ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P00701


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LYSC_COTJA
Primary accession number P00701
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 69)
Name and origin of the protein
Protein name Lysozyme C [Precursor]
Synonyms EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
Gene name
Name: LYZ
From
Coturnix coturnix japonica (Japanese quail) [TaxID: 93934] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Perdicinae; Coturnix.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE OF 1-18.
PubMed=3511061 [NCBI, ExPASy, EBI, Israel, Japan]
Weisman L.S., Krummel B.M., Wilson A.C.;
"Evolutionary shift in the site of cleavage of prelysozyme.";
J. Biol. Chem. 261:2309-2313(1986).
[2]
PROTEIN SEQUENCE OF 19-147.
PubMed=5358633 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneda M., Kato I., Tominaga N., Titani K., Narita K.;
"The amino acid sequence of quail lysozyme.";
J. Biochem. 66:747-749(1969).
[3]
PROTEIN SEQUENCE OF 19-147, AND CATALYTIC ACTIVITY.
TISSUE=Egg white;
Thammasirirak S., Preecharram S., Phonkham P., Daduang S., Araki T., Svasti J.;
"Quail lysozyme II.";
Submitted (SEP-2006) to UniProtKB.
[4]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 19-147.
Houdusse A., Bentley G.A., Poljak R.J., Souchon H., Zhang Z.;
Submitted (JUN-1993) to the PDB data bank.
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: Monomer.
  • 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.
  • SIMILARITY: Belongs to the glycosyl hydrolase 22 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR A91922; LZQJE.
JU0237; JU0237.
3D structure databases
PDB
2IHL; X-ray; 1.40 A; A=19-147.[ExPASy / RCSB / EBI]
PDBsum 2IHL; -.
ModBase P00701.
Ontologies
GO
GO:0019835; Biological process: cytolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0042742; Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001916; Glyco_hydro_22.
IPR000974; Glyco_hydro_22_lys.
Graphical view of domain structure.
Pfam PF00062; Lys; 1.
Pfam graphical view of domain structure.
PRINTS PR00137; LYSOZYME.
PR00135; LYZLACT.
SMART SM00263; LYZ1; 1.
SMART graphical view of domain structure.
PROSITE PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00701.
ProtoNet P00701.
Phylogenomic databases
HOVERGEN P00701; -.
Other
LinkHub P00701; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing; Glycosidase; Hydrolase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   147  129     Lysozyme C. PRO_0000018496
ACT_SITE   53    53         
ACT_SITE   70    70         
DISULFID   24   145         
DISULFID   48   133         
DISULFID   82    98         
DISULFID   94   112         
CONFLICT   39    39        Q -> LK (in Ref. 3; AA sequence). 
HELIX   23    32  10      
HELIX   43    54  12      
STRAND   61    63  3      
STRAND   69    71  3      
TURN   72    75  4      
TURN   78    80  3      
HELIX   98   102  5      
STRAND   103   105  3      
HELIX   107   116  10      
HELIX   122   125  4      
HELIX   127   132  6      
TURN   133   135  3      
HELIX   138   142  5      
Sequence information
Length: 147 AA [This is the length of the unprocessed precursor] Molecular weight: 16278 Da [This is the MW of the unprocessed precursor] CRC64: B1D03EDA0E85DED3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRSLLVLVLC FLPLAALGKV YGRCELAAAM KRHGLDKYQG YSLGNWVCAA KFESNFNTQA 

        70         80         90        100        110        120 
TNRNTDGSTD YGILQINSRW WCNDGRTPGS RNLCNIPCSA LLSSDITASV NCAKKIVSDV 

       130        140 
HGMNAWVAWR NRCKGTDVNA WIRGCRL 

P00701 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!