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UniProtKB/Swiss-Prot entry P00700


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

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Entry information
Entry name LYSC_COLVI
Primary accession number P00700
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 66)
Name and origin of the protein
Protein name Lysozyme C
Synonyms EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
Gene name
Name: LYZ
From
Colinus virginianus (Bobwhite quail) (Common bobwhite) [TaxID: 9014] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Odontophoridae; Colinus.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
TISSUE=Egg white;
PubMed=4112539 [NCBI, ExPASy, EBI, Israel, Japan]
Prager E.M., Arnheim N., Mross G.A., Wilson A.C.;
"Amino acid sequence studies on bobwhite quail egg white lysozyme.";
J. Biol. Chem. 247:2905-2916(1972).
[2]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1002/(SICI)1097-0134(199609)26:1<55::AID-PROT5>3.0.CO;2-F; PubMed=8880929 [NCBI, ExPASy, EBI, Israel, Japan]
Chacko S., Silverton E.W., Smith-Gill S.J., Davies D.R., Schick K.A., Xavier K.A., Willson R.C., Jeffrey P.D., Chang C.Y., Sieker L.C., Sheriff S.;
"Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment.";
Proteins 26:55-65(1996).
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 A00855; LZQJEB.
3D structure databases
PDB
1BQL; X-ray; 2.60 A; Y=1-129.[ExPASy / RCSB / EBI]
1DKJ; X-ray; 2.00 A; A=1-129.[ExPASy / RCSB / EBI]
1DKK; X-ray; 1.90 A; A/B=1-129.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BQL; -.
1DKJ; -.
1DKK; -.
ModBase P00700.
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 P00700.
ProtoNet P00700.
Phylogenomic databases
HOVERGEN P00700; -.
Other
BindingDB P00700; -.
LinkHub P00700; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing; Glycosidase; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   129  129     Lysozyme C. PRO_0000208863
ACT_SITE   35    35         
ACT_SITE   52    52         
DISULFID   6   127         
DISULFID   30   115         
DISULFID   64    80         
DISULFID   76    94         
HELIX   5    14  10      
HELIX   25    36  12      
STRAND   43    45  3      
STRAND   51    53  3      
TURN   54    57  4      
TURN   60    62  3      
HELIX   80    84  5      
STRAND   85    87  3      
HELIX   89   101  13      
HELIX   104   107  4      
HELIX   109   114  6      
TURN   115   117  3      
HELIX   120   124  5      
Sequence information
Length: 129 AA [This is the length of the unprocessed precursor] Molecular weight: 14271 Da [This is the MW of the unprocessed precursor] CRC64: 1C5797001951FF38 [This is a checksum on the sequence]
        10         20         30         40         50         60 
KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS TDYGVLQINS 

        70         80         90        100        110        120 
RWWCNDGKTP GSRNLCNIPC SALLSSDITA TVNCAKKIVS DGNGMNAWVA WRNRCKGTDV 


QAWIRGCRL 

P00700 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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