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Q37875

- LYS_BPP1

UniProt

Q37875 - LYS_BPP1

Protein

Lysozyme

Gene

17

Organism
Enterobacteria phage P1 (Bacteriophage P1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity.By similarity

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei42 – 421Proton donorBy similarity

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC

    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

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH24. Glycoside Hydrolase Family 24.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme (EC:3.2.1.17)
    Alternative name(s):
    Endolysin
    Lysis protein
    Muramidase
    Protein gp17
    Gene namesi
    Name:17
    Synonyms:lysa, lyz
    OrganismiEnterobacteria phage P1 (Bacteriophage P1)
    Taxonomic identifieri10678 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaePunalikevirus
    Virus hostiEnterobacteriaceae [TaxID: 543]
    ProteomesiUP000008091: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 185185LysozymePRO_0000218099Add
    BLAST

    Structurei

    Secondary structure

    1
    185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 2511
    Helixi32 – 387
    Helixi41 – 466
    Helixi48 – 503
    Helixi53 – 553
    Beta strandi56 – 594
    Helixi74 – 9522
    Helixi98 – 1003
    Helixi103 – 11614
    Helixi118 – 1225
    Beta strandi123 – 1264
    Turni127 – 1304
    Beta strandi131 – 1344
    Helixi136 – 1427
    Helixi146 – 1516
    Helixi152 – 1554
    Helixi165 – 17915
    Turni180 – 1823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XJTX-ray1.75A1-185[»]
    1XJUX-ray1.07A/B29-185[»]
    ProteinModelPortaliQ37875.
    SMRiQ37875. Positions 9-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ37875.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 24 family.Curated

    Family and domain databases

    Gene3Di1.10.530.40. 1 hit.
    InterProiIPR002196. Glyco_hydro_24.
    IPR023346. Lysozyme-like_dom.
    IPR023347. Lysozyme_dom.
    [Graphical view]
    PfamiPF00959. Phage_lysozyme. 1 hit.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q37875-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGKTAAGGG AICAIAVMIT IVMGNGNVRT NQAGLELIGN AEGCRRDPYM    50
    CPAGVWTDGI GNTHGVTPGV RKTDQQIAAD WEKNILIAER CINQHFRGKD 100
    MPDNAFSAMT SAAFNMGCNS LRTYYSKARG MRVETSIHKW AQKGEWVNMC 150
    NHLPDFVNSN GVPLRGLKIR REKERQLCLT GLVNE 185
    Length:185
    Mass (Da):20,256
    Last modified:November 1, 1996 - v1
    Checksum:i8F7CA469850049B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87673 Genomic DNA. Translation: CAA61013.1.
    AF125376 Genomic DNA. Translation: AAD20630.1.
    AF234172 Genomic DNA. Translation: AAQ13989.1.
    RefSeqiYP_006484.1. NC_005856.1.

    Genome annotation databases

    GeneIDi2777454.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87673 Genomic DNA. Translation: CAA61013.1 .
    AF125376 Genomic DNA. Translation: AAD20630.1 .
    AF234172 Genomic DNA. Translation: AAQ13989.1 .
    RefSeqi YP_006484.1. NC_005856.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XJT X-ray 1.75 A 1-185 [» ]
    1XJU X-ray 1.07 A/B 29-185 [» ]
    ProteinModelPortali Q37875.
    SMRi Q37875. Positions 9-185.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH24. Glycoside Hydrolase Family 24.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2777454.

    Miscellaneous databases

    EvolutionaryTracei Q37875.

    Family and domain databases

    Gene3Di 1.10.530.40. 1 hit.
    InterProi IPR002196. Glyco_hydro_24.
    IPR023346. Lysozyme-like_dom.
    IPR023347. Lysozyme_dom.
    [Graphical view ]
    Pfami PF00959. Phage_lysozyme. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Three functions of bacteriophage P1 involved in cell lysis."
      Schmidt C., Velleman M., Arber W.
      J. Bacteriol. 178:1099-1104(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Lehnherr H., Bendtsen J.D., Preuss F., Ilyina T.V.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiLYS_BPP1
    AccessioniPrimary (citable) accession number: Q37875
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 73 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, 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