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P85143

- NAAA_LYSSP

UniProt

P85143 - NAAA_LYSSP

Protein

N-acetylmuramoyl-L-alanine amidase L2

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

    Has bacteriolytic activity.1 Publication

    Catalytic activityi

    Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.1 Publication

    Enzyme regulationi

    Inhibited by phenylmethanesulfonyl fluoride (PMSF) and EDTA.1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius.1 Publication

    GO - Molecular functioni

    1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. defense response to bacterium Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylmuramoyl-L-alanine amidase L2 (EC:3.5.1.28)
    OrganismiLysobacter sp.
    Taxonomic identifieri72226 [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 – ›13›13N-acetylmuramoyl-L-alanine amidase L2PRO_0000287396Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Sequencei

    Sequence statusi: Fragment.

    P85143-1 [UniParc]FASTAAdd to Basket

    « Hide

    XNVVFLNXPX PQW                                           13
    Length:13
    Mass (Da):1,547
    Last modified:May 15, 2007 - v1
    Checksum:i49FA0BA84E42E447
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei13 – 1311 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 (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
      Strain: XL11 Publication.

    Entry informationi

    Entry nameiNAAA_LYSSP
    AccessioniPrimary (citable) accession number: P85143
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 11 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

    External Data

    Dasty 3