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P85152

- LYS1_LYSSX

UniProt

P85152 - LYS1_LYSSX

Protein

Lysozyme

Gene
N/A
Organism
Lysobacter sp. (strain XL1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Has bacteriolytic activity.1 Publication

    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 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. cytolysis Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme (EC:3.2.1.17)
    Alternative name(s):
    Endolysin
    Lysis protein
    Muramidase L3
    OrganismiLysobacter sp. (strain XL1)
    Taxonomic identifieri186334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeLysobacter

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›20›20LysozymePRO_0000291306Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Sequencei

    Sequence statusi: Fragment.

    P85152-1 [UniParc]FASTAAdd to Basket

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    IAIQGGXGYL XQPGDGYKYA                                    20
    Length:20
    Mass (Da):2,094
    Last modified:June 12, 2007 - v1
    Checksum:i8F48EE97DE5EC7AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei20 – 2011 Publication

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Identification of extracellular bacteriolytic enzymes from Lysobacter sp. XL1."
      Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S.
      Submitted (MAY-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiLYS1_LYSSX
    AccessioniPrimary (citable) accession number: P85152
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 12, 2007
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 13 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries

    External Data

    Dasty 3