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P37156 (LYSC1_TACAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lysozyme C I
EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismTachyglossus aculeatus aculeatus (Australian echidna)
Taxonomic identifier49271 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Monotremata › Tachyglossidae › Tachyglossus ›

Protein attributes

Sequence length125 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.

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

Chain1 – 125125Lysozyme C I
PRO_0000208857

Sites

Active site351
Active site521

Amino acid modifications

Disulfide bond9 ↔ 125
Disulfide bond30 ↔ 115
Disulfide bond64 ↔ 80
Disulfide bond76 ↔ 94

Secondary structure

1 ...................... 125
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37156 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 18D8A1DBA3724073

FASTA12513,994
        10         20         30         40         50         60 
KILKKQELCK NLVAQGMNGY QHITLPNWVC TAFHESSYNT RATNHNTDGS TDYGILQINS 

        70         80         90        100        110        120 
RYWCHDGKTP GSKNACNISC SKLLDDDITD DLKCAKKIAG EAKGLTPWVA WKSKCRGHDL 


SKFKC

« Hide

References

[1]"The isolation and amino acid sequences of echidna (Tachyglossus aculeatus) milk lysozyme I and II."
Teahan C.G., McKenzie H.A., Shaw D.C., Griffiths M.
Biochem. Int. 24:85-95(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Milk.
[2]"Structure of the calcium-binding Echidna milk lysozyme at 1.9-A resolution."
Guss J.M., Messer M., Costello M., Hardy K., Kumar V.
Acta Crystallogr. D 53:355-363(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[3]Erratum
Guss J.M., Messer M., Costello M., Hardy K., Kumar V.
Acta Crystallogr. D 53:805-805(1997)

Cross-references

Sequence databases

PIRA45660.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JUGX-ray1.90A1-125[»]
ProteinModelPortalP37156.
SMRP37156. Positions 1-125.
ModBaseSearch...

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

EvolutionaryTraceP37156.

Entry information

Entry nameLYSC1_TACAC
AccessionPrimary (citable) accession number: P37156
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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