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P00703

- LYSC_MELGA

UniProt

P00703 - LYSC_MELGA

Protein

Lysozyme C

Gene

LYZ

Organism
Meleagris gallopavo (Common turkey)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 147129Lysozyme CPRO_0000018497Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 1451 PublicationPROSITE-ProRule annotation
    Disulfide bondi48 ↔ 1331 PublicationPROSITE-ProRule annotation
    Disulfide bondi82 ↔ 981 PublicationPROSITE-ProRule annotation
    Disulfide bondi94 ↔ 1121 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    147
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00703.

    Family & Domainsi

    Sequence similaritiesi

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

    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

    « Hide

    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: October 1, 2014
    This is version 105 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