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Protein

Lysozyme

Gene

CPL7

Organism
Streptococcus phage Cp-7 (Bacteriophage Cp-7)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CVDX-ray1.67A253-300[»]
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MVKKNDLFVD VASHQGYDIS GILEEAGTTN TIIKVSESTS YLNPCLSAQV
60 70 80 90 100
SQSNPIGFYH FAWFGGNEEE AEAEARYFLD NVPTQVKYLV LDYEDHASAS
110 120 130 140 150
VQRNTTACLR FMQIIAEAGY TPIYYSYKPF TLDNVDYQQI LAQFPNSLWI
160 170 180 190 200
AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EKEDNINNEN
210 220 230 240 250
TLKSLTTVAN EVIQGLWGNG QERYDSLANA GYDPQAVQDK VNEILNAREI
260 270 280 290 300
ADLTTVANEV IQGLWGNGQE RYDSLANAGY DPQAVQDKVN EILNAREIAD
310 320 330 340
LTTVANEVIQ GLWGNGQERY DSLANAGYDP QAVQDKVNEL LS
Length:342
Mass (Da):38,248
Last modified:September 5, 2012 - v2
Checksum:i6B1F431DD068CC52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34779 Genomic DNA. Translation: AAA72844.2.
PIRiJQ0437. MUBPC7.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34779 Genomic DNA. Translation: AAA72844.2.
PIRiJQ0437. MUBPC7.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CVDX-ray1.67A253-300[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH25. Glycoside Hydrolase Family 25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 86 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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.