtle)

Taxonomic identifier

161655 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Testudines › Cryptodira › Trionychoidea › Trionychidae › Amyda

Protein attributes

Sequence length	130 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. Has strong bacteriolytic activity against M.luteus and V.cholerae, weak bacteriolytic activity against P.aeruginosa and no activity against A.hydrophila. Ref.1 UniProtKB P00702
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.1
Subunit structure	Monomer By similarity. UniProtKB P00702
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.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0. Ref.1 Temperature dependence: Optimum temperature is 40 degrees Celsius. Retains the bulk of its activity after incubation for 1 hour at 90 egrees Celsius. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	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 – 130	130	Lysozyme C		PRO_0000315890
Sites
	Active site	35	1	By similarity UniProtKB P00702
	Active site	53	1	By similarity UniProtKB P00702
Amino acid modifications
	Disulfide bond	6 ↔ 128		By similarity UniProtKB P00702
	Disulfide bond	30 ↔ 116		By similarity UniProtKB P00702
	Disulfide bond	65 ↔ 81		By similarity UniProtKB P00702
	Disulfide bond	77 ↔ 95		By similarity UniProtKB P00702

Sequences

	Sequence		Length	Mass (Da)
	P85345 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: F6760A314D34FF91	FASTA	130	14,543
	10 20 30 40 50 60 KIYEQCEAAR EMKRLGLDGY DGYSLGDWVC TAKHESNFNT GATNYNRGDQ STDYGIFQIN 70 80 90 100 110 120 SRWWCNDGKT PNAKNACGIE CSELLKADIT AAVICAKRVV RDPNGMGAWV AWTKYCKGKD 130 VSQWIKGCKL

References

[1]

"Purification, characterization and comparison of reptile lysozymes." Thammasirirak S., Ponkham P., Preecharram S., Khanchanuan R., Phonyothee P., Daduang S., Srisomsap C., Araki T., Svasti J. Comp. Biochem. Physiol. 143:209-217(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Egg white.

Cross-references

3D structure databases
ProteinModelPortal	P85345.
SMR	P85345. Positions 1-130.
ModBase	Search...
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_AMYCA

Accession

Primary (citable) accession number: P85345

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	April 5, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program