Detail of EN98666809

Summary

    Name:LYS_BPCP1
    FullName:phage Cp-1 lysin,Cpl-1
    Producer Organism:Streptococcus phage Cp-1
    Sequence Length:339
    Mass:39190
    Calculated Isoelectric Point:4.38
    Target:S. pneumoniae
    Link:P15057
    Function: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.

Domains

IPR017853:3-185

IPR018337:220-239

IPR018337:241-260

IPR018337:261-280

IPR018337:281-301

IPR018337:303-322

InterPro

100

150

200

250

300

339

  1  [3-185]:IPR017853,Glycoside hydrolase, catalytic domain?
  2  [220-239]:IPR018337,Cell wall/choline-binding repeat
  3  [241-260]:IPR018337,Cell wall/choline-binding repeat
  4  [261-280]:IPR018337,Cell wall/choline-binding repeat
  5  [281-301]:IPR018337,Cell wall/choline-binding repeat
  6  [303-322]:IPR018337,Cell wall/choline-binding repeat

GO term prediction

No GO term prediction

Structures

1
1H09Method:X-ray
Chains:A=2-339
2
1OBAMethod:X-ray
Chains:A=1-339
3
2IXUMethod:X-ray
Chains:A=1-339
4
2IXVMethod:X-ray
Chains:A=1-339
5
2J8FMethod:X-ray
Chains:A=1-339
6
2J8GMethod:X-ray
Chains:A=1-339

Sequence

MVKKNDLFVDVSSHNGYDITGILEQMGTTNTIIKISESTTYLNPCLSAQVEQSNPIGFYH
FARFGGDVAEAEREAQFFLDNVPMQVKYLVLDYEDDPSGDAQANTNACLRFMQMIADAGY
KPIYYSYKPFTHDNVDYQQILAQFPNSLWIAGYGLNDGTANFEYFPSMDGIRWWQYSSNP
FDKNIVLLDDEEDDKPKTAGTWKQDSKGWWFRRNNGSFPYNKWEKIGGVWYYFDSKGYCL
TSEWLKDNEKWYYLKDNGAMATGWVLVGSEWYYMDDSGAMVTGWVKYKNNWYYMTNERGN
MVSNEFIKSGKGWYFMNTNGELADNPSFTKEPDGLITVA

BlastP to EnzyBase2

Activity

No MICs found on enzybiotics database

References

  [1]  Ahrazem O.,Galan B.,Albert A.,Monterroso B.,Hermoso J.A.,  Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.  Structure,2003,(11):1239-1249  [MEDLINE:22890810]
  [2]  Garcia P.,Lopez R.,Martin A.C.,  Analysis of the complete nucleotide sequence and functional organization of the genome of Streptococcus pneumoniae bacteriophage Cp-1.  J. Virol.,1996,(70):3678-3687  [MEDLINE:96211500]
  [3]  Garcia J.L.,Garcia P.,Sanz J.M.,  Role of Asp-9 and Glu-36 in the active site of the pneumococcal CPL1 lysozyme: an evolutionary perspective of lysozyme mechanism.  Biochemistry,1992,(31):8495-8499  [MEDLINE:93002976]
  [4]  Sanchez-Puelles J.M.,Arraras A.,Garcia P.,Garcia J.L.,Garcia E.,  Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages.  Proc. Natl. Acad. Sci. U.S.A.,1988,(85):914-918  [MEDLINE:88124951]