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P85345 (LYSC_AMYCA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismAmyda cartilaginea (Asiatic softshell turtle)
Taxonomic identifier161655 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupTestudinesCryptodiraTrionychoideaTrionychidaeAmyda

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Protein existenceEvidence 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 degrees Celsius.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcell 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_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 130130Lysozyme C
PRO_0000315890

Sites

Active site351 By similarity UniProtKB P00702
Active site531 By similarity UniProtKB P00702

Amino acid modifications

Disulfide bond6 ↔ 128 By similarity UniProtKB P00702
Disulfide bond30 ↔ 116 By similarity UniProtKB P00702
Disulfide bond65 ↔ 81 By similarity UniProtKB P00702
Disulfide bond77 ↔ 95 By similarity UniProtKB P00702

Sequences

Sequence LengthMass (Da)Tools
P85345 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: F6760A314D34FF91

FASTA13014,543
        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 

« Hide

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

ProteinModelPortalP85345.
SMRP85345. Positions 1-130.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052297.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC_AMYCA
AccessionPrimary (citable) accession number: P85345
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: March 19, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries