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P00700

- LYSC_COLVI

UniProt

P00700 - LYSC_COLVI

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Protein

Lysozyme C

Gene
LYZ
Organism
Colinus virginianus (Northern bobwhite) (Tetrao virginianus)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351
Active sitei52 – 521

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

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
OrganismiColinus virginianus (Northern bobwhite) (Tetrao virginianus)
Taxonomic identifieri9014 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesOdontophoridaeColinus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Lysozyme CPRO_0000208863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 1271 Publication
Disulfide bondi30 ↔ 1151 Publication
Disulfide bondi64 ↔ 801 Publication
Disulfide bondi76 ↔ 941 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00700.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410
Helixi25 – 3612
Beta strandi43 – 453
Beta strandi51 – 533
Turni54 – 574
Turni60 – 634
Helixi80 – 845
Beta strandi85 – 873
Helixi89 – 9911
Beta strandi101 – 1033
Helixi104 – 1074
Helixi109 – 1146
Turni115 – 1173
Helixi120 – 1245

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQLX-ray2.60Y1-129[»]
1DKJX-ray2.00A1-129[»]
1DKKX-ray1.90A/B1-129[»]
ProteinModelPortaliP00700.
SMRiP00700. Positions 1-129.

Miscellaneous databases

EvolutionaryTraceiP00700.

Family & Domainsi

Sequence similaritiesi

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.
[Graphical view]
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.

P00700-1 [UniParc]FASTAAdd to Basket

« Hide

KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS    50
TDYGVLQINS RWWCNDGKTP GSRNLCNIPC SALLSSDITA TVNCAKKIVS 100
DGNGMNAWVA WRNRCKGTDV QAWIRGCRL 129
Length:129
Mass (Da):14,271
Last modified:November 1, 1997 - v2
Checksum:i1C5797001951FF38
GO

Sequence databases

PIRiA00855. LZQJEB.

Cross-referencesi

Sequence databases

PIRi A00855. LZQJEB.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BQL X-ray 2.60 Y 1-129 [» ]
1DKJ X-ray 2.00 A 1-129 [» ]
1DKK X-ray 1.90 A/B 1-129 [» ]
ProteinModelPortali P00700.
SMRi P00700. Positions 1-129.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEi P00700.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052297.

Miscellaneous databases

EvolutionaryTracei P00700.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Amino acid sequence studies on bobwhite quail egg white lysozyme."
    Prager E.M., Arnheim N., Mross G.A., Wilson A.C.
    J. Biol. Chem. 247:2905-2916(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Egg white.
  2. "Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment."
    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.
    Proteins 26:55-65(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiLYSC_COLVI
AccessioniPrimary (citable) accession number: P00700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 87 of the entry and version 2 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

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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