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P00702 (LYSC_PHACO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. 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
OrganismPhasianus colchicus colchicus (Ring-necked pheasant)
Taxonomic identifier9057 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaePhasianus

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.

Post-translational modification

By an evolutionary shift in the site of proteolytic cleavage of prelysozyme, Gly-18 became the N-terminal residue of the mature protein instead of being the C-terminal residue of the signal sequence as in other birds.

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.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   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

Signal peptide1 – 1717 Ref.2
Chain18 – 147130Lysozyme C
PRO_0000018499

Sites

Active site531
Active site701

Amino acid modifications

Disulfide bond24 ↔ 145
Disulfide bond48 ↔ 133
Disulfide bond82 ↔ 98
Disulfide bond94 ↔ 112

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00702 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 7A0EF8CCFD6B8249

FASTA14716,166
        10         20         30         40         50         60 
MRSLLILVLC FLPLAAPGKV YGRCELAAAM KRMGLDNYRG YSLGNWVCAA KFESNFNTGA 

        70         80         90        100        110        120 
TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCHIPCSA LLSSDITASV NCAKKIVSDG 

       130        140 
NGMNAWVAWR KHCKGTDVNV 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]"Amino acid sequence of pheasant lysozyme. Evolutionary change affecting processing of prelysozyme."
Jolles J., Ibrahimi I.M., Prager E.M., Schoentgen F., Jolles P., Wilson A.C.
Biochemistry 18:2744-2752(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-147.
[3]"Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex."
Chitarra V., Alzari P.M., Bentley G.A., Bhat T.N., Eisele J.L., Houdusse A., Lescar J., Souchon H., Poljak R.J.
Proc. Natl. Acad. Sci. U.S.A. 90:7711-7715(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]"Crystal structures of pheasant and guinea fowl egg-white lysozymes."
Lescar J., Souchon H., Alzari P.M.
Protein Sci. 3:788-798(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 121.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHLX-ray2.10A/B18-147[»]
1JHLX-ray2.40A19-147[»]
ProteinModelPortalP00702.
SMRP00702. Positions 18-147.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEP00702.

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

EvolutionaryTraceP00702.

Entry information

Entry nameLYSC_PHACO
AccessionPrimary (citable) accession number: P00702
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 83 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