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P15057

- LYS_BPCP1

UniProt

P15057 - LYS_BPCP1

Protein

Lysozyme

Gene

CPL1

Organism
Streptococcus phage Cp-1 (Bacteriophage Cp-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (31 Jan 2002)
      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 – 101
    Active sitei94 – 941

    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-1 lysin
    Endolysin
    Muramidase
    Gene namesi
    Name:CPL1
    Synonyms:22
    OrganismiStreptococcus phage Cp-1 (Bacteriophage Cp-1)
    Taxonomic identifieri10747 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaePicovirinaeunassigned Picovirinae
    Virus hostiStreptococcus pneumoniae [TaxID: 1313]
    ProteomesiUP000009089: Genome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101D → A, E, H, K or N: Almost complete loss of activity. 1 Publication
    Mutagenesisi37 – 371E → A: 95% loss of activity. 1 Publication
    Mutagenesisi37 – 371E → D: 63% loss of activity. 1 Publication
    Mutagenesisi37 – 371E → K: Almost complete loss of activity. 1 Publication
    Mutagenesisi37 – 371E → Q: 13% loss of activity. 1 Publication
    Mutagenesisi92 – 921D → A: Almost complete loss of activity. 1 Publication
    Mutagenesisi94 – 941E → A or Q: Almost complete loss of activity. 1 Publication
    Mutagenesisi182 – 1821D → A: Almost complete loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339LysozymePRO_0000208259Add
    BLAST

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Helixi13 – 153
    Helixi20 – 267
    Beta strandi30 – 378
    Turni38 – 403
    Helixi46 – 516
    Beta strandi53 – 619
    Helixi68 – 8013
    Beta strandi87 – 926
    Helixi101 – 11717
    Beta strandi120 – 1278
    Helixi128 – 1347
    Helixi137 – 1437
    Beta strandi148 – 1514
    Beta strandi157 – 1593
    Helixi162 – 1643
    Beta strandi171 – 1777
    Beta strandi179 – 18810
    Beta strandi200 – 2045
    Beta strandi209 – 2135
    Beta strandi221 – 2266
    Beta strandi229 – 2335
    Beta strandi242 – 2476
    Beta strandi250 – 2545
    Beta strandi263 – 2675
    Beta strandi270 – 2745
    Beta strandi283 – 2875
    Beta strandi290 – 2956
    Helixi297 – 2993
    Beta strandi302 – 3098
    Beta strandi312 – 3165
    Turni318 – 3203
    Beta strandi327 – 3304
    Beta strandi335 – 3373

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H09X-ray2.10A2-339[»]
    1OBAX-ray2.45A1-339[»]
    2IXUX-ray2.28A1-339[»]
    2IXVX-ray1.96A1-339[»]
    2J8FX-ray1.84A1-339[»]
    2J8GX-ray1.69A1-339[»]
    ProteinModelPortaliP15057.
    SMRiP15057. Positions 2-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15057.

    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.

    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.

    P15057-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKKNDLFVD VSSHNGYDIT GILEQMGTTN TIIKISESTT YLNPCLSAQV    50
    EQSNPIGFYH FARFGGDVAE AEREAQFFLD NVPMQVKYLV LDYEDDPSGD 100
    AQANTNACLR FMQMIADAGY KPIYYSYKPF THDNVDYQQI LAQFPNSLWI 150
    AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EEDDKPKTAG 200
    TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL TSEWLKDNEK 250
    WYYLKDNGAM ATGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN 300
    MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA 339
    Length:339
    Mass (Da):39,190
    Last modified:January 31, 2002 - v2
    Checksum:iE2947566AC676B05
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441P → R in AAA32204. (PubMed:8648702)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03586 Genomic DNA. Translation: AAA32204.1.
    Z47794 Genomic DNA. Translation: CAA87744.1.
    PIRiA31086. MUBPCP.
    RefSeqiNP_044837.1. NC_001825.1.

    Genome annotation databases

    GeneIDi1261221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03586 Genomic DNA. Translation: AAA32204.1 .
    Z47794 Genomic DNA. Translation: CAA87744.1 .
    PIRi A31086. MUBPCP.
    RefSeqi NP_044837.1. NC_001825.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H09 X-ray 2.10 A 2-339 [» ]
    1OBA X-ray 2.45 A 1-339 [» ]
    2IXU X-ray 2.28 A 1-339 [» ]
    2IXV X-ray 1.96 A 1-339 [» ]
    2J8F X-ray 1.84 A 1-339 [» ]
    2J8G X-ray 1.69 A 1-339 [» ]
    ProteinModelPortali P15057.
    SMRi P15057. 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...

    Genome annotation databases

    GeneIDi 1261221.

    Miscellaneous databases

    EvolutionaryTracei P15057.

    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. "Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages."
      Garcia E., Garcia J.L., Garcia P., Arraras A., Sanchez-Puelles J.M., Lopez R.
      Proc. Natl. Acad. Sci. U.S.A. 85:914-918(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the complete nucleotide sequence and functional organization of the genome of Streptococcus pneumoniae bacteriophage Cp-1."
      Martin A.C., Lopez R., Garcia P.
      J. Virol. 70:3678-3687(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Role of Asp-9 and Glu-36 in the active site of the pneumococcal CPL1 lysozyme: an evolutionary perspective of lysozyme mechanism."
      Sanz J.M., Garcia P., Garcia J.L.
      Biochemistry 31:8495-8499(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-10 AND GLU-37.
    4. "Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1."
      Hermoso J.A., Monterroso B., Albert A., Galan B., Ahrazem O., Garcia P., Martinez-Ripoll M., Garcia J.L., Menendez M.
      Structure 11:1239-1249(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH CHOLINE, MUTAGENESIS OF ASP-92; GLU-94 AND ASP-182.

    Entry informationi

    Entry nameiLYS_BPCP1
    AccessioniPrimary (citable) accession number: P15057
    Secondary accession number(s): Q38009
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete 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