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P03706

- ENLYS_LAMBD

UniProt

P03706 - ENLYS_LAMBD

Protein

Endolysin

Gene

R

Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Endolysin with transglycosylase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.

    Catalytic activityi

    Endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei19 – 1911 Publication

    GO - Molecular functioni

    1. carbon-oxygen lyase activity, acting on polysaccharides Source: UniProtKB-EC
    2. lysozyme activity Source: InterPro

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. cytolysis Source: UniProtKB-KW
    3. defense response to bacterium Source: UniProtKB-KW
    4. peptidoglycan catabolic process Source: InterPro
    5. viral release from host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Lyase

    Keywords - Biological processi

    Cytolysis, Host cell lysis by virus, Virus exit from host cell

    Protein family/group databases

    CAZyiGH104. Glycoside Hydrolase Family 104.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endolysin (EC:4.2.2.n2)
    Alternative name(s):
    Lysis protein
    Lysozyme
    Muramidase
    Transglycosylase
    Gene namesi
    Name:R
    OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
    Taxonomic identifieri10710 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
    Virus hostiEscherichia coli [TaxID: 562]
    ProteomesiUP000001711: Genome

    Subcellular locationi

    Host cytoplasm Curated
    Note: The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane.

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311H → D: No effect on lytic activity. 1 Publication
    Mutagenesisi31 – 311H → N: No effect on lytic activity; when associated with N-137. 1 Publication
    Mutagenesisi48 – 481H → N: 97% loss of lytic activity. 1 Publication
    Mutagenesisi137 – 1371H → N: No effect on lytic activity; when associated with N-31. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 158158EndolysinPRO_0000218108Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    IntActiP03706. 1 interaction.

    Structurei

    Secondary structure

    1
    158
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1813
    Beta strandi21 – 266
    Turni31 – 344
    Beta strandi53 – 564
    Beta strandi59 – 613
    Turni65 – 684
    Helixi71 – 8111
    Helixi88 – 10114
    Helixi105 – 1106
    Helixi113 – 1208
    Turni121 – 1233
    Beta strandi132 – 1343
    Helixi135 – 14814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AM7X-ray2.30A/B/C1-158[»]
    1D9UX-ray2.60A/B1-154[»]
    3D3DX-ray2.60A/B1-154[»]
    ProteinModelPortaliP03706.
    SMRiP03706. Positions 1-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03706.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 24 family.Curated

    Family and domain databases

    InterProiIPR002196. Glyco_hydro_24.
    IPR023346. Lysozyme-like_dom.
    [Graphical view]
    PfamiPF00959. Phage_lysozyme. 1 hit.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P03706-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVEINNQRKA FLDMLAWSEG TDNGRQKTRN HGYDVIVGGE LFTDYSDHPR    50
    KLVTLNPKLK STGAGRYQLL SRWWDAYRKQ LGLKDFSPKS QDAVALQQIK 100
    ERGALPMIDR GDIRQAIDRC SNIWASLPGA GYGQFEHKAD SLIAKFKEAG 150
    GTVREIDV 158
    Length:158
    Mass (Da):17,825
    Last modified:July 21, 1986 - v1
    Checksum:i94F8E9A512EAA03E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741Missing AA sequence 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02459 Genomic DNA. Translation: AAA96598.1.
    PIRiB04333. EYBPL.
    RefSeqiNP_040645.1. NC_001416.1.

    Genome annotation databases

    GeneIDi2703480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02459 Genomic DNA. Translation: AAA96598.1 .
    PIRi B04333. EYBPL.
    RefSeqi NP_040645.1. NC_001416.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AM7 X-ray 2.30 A/B/C 1-158 [» ]
    1D9U X-ray 2.60 A/B 1-154 [» ]
    3D3D X-ray 2.60 A/B 1-154 [» ]
    ProteinModelPortali P03706.
    SMRi P03706. Positions 1-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03706. 1 interaction.

    Protein family/group databases

    CAZyi GH104. Glycoside Hydrolase Family 104.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703480.

    Miscellaneous databases

    EvolutionaryTracei P03706.

    Family and domain databases

    InterProi IPR002196. Glyco_hydro_24.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00959. Phage_lysozyme. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Amino-acid sequence of lambda phage endolysin."
      Imada M., Tsugita A.
      Nature New Biol. 233:230-231(1971)
      Cited for: PROTEIN SEQUENCE.
    3. "The R gene product of bacteriophage lambda is the murein transglycosylase."
      Bienkowska-Szewczyk K., Lipinska B., Taylor A.
      Mol. Gen. Genet. 184:111-114(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    4. "Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme."
      Evrard C., Fastrez J., Soumillion P.
      FEBS Lett. 460:442-446(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-31; HIS-48 AND HIS-137.
    5. "Phage lysis: do we have the hole story yet?"
      Young R.
      Curr. Opin. Microbiol. 16:790-797(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    6. "Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes."
      Evrard C., Fastrez J., Declercq J.-P.
      J. Mol. Biol. 276:151-164(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), ACTIVE SITE.
    7. "Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda."
      Di Paolo A., Duval V., Matagne A., Redfield C.
      Biomol. NMR. Assign. 4:111-114(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiENLYS_LAMBD
    AccessioniPrimary (citable) accession number: P03706
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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