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Q7LZQ1

- LYSC_PELSI

UniProt

Q7LZQ1 - LYSC_PELSI

Protein

Lysozyme C

Gene

LYZ

Organism
Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis)
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. Has strong bacteriolytic activity against M.luteus and V.cholerae, weak bacteriolytic activity against P.aeruginosa and no activity against A.hydrophila.1 PublicationPROSITE-ProRule annotation

    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

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius. Activity rapidly decreases within 30 minutes of incubation at 90 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei36 – 361PROSITE-ProRule annotation
    Active sitei54 – 541PROSITE-ProRule annotation

    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
    Softshell turtle lysozyme C
    Short name:
    SSTL
    Gene namesi
    Name:LYZ
    OrganismiPelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis)
    Taxonomic identifieri13735 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupTestudinesCryptodiraTrionychoideaTrionychidaePelodiscus

    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
    Chaini1 – 131131Lysozyme CPRO_0000208876Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi7 ↔ 129
    Disulfide bondi31 ↔ 117
    Disulfide bondi66 ↔ 82
    Disulfide bondi78 ↔ 96

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    Secondary structure

    1
    131
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1510
    Helixi21 – 233
    Helixi26 – 3712
    Beta strandi44 – 474
    Turni48 – 514
    Beta strandi52 – 554
    Turni56 – 594
    Turni62 – 654
    Helixi82 – 865
    Helixi91 – 10212
    Helixi106 – 1094
    Helixi111 – 1166
    Turni117 – 1193
    Helixi123 – 1253
    Turni126 – 1283

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GV0X-ray1.90A1-131[»]
    ProteinModelPortaliQ7LZQ1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7LZQ1.

    Family & Domainsi

    Sequence similaritiesi

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

    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.

    Q7LZQ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    GKIYEQCELA REFKRHGMDG YHGYSLGDWV CTAKHESNFN TAATNYNRGD    50
    QSTDYGILQI NSRWWCNDGK TPKAKNACGI ECSELLKADI TAAVNCAKRI 100
    VRDPNGMGAW VAWTKYCKGK DVSQWIKGCK L 131
    Length:131
    Mass (Da):14,732
    Last modified:September 22, 2009 - v3
    Checksum:iD59A7791775E6AA1
    GO

    Sequence databases

    PIRiJC5493.

    Cross-referencesi

    Sequence databases

    PIRi JC5493.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GV0 X-ray 1.90 A 1-131 [» ]
    ProteinModelPortali Q7LZQ1.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG052297.

    Miscellaneous databases

    EvolutionaryTracei Q7LZQ1.

    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. Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Egg white.
    2. "The 1.9 A X-ray structure of egg-white lysozyme from Taiwanese soft-shelled turtle (Trionyx Sinensis Wiegmann) exhibits structural differences from the standard chicken-type lysozyme."
      Siritapetawee J., Thammasirirak S., Robinson R.C., Yuvaniyama J.
      J. Biochem. 145:193-198(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
      Tissue: Egg white.

    Entry informationi

    Entry nameiLYSC_PELSI
    AccessioniPrimary (citable) accession number: Q7LZQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 53 of the entry and version 3 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