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P00702

- LYSC_PHACO

UniProt

P00702 - LYSC_PHACO

Protein

Lysozyme C

Gene

LYZ

Organism
Phasianus colchicus colchicus (Ring-necked pheasant)
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.

    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
    OrganismiPhasianus colchicus colchicus (Ring-necked pheasant)
    Taxonomic identifieri9057 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaePhasianus

    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 – 17171 PublicationAdd
    BLAST
    Chaini18 – 147130Lysozyme CPRO_0000018499Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    By an evolutionary shift in the site of proteolytic cleavage of prelysozyme, Gly-18 became the N-terminal residue of the mature protein instead of being the C-terminal residue of the signal sequence as in other birds.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP00702.

    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 strandi55 – 573
    Beta strandi61 – 633
    Beta strandi69 – 713
    Turni72 – 754
    Turni78 – 803
    Beta strandi85 – 873
    Helixi98 – 1025
    Beta strandi103 – 1053
    Helixi107 – 11711
    Turni118 – 1214
    Helixi122 – 1254
    Helixi127 – 1326
    Turni133 – 1353
    Helixi138 – 1425

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GHLX-ray2.10A/B18-147[»]
    1JHLX-ray2.40A19-147[»]
    ProteinModelPortaliP00702.
    SMRiP00702. Positions 18-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00702.

    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.

    P00702-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSLLILVLC FLPLAAPGKV YGRCELAAAM KRMGLDNYRG YSLGNWVCAA    50
    KFESNFNTGA TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCHIPCSA 100
    LLSSDITASV NCAKKIVSDG NGMNAWVAWR KHCKGTDVNV WIRGCRL 147
    Length:147
    Mass (Da):16,166
    Last modified:June 1, 1994 - v2
    Checksum:i7A0EF8CCFD6B8249
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GHL X-ray 2.10 A/B 18-147 [» ]
    1JHL X-ray 2.40 A 19-147 [» ]
    ProteinModelPortali P00702.
    SMRi P00702. Positions 18-147.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PRIDEi P00702.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG052297.

    Miscellaneous databases

    EvolutionaryTracei P00702.

    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. "Amino acid sequence of pheasant lysozyme. Evolutionary change affecting processing of prelysozyme."
      Jolles J., Ibrahimi I.M., Prager E.M., Schoentgen F., Jolles P., Wilson A.C.
      Biochemistry 18:2744-2752(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-147.
    3. "Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex."
      Chitarra V., Alzari P.M., Bentley G.A., Bhat T.N., Eisele J.L., Houdusse A., Lescar J., Souchon H., Poljak R.J.
      Proc. Natl. Acad. Sci. U.S.A. 90:7711-7715(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    4. "Crystal structures of pheasant and guinea fowl egg-white lysozymes."
      Lescar J., Souchon H., Alzari P.M.
      Protein Sci. 3:788-798(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 121.

    Entry informationi

    Entry nameiLYSC_PHACO
    AccessioniPrimary (citable) accession number: P00702
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 84 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