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P00806

- ENLYS_BPT7

UniProt

P00806 - ENLYS_BPT7

Protein

Endolysin

Gene

3.5

Organism
Enterobacteria phage T7 (Bacteriophage T7)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Plays an important role in the switch between viral transcription and T7 genome replication. Once produced in sufficient amount, interacts with and inhibits T7 RNA polymerase that becomes unable to produce additional transcripts. This lysozyme-polymerase complex in turn plays an active role in T7 genome replication and packaging.
    Endolysin with amidase 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 breaking down the peptidoglycan layer.

    Catalytic activityi

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

    Cofactori

    Zinc; required for amidase activity.

    Enzyme regulationi

    Binding of T7 RNA polymerase inhibits amidase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi18 – 181Zinc
    Sitei47 – 471Essential for amidase activity and zinc hydrate coordination
    Metal bindingi123 – 1231Zinc
    Metal bindingi131 – 1311Zinc

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

    GO - Biological processi

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

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Hydrolase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endolysin (EC:3.5.1.28)
    Alternative name(s):
    N-acetylmuramoyl-L-alanine amidase
    T7 lysozyme
    Gene namesi
    Ordered Locus Names:3.5
    OrganismiEnterobacteria phage T7 (Bacteriophage T7)
    Taxonomic identifieri10760 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
    Virus hostiEscherichia coli [TaxID: 562]
    ProteomesiUP000000840: 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.By similarity

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by host
    Chaini2 – 151150EndolysinPRO_0000164410Add
    BLAST

    Expressioni

    Keywords - Developmental stagei

    Late protein

    Interactioni

    Subunit structurei

    Interacts with T7 RNA polymerase/Pol.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    1P005731EBI-1026942,EBI-1026948

    Protein-protein interaction databases

    DIPiDIP-6090N.
    IntActiP00806. 1 interaction.
    MINTiMINT-1513681.

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196
    Helixi30 – 3910
    Beta strandi48 – 514
    Beta strandi53 – 553
    Beta strandi57 – 593
    Beta strandi68 – 703
    Helixi74 – 763
    Beta strandi77 – 837
    Beta strandi90 – 923
    Helixi98 – 11417
    Turni115 – 1173
    Beta strandi119 – 1224
    Helixi123 – 1253
    Beta strandi127 – 1293
    Helixi136 – 1427

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AROX-ray2.80L1-151[»]
    1LBAX-ray2.20A7-151[»]
    ProteinModelPortaliP00806.
    SMRiP00806. Positions 3-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00806.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.80.10. 1 hit.
    InterProiIPR002502. Amidase_domain.
    IPR015510. PGRP.
    [Graphical view]
    PANTHERiPTHR11022. PTHR11022. 1 hit.
    PfamiPF01510. Amidase_2. 1 hit.
    [Graphical view]
    SMARTiSM00644. Ami_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55846. SSF55846. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P00806-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARVQFKQRE STDAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI    50
    IKRDGTVEAG RDEMAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ 100
    MQSLRSLLVT LLAKYEGAVL RAHHEVAPKA CPSFDLKRWW EKNELVTSDR 150
    G 151
    Length:151
    Mass (Da):16,979
    Last modified:January 23, 2007 - v4
    Checksum:iC36BC018754A4146
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901G → V in AAB32819. (PubMed:7801634)Curated
    Sequence conflicti119 – 1191V → G(PubMed:6864790)Curated
    Sequence conflicti119 – 1191V → G(PubMed:7310871)Curated
    Sequence conflicti119 – 1191V → G(PubMed:7801634)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01146 Genomic DNA. Translation: CAA24403.1.
    V01127 Genomic DNA. Translation: CAA24346.1.
    S75616 Genomic DNA. Translation: AAB32819.1.
    PIRiC94615. MUBPA7.
    RefSeqiNP_041973.1. NC_001604.1.

    Genome annotation databases

    GeneIDi1261077.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01146 Genomic DNA. Translation: CAA24403.1 .
    V01127 Genomic DNA. Translation: CAA24346.1 .
    S75616 Genomic DNA. Translation: AAB32819.1 .
    PIRi C94615. MUBPA7.
    RefSeqi NP_041973.1. NC_001604.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ARO X-ray 2.80 L 1-151 [» ]
    1LBA X-ray 2.20 A 7-151 [» ]
    ProteinModelPortali P00806.
    SMRi P00806. Positions 3-151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6090N.
    IntActi P00806. 1 interaction.
    MINTi MINT-1513681.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1261077.

    Miscellaneous databases

    EvolutionaryTracei P00806.

    Family and domain databases

    Gene3Di 3.40.80.10. 1 hit.
    InterProi IPR002502. Amidase_domain.
    IPR015510. PGRP.
    [Graphical view ]
    PANTHERi PTHR11022. PTHR11022. 1 hit.
    Pfami PF01510. Amidase_2. 1 hit.
    [Graphical view ]
    SMARTi SM00644. Ami_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55846. SSF55846. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements."
      Dunn J.J., Studier F.W.
      J. Mol. Biol. 166:477-535(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4."
      Dunn J.J., Studier F.W.
      J. Mol. Biol. 148:303-330(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of T7 lysozyme gene and construction of the vector for transgenic plants resistant to bacterial infection."
      Huang W., Cui X., Tian Y., Lin M., Peng X.
      Wei Sheng Wu Xue Bao 34:261-265(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "T7 lysozyme inhibits transcription by T7 RNA polymerase."
      Moffatt B.A., Studier F.W.
      Cell 49:221-227(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme."
      Zhang X., Studier F.W.
      J. Mol. Biol. 269:10-27(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation."
      Stano N.M., Patel S.S.
      J. Biol. Chem. 279:16136-16143(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase."
      Cheng X., Zhang X., Pflugrath J.W., Studier F.W.
      Proc. Natl. Acad. Sci. U.S.A. 91:4034-4038(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SEQUENCE REVISION TO 119.
    8. "Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme."
      Jeruzalmi D., Steitz T.A.
      EMBO J. 17:4101-4113(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH POLYMERASE.

    Entry informationi

    Entry nameiENLYS_BPT7
    AccessioniPrimary (citable) accession number: P00806
    Secondary accession number(s): Q38567
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 101 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3