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P15057 (LYS_BPCP1) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme

EC=3.2.1.17
Alternative name(s):
CP-1 lysin
Endolysin
Muramidase
Gene names
Name:CPL1
Synonyms:22
OrganismStreptococcus phage Cp-1 (Bacteriophage Cp-1) [Complete proteome]
Taxonomic identifier10747 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaePicovirinaeunassigned Picovirinae
Virus hostStreptococcus pneumoniae [TaxID: 1313]

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

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.

Domain

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

Sequence similarities

Belongs to the glycosyl hydrolase 25 family.

Contains 6 cell wall-binding repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Lysozyme
PRO_0000208259

Regions

Repeat200 – 21920Cell wall-binding 1
Repeat220 – 23920Cell wall-binding 2
Repeat241 – 26020Cell wall-binding 3
Repeat261 – 28020Cell wall-binding 4
Repeat281 – 30020Cell wall-binding 5
Repeat303 – 32220Cell wall-binding 6

Sites

Active site101
Active site941

Experimental info

Mutagenesis101D → A, E, H, K or N: Almost complete loss of activity. Ref.3
Mutagenesis371E → A: 95% loss of activity. Ref.3
Mutagenesis371E → D: 63% loss of activity. Ref.3
Mutagenesis371E → K: Almost complete loss of activity. Ref.3
Mutagenesis371E → Q: 13% loss of activity. Ref.3
Mutagenesis921D → A: Almost complete loss of activity. Ref.4
Mutagenesis941E → A or Q: Almost complete loss of activity. Ref.4
Mutagenesis1821D → A: Almost complete loss of activity. Ref.4
Sequence conflict441P → R in AAA32204. Ref.2

Secondary structure

................................................................... 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15057 [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: E2947566AC676B05

FASTA33939,190
        10         20         30         40         50         60 
MVKKNDLFVD VSSHNGYDIT GILEQMGTTN TIIKISESTT YLNPCLSAQV EQSNPIGFYH 

        70         80         90        100        110        120 
FARFGGDVAE AEREAQFFLD NVPMQVKYLV LDYEDDPSGD AQANTNACLR FMQMIADAGY 

       130        140        150        160        170        180 
KPIYYSYKPF THDNVDYQQI LAQFPNSLWI AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP 

       190        200        210        220        230        240 
FDKNIVLLDD EEDDKPKTAG TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL 

       250        260        270        280        290        300 
TSEWLKDNEK WYYLKDNGAM ATGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN 

       310        320        330 
MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03586 Genomic DNA. Translation: AAA32204.1.
Z47794 Genomic DNA. Translation: CAA87744.1.
PIRMUBPCP. A31086.
RefSeqNP_044837.1. NC_001825.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP15057.
SMRP15057. Positions 2-339.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH25. Glycoside Hydrolase Family 25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1261221.

Phylogenomic databases

ProtClustDBCLSP2513893.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR018337. 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]
PfamPF01473. CW_binding_1. 5 hits.
PF01183. Glyco_hydro_25. 1 hit.
[Graphical view]
SMARTSM00641. Glyco_25. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS51170. CW. 5 hits.
PS00953. GLYCOSYL_HYDROL_F25. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15057.

Entry information

Entry nameLYS_BPCP1
AccessionPrimary (citable) accession number: P15057
Secondary accession number(s): Q38009
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 31, 2002
Last modified: October 16, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries