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P00703

- LYSC_MELGA

UniProt

P00703 - LYSC_MELGA

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Protein
Lysozyme C
Gene
LYZ
Organism
Meleagris gallopavo (Common turkey)
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.

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
OrganismiMeleagris gallopavo (Common turkey)
Taxonomic identifieri9103 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaeMeleagridinaeMeleagris
ProteomesiUP000001645: Chromosome 1

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
Signal peptidei1 – 18181 Publication
Add
BLAST
Chaini19 – 147129Lysozyme C
PRO_0000018497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 1451 Publication
Disulfide bondi48 ↔ 1331 Publication
Disulfide bondi82 ↔ 981 Publication
Disulfide bondi94 ↔ 1121 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3210
Helixi38 – 403
Helixi43 – 5412
Beta strandi55 – 595
Beta strandi61 – 633
Beta strandi69 – 713
Turni72 – 754
Turni78 – 814
Beta strandi85 – 873
Helixi98 – 1025
Beta strandi103 – 1053
Helixi107 – 11711
Beta strandi119 – 1213
Helixi122 – 1254
Helixi127 – 1326
Turni133 – 1353
Helixi138 – 1425

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
135LX-ray1.30A19-147[»]
1DZBX-ray2.00X/Y19-147[»]
1JEFX-ray1.77A19-147[»]
1JSEX-ray1.12A19-147[»]
1JTPX-ray1.90L/M19-147[»]
1LJNX-ray1.19A19-147[»]
1LZ2X-ray2.80A19-147[»]
1LZYX-ray1.55A19-147[»]
1TEWX-ray1.65A19-147[»]
1UACX-ray1.70Y19-147[»]
1XFTX-ray3.35A19-147[»]
2LZ2X-ray2.20A19-147[»]
3LZ2X-ray2.50A19-147[»]
DisProtiDP00259.
ProteinModelPortaliP00703.
SMRiP00703. Positions 19-147.

Miscellaneous databases

EvolutionaryTraceiP00703.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00550000074398.
HOVERGENiHBG052297.
KOiK13915.
OMAiGNGMNAW.
OrthoDBiEOG7BW0M5.
TreeFamiTF324882.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00703-1 [UniParc]FASTAAdd to Basket

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MRSLLILVLC FLPLAALGKV YGRCELAAAM KRLGLDNYRG YSLGNWVCAA    50
KFESNFNTHA TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCNIPCSA 100
LLSSDITASV NCAKKIASGG NGMNAWVAWR NRCKGTDVHA WIRGCRL 147
Length:147
Mass (Da):16,135
Last modified:April 1, 1990 - v2
Checksum:i77C54CD70834583F
GO

Sequence databases

PIRiC92574. LZTK.
RefSeqiXP_003202118.1. XM_003202070.1.

Genome annotation databases

EnsembliENSMGAT00000011853; ENSMGAP00000010985; ENSMGAG00000010559.
GeneIDi100547044.
KEGGimgp:100547044.

Cross-referencesi

Sequence databases

PIRi C92574. LZTK.
RefSeqi XP_003202118.1. XM_003202070.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
135L X-ray 1.30 A 19-147 [» ]
1DZB X-ray 2.00 X/Y 19-147 [» ]
1JEF X-ray 1.77 A 19-147 [» ]
1JSE X-ray 1.12 A 19-147 [» ]
1JTP X-ray 1.90 L/M 19-147 [» ]
1LJN X-ray 1.19 A 19-147 [» ]
1LZ2 X-ray 2.80 A 19-147 [» ]
1LZY X-ray 1.55 A 19-147 [» ]
1TEW X-ray 1.65 A 19-147 [» ]
1UAC X-ray 1.70 Y 19-147 [» ]
1XFT X-ray 3.35 A 19-147 [» ]
2LZ2 X-ray 2.20 A 19-147 [» ]
3LZ2 X-ray 2.50 A 19-147 [» ]
DisProti DP00259.
ProteinModelPortali P00703.
SMRi P00703. Positions 19-147.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMGAT00000011853 ; ENSMGAP00000010985 ; ENSMGAG00000010559 .
GeneIDi 100547044.
KEGGi mgp:100547044.

Organism-specific databases

CTDi 4069.

Phylogenomic databases

GeneTreei ENSGT00550000074398.
HOVERGENi HBG052297.
KOi K13915.
OMAi GNGMNAW.
OrthoDBi EOG7BW0M5.
TreeFami TF324882.

Miscellaneous databases

EvolutionaryTracei P00703.

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. "Evolutionary shift in the site of cleavage of prelysozyme."
    Weisman L.S., Krummel B.M., Wilson A.C.
    J. Biol. Chem. 261:2309-2313(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18.
  2. "Turkey egg white lysozyme. Preparation of the crystalline enzyme and investigation of the amino acid sequence."
    Larue J.N., Speck J.C. Jr.
    J. Biol. Chem. 245:1985-1991(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-147.
    Tissue: Egg white.
  3. "Crystallographic study of turkey egg-white lysozyme and its complex with a disaccharide."
    Sarma R., Bott R.
    J. Mol. Biol. 113:555-565(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS.
  4. "Structure determination of turkey egg-white lysozyme using Laue diffraction data."
    Howell P.L., Almo S.C., Parsons M., Petsko G.A., Hajdu J.
    Acta Crystallogr. B 48:200-207(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  5. "Structure of hexagonal turkey egg-white lysozyme at 1.65-A resolution."
    Howell P.L.
    Acta Crystallogr. D 51:654-662(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  6. "1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme."
    Bartik K., Dobson C.M., Redfield C.
    Eur. J. Biochem. 215:255-266(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiLYSC_MELGA
AccessioniPrimary (citable) accession number: P00703
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: May 14, 2014
This is version 104 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, Complete proteome, Direct protein sequencing, Reference proteome

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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