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P19386

- LYS_BPCP9

UniProt

P19386 - LYS_BPCP9

Protein

Lysozyme

Gene

CPL9

Organism
Streptococcus phage Cp-9 (Bacteriophage Cp-9)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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. Strictly depends on the presence of choline-containing cell walls for activity.

    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-9 lysin
    Endolysin
    Muramidase
    Gene namesi
    Name:CPL9
    OrganismiStreptococcus phage Cp-9 (Bacteriophage Cp-9)
    Taxonomic identifieri10749 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaePicovirinaeunassigned Picovirinae
    Virus hostiStreptococcus pneumoniae [TaxID: 1313]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339LysozymePRO_0000208261Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP19386.
    SMRiP19386. Positions 2-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati200 – 21920Cell wall-binding 1Add
    BLAST
    Repeati220 – 23920Cell wall-binding 2Add
    BLAST
    Repeati241 – 26020Cell wall-binding 3Add
    BLAST
    Repeati261 – 28020Cell wall-binding 4Add
    BLAST
    Repeati281 – 30020Cell wall-binding 5Add
    BLAST
    Repeati303 – 32220Cell wall-binding 6Add
    BLAST

    Domaini

    The C-terminal domain comprising the repeats is involved in choline binding.By similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 25 family.Curated
    Contains 6 cell wall-binding repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR018337. Cell_wall/Cho-bd_repeat.
    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]
    PfamiPF01473. CW_binding_1. 5 hits.
    PF01183. Glyco_hydro_25. 1 hit.
    [Graphical view]
    SMARTiSM00641. Glyco_25. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS51170. CW. 5 hits.
    PS00953. GLYCOSYL_HYDROL_F25. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19386-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKKNDLFID VSSHNGYDIT GILEQMGTTN TIVKISESTT YLNPCLSAQV    50
    EQSTPIGFYH FARFGGDVAE AEREAQFFLD NVPTQVKYLV LDYEDDPSGN 100
    AQANTNACLR FMQMIADAGY TPIYYSYKPF TLDNVDYQQI LAQFPNSLWI 150
    AGYGLNDGNA DFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EEDEKPKTAG 200
    TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL TSEWLKDNEK 250
    WYYLKDNGAM VTGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN 300
    MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA 339
    Length:339
    Mass (Da):39,151
    Last modified:November 1, 1990 - v1
    Checksum:iA2143F05BDED4EDD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34780 Genomic DNA. Translation: AAA72845.1.
    PIRiJQ0438. MUBPC9.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34780 Genomic DNA. Translation: AAA72845.1 .
    PIRi JQ0438. MUBPC9.

    3D structure databases

    ProteinModelPortali P19386.
    SMRi P19386. Positions 2-339.
    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 IPR018337. Cell_wall/Cho-bd_repeat.
    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 PF01473. CW_binding_1. 5 hits.
    PF01183. Glyco_hydro_25. 1 hit.
    [Graphical view ]
    SMARTi SM00641. Glyco_25. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS51170. CW. 5 hits.
    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].

    Entry informationi

    Entry nameiLYS_BPCP9
    AccessioniPrimary (citable) accession number: P19386
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 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