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P19385

- LYS_BPCP7

UniProt

P19385 - LYS_BPCP7

Protein

Lysozyme

Gene

CPL7

Organism
Streptococcus phage Cp-7 (Bacteriophage Cp-7)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (05 Sep 2012)
      Previous versions | rss
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    Functioni

    Responsible for the separation of the host daughter cells at the end of cell division and participates in the liberation of progeny bacteriophage into the medium. Degrades cell walls containing either choline or ethanolamine.

    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 sitei10 – 101PROSITE-ProRule annotation
    Active sitei94 – 941PROSITE-ProRule annotation

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cell wall macromolecule catabolic process Source: InterPro
    3. cytolysis Source: UniProtKB-KW
    4. defense response to bacterium Source: UniProtKB-KW
    5. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH25. Glycoside Hydrolase Family 25.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme (EC:3.2.1.17)
    Alternative name(s):
    CP-7 lysin
    Endolysin
    Muramidase
    Gene namesi
    Name:CPL7
    OrganismiStreptococcus phage Cp-7 (Bacteriophage Cp-7)
    Taxonomic identifieri10748 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaePicovirinaeunassigned Picovirinae
    Virus hostiStreptococcus pneumoniae [TaxID: 1313]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342LysozymePRO_0000208260Add
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati205 – 242381; truncatedAdd
    BLAST
    Repeati243 – 290482Add
    BLAST
    Repeati291 – 338483Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni205 – 3381343 X 48 AA tandem repeatsAdd
    BLAST

    Domaini

    The C-terminal domain could be responsible for the substrate recognition.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 25 family.Curated

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR013168. Cpl_7_lyso_C.
    IPR002053. Glyco_hydro_25.
    IPR008270. Glyco_hydro_25_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR018077. Glyco_hydro_fam25_subgr.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF08230. Cpl-7. 3 hits.
    PF01183. Glyco_hydro_25. 1 hit.
    [Graphical view]
    SMARTiSM01095. Cpl-7. 3 hits.
    SM00641. Glyco_25. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00953. GLYCOSYL_HYDROL_F25. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19385-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKKNDLFVD VASHQGYDIS GILEEAGTTN TIIKVSESTS YLNPCLSAQV    50
    SQSNPIGFYH FAWFGGNEEE AEAEARYFLD NVPTQVKYLV LDYEDHASAS 100
    VQRNTTACLR FMQIIAEAGY TPIYYSYKPF TLDNVDYQQI LAQFPNSLWI 150
    AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EKEDNINNEN 200
    TLKSLTTVAN EVIQGLWGNG QERYDSLANA GYDPQAVQDK VNEILNAREI 250
    ADLTTVANEV IQGLWGNGQE RYDSLANAGY DPQAVQDKVN EILNAREIAD 300
    LTTVANEVIQ GLWGNGQERY DSLANAGYDP QAVQDKVNEL LS 342
    Length:342
    Mass (Da):38,248
    Last modified:September 5, 2012 - v2
    Checksum:i6B1F431DD068CC52
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34779 Genomic DNA. Translation: AAA72844.2.
    PIRiJQ0437. MUBPC7.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34779 Genomic DNA. Translation: AAA72844.2 .
    PIRi JQ0437. MUBPC7.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH25. Glycoside Hydrolase Family 25.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR013168. Cpl_7_lyso_C.
    IPR002053. Glyco_hydro_25.
    IPR008270. Glyco_hydro_25_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR018077. Glyco_hydro_fam25_subgr.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF08230. Cpl-7. 3 hits.
    PF01183. Glyco_hydro_25. 1 hit.
    [Graphical view ]
    SMARTi SM01095. Cpl-7. 3 hits.
    SM00641. Glyco_25. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00953. GLYCOSYL_HYDROL_F25. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages."
      Garcia P., Garcia J.L., Garcia E., Sanchez-Puelles J.M., Lopez R.
      Gene 86:81-88(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Garcia P., Garcia J.L., Garcia E., Sanchez-Puelles J.M., Lopez R.
      Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 63; 114; 230; 278 AND 326.

    Entry informationi

    Entry nameiLYS_BPCP7
    AccessioniPrimary (citable) accession number: P19385
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: September 5, 2012
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3