Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7LZQ1 (LYSC_PELSI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Softshell turtle lysozyme C
Short name=SSTL
Gene names
Name:LYZ
OrganismPelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis)
Taxonomic identifier13735 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupTestudinesCryptodiraTrionychoideaTrionychidaePelodiscus

Protein attributes

Sequence length131 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

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.

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. Activity rapidly decreases within 30 minutes of incubation at 90 degrees Celsius.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct 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 – 131131Lysozyme C
PRO_0000208876

Sites

Active site361 By similarity
Active site541 By similarity

Amino acid modifications

Disulfide bond7 ↔ 129
Disulfide bond31 ↔ 117
Disulfide bond66 ↔ 82
Disulfide bond78 ↔ 96

Secondary structure

.......................... 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7LZQ1 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: D59A7791775E6AA1

FASTA13114,732
        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 
DVSQWIKGCK L 

« 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.
[2]"The 1.9 A X-ray structure of egg-white lysozyme from Taiwanese soft-shelled turtle (Trionyx Sinensis Wiegmann) exhibits structural differences from the standard chicken-type lysozyme."
Siritapetawee J., Thammasirirak S., Robinson R.C., Yuvaniyama J.
J. Biochem. 145:193-198(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Tissue: Egg white.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRJC5493.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GV0X-ray1.90A1-131[»]
ProteinModelPortalQ7LZQ1.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

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...

Other

EvolutionaryTraceQ7LZQ1.

Entry information

Entry nameLYSC_PELSI
AccessionPrimary (citable) accession number: Q7LZQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: September 22, 2009
Last modified: January 22, 2014
This is version 52 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries