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Protein

Lysozyme C

Gene

LYZ

Organism
Columba livia (Rock dove)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351PROSITE-ProRule annotation
Active sitei52 – 521PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi81 – 9212PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
OrganismiColumba livia (Rock dove)
Taxonomic identifieri8932 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeColumbiformesColumbidaeColumba

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Lysozyme CPRO_0000208862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 127PROSITE-ProRule annotation
Disulfide bondi30 ↔ 115PROSITE-ProRule annotation
Disulfide bondi64 ↔ 80PROSITE-ProRule annotation
Disulfide bondi76 ↔ 94PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP00708.
SMRiP00708. Positions 1-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00708-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KDIPRCELVK ILRRHGFEGF VGKTVANWVC LVKHESGYRT TAFNNNGPNS
60 70 80 90 100
RDYGIFQINS KYWCNDGKTR GSKNACNINC SKLRDDNIAD DIQCAKKIAR
110 120
EARGLTPWVA WKKYCQGKDL SSYVRGC
Length:127
Mass (Da):14,452
Last modified:July 21, 1986 - v1
Checksum:i96D3BAFDFD934DD8
GO

Sequence databases

PIRiA00863. LZPY.

Cross-referencesi

Sequence databases

PIRiA00863. LZPY.

3D structure databases

ProteinModelPortaliP00708.
SMRiP00708. Positions 1-124.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amino acid sequence of pigeon egg-white lysozyme."
    Rodriguez R., Menendez-Arias L., Gonzalez de Buitrago G., Gavilanes J.G.
    Biochem. Int. 11:841-843(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Egg white.
  2. "Calcium-binding lysozymes."
    Nitta K., Tsuge H., Shimazaki K., Sugai S.
    Biol. Chem. Hoppe-Seyler 369:671-675(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.
  3. "Crystallization and preliminary X-ray structure analysis of pigeon egg-white lysozyme."
    Yao M., Tanaka I., Hikichi K., Nitta K.
    J. Biochem. 111:1-3(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiLYSC_COLLI
AccessioniPrimary (citable) accession number: P00708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 1, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.