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P00701

- LYSC_COTJA

UniProt

P00701 - LYSC_COTJA

Protein

Lysozyme C

Gene

LYZ

Organism
Coturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Status
Reviewed - Annotation score: 5 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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei53 – 531
    Active sitei70 – 701

    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
    OrganismiCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
    Taxonomic identifieri93934 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePerdicinaeCoturnix

    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 – 18182 PublicationsAdd
    BLAST
    Chaini19 – 147129Lysozyme CPRO_0000018496Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 145
    Disulfide bondi48 ↔ 133
    Disulfide bondi82 ↔ 98
    Disulfide bondi94 ↔ 112

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP00701.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 3210
    Helixi43 – 5412
    Beta strandi61 – 633
    Beta strandi69 – 713
    Turni72 – 754
    Turni78 – 803
    Helixi98 – 1025
    Beta strandi103 – 1053
    Helixi107 – 11610
    Helixi122 – 1254
    Helixi127 – 1326
    Turni133 – 1353
    Helixi138 – 1425

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IHLX-ray1.40A19-147[»]
    ProteinModelPortaliP00701.
    SMRiP00701. Positions 19-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00701.

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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.

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

    P00701-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSLLVLVLC FLPLAALGKV YGRCELAAAM KRHGLDKYQG YSLGNWVCAA    50
    KFESNFNTQA TNRNTDGSTD YGILQINSRW WCNDGRTPGS RNLCNIPCSA 100
    LLSSDITASV NCAKKIVSDV HGMNAWVAWR NRCKGTDVNA WIRGCRL 147
    Length:147
    Mass (Da):16,278
    Last modified:July 15, 1998 - v2
    Checksum:iB1D03EDA0E85DED3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391Q → LK AA sequence 1 PublicationCurated

    Sequence databases

    PIRiA91922. LZQJE.
    JU0237.

    Cross-referencesi

    Sequence databases

    PIRi A91922. LZQJE.
    JU0237.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IHL X-ray 1.40 A 19-147 [» ]
    ProteinModelPortali P00701.
    SMRi P00701. Positions 19-147.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PRIDEi P00701.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG052297.

    Miscellaneous databases

    EvolutionaryTracei P00701.

    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. "The amino acid sequence of quail lysozyme."
      Kaneda M., Kato I., Tominaga N., Titani K., Narita K.
      J. Biochem. 66:747-749(1969) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-147.
    3. "Quail lysozyme II."
      Thammasirirak S., Preecharram S., Phonkham P., Daduang S., Araki T., Svasti J.
      Submitted (SEP-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 19-147, CATALYTIC ACTIVITY.
      Tissue: Egg white.
    4. Houdusse A., Bentley G.A., Poljak R.J., Souchon H., Zhang Z.
      Submitted (JUN-1993) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 19-147.

    Entry informationi

    Entry nameiLYSC_COTJA
    AccessioniPrimary (citable) accession number: P00701
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 15, 1998
    Last modified: October 1, 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