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P00703 (LYSC_MELGA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 103. 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
Gene names
Name:LYZ
OrganismMeleagris gallopavo (Common turkey) [Reference proteome]
Taxonomic identifier9103 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaeMeleagridinaeMeleagris

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2
Chain19 – 147129Lysozyme C
PRO_0000018497

Amino acid modifications

Disulfide bond24 ↔ 145 Ref.3
Disulfide bond48 ↔ 133 Ref.3
Disulfide bond82 ↔ 98 Ref.3
Disulfide bond94 ↔ 112 Ref.3

Secondary structure

.............................. 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00703 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 77C54CD70834583F

FASTA14716,135
        10         20         30         40         50         60 
MRSLLILVLC FLPLAALGKV YGRCELAAAM KRLGLDNYRG YSLGNWVCAA KFESNFNTHA 

        70         80         90        100        110        120 
TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCNIPCSA LLSSDITASV NCAKKIASGG 

       130        140 
NGMNAWVAWR NRCKGTDVHA WIRGCRL 

« Hide

References

[1]"Evolutionary shift in the site of cleavage of prelysozyme."
Weisman L.S., Krummel B.M., Wilson A.C.
J. Biol. Chem. 261:2309-2313(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-18.
[2]"Turkey egg white lysozyme. Preparation of the crystalline enzyme and investigation of the amino acid sequence."
Larue J.N., Speck J.C. Jr.
J. Biol. Chem. 245:1985-1991(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-147.
Tissue: Egg white.
[3]"Crystallographic study of turkey egg-white lysozyme and its complex with a disaccharide."
Sarma R., Bott R.
J. Mol. Biol. 113:555-565(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS.
[4]"Structure determination of turkey egg-white lysozyme using Laue diffraction data."
Howell P.L., Almo S.C., Parsons M., Petsko G.A., Hajdu J.
Acta Crystallogr. B 48:200-207(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Structure of hexagonal turkey egg-white lysozyme at 1.65-A resolution."
Howell P.L.
Acta Crystallogr. D 51:654-662(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[6]"1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme."
Bartik K., Dobson C.M., Redfield C.
Eur. J. Biochem. 215:255-266(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRLZTK. C92574.
RefSeqXP_003202118.1. XM_003202070.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
135LX-ray1.30A19-147[»]
1DZBX-ray2.00X/Y19-147[»]
1JEFX-ray1.77A19-147[»]
1JSEX-ray1.12A19-147[»]
1JTPX-ray1.90L/M19-147[»]
1LJNX-ray1.19A19-147[»]
1LZ2X-ray2.80A19-147[»]
1LZYX-ray1.55A19-147[»]
1TEWX-ray1.65A19-147[»]
1UACX-ray1.70Y19-147[»]
1XFTX-ray3.35A19-147[»]
2LZ2X-ray2.20A19-147[»]
3LZ2X-ray2.50A19-147[»]
DisProtDP00259.
ProteinModelPortalP00703.
SMRP00703. Positions 19-147.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMGAT00000011853; ENSMGAP00000010985; ENSMGAG00000010559.
GeneID100547044.
KEGGmgp:100547044.

Organism-specific databases

CTD4069.

Phylogenomic databases

GeneTreeENSGT00550000074398.
HOVERGENHBG052297.
KOK13915.
OMAIACAKYI.
OrthoDBEOG7BW0M5.
TreeFamTF324882.

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

EvolutionaryTraceP00703.

Entry information

Entry nameLYSC_MELGA
AccessionPrimary (citable) accession number: P00703
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: February 19, 2014
This is version 103 of the entry and version 2 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