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P85045

- LYS_BUFGA

UniProt

P85045 - LYS_BUFGA

Protein

Lysozyme C

Gene
N/A
Organism
Bufo gargarizans andrewsi (Andrew's toad) (Bufo andrewsi)
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 antibacterial activity against the Gram-positive bacterium S.aureus and against the Gram-negative bacterium E.coli with a MIC of 1 µM and 8 µM respectively. No antifungal activity against C.albicans.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

    Stable from 20 degrees Celsius to 70 degrees Celsius. Activity decreases sharply above 70 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei51 – 511By similarityPROSITE-ProRule annotation
    Active sitei69 – 691By similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. cytolysis Source: UniProtKB-KW
    3. defense response to Gram-negative bacterium Source: UniProtKB
    4. defense response to Gram-positive bacterium Source: UniProtKB

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme C (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    OrganismiBufo gargarizans andrewsi (Andrew's toad) (Bufo andrewsi)
    Taxonomic identifieri61428 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaBufonidaeBufo

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 16›161 PublicationAdd
    BLAST
    Chaini17 – 146130Lysozyme C1 PublicationPRO_0000271190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi22 ↔ 144By similarityPROSITE-ProRule annotation
    Disulfide bondi46 ↔ 132By similarityPROSITE-ProRule annotation
    Disulfide bondi81 ↔ 97By similarityPROSITE-ProRule annotation
    Disulfide bondi93 ↔ 111By similarityPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP85045.

    Expressioni

    Tissue specificityi

    Expressed by the skin glands.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP85045.
    SMRiP85045. Positions 19-146.
    ModBaseiSearch...
    MobiDBiSearch...

    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: Fragment.

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

    P85045-1 [UniParc]FASTAAdd to Basket

    « Hide

    SGKYISWEDS CSYLQLQKYE RCELAKALKK GGLADFKGYS LENWICTAFH    50
    ESGYNTASTN YNPPDKSTDY GIFQINSRWW CNDYKTPRSK NTCNIDCKVL 100
    LGDDISPAIK CAKRVVSDPN GMGAWVAWKK YCKGKNLSQW TQGCKL 146
    Length:146
    Mass (Da):16,608
    Last modified:January 9, 2007 - v1
    Checksum:i126AA86ED3D01EBB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 111 Publication

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P85045.
    SMRi P85045. Positions 19-146.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P85045.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG052297.

    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. "Purification of a lysozyme from skin secretions of Bufo andrewsi."
      Zhao Y., Jin Y., Lee W.-H., Zhang Y.
      Comp. Biochem. Physiol. 142C:46-52(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Skin secretion1 Publication.

    Entry informationi

    Entry nameiLYS_BUFGA
    AccessioniPrimary (citable) accession number: P85045
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 25 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3