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Protein

Lysozyme

Gene

CPL9

Organism
Streptococcus phage Cp-9 (Bacteriophage Cp-9)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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
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-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

        10         20         30         40         50
MVKKNDLFID VSSHNGYDIT GILEQMGTTN TIVKISESTT YLNPCLSAQV
60 70 80 90 100
EQSTPIGFYH FARFGGDVAE AEREAQFFLD NVPTQVKYLV LDYEDDPSGN
110 120 130 140 150
AQANTNACLR FMQMIADAGY TPIYYSYKPF TLDNVDYQQI LAQFPNSLWI
160 170 180 190 200
AGYGLNDGNA DFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EEDEKPKTAG
210 220 230 240 250
TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL TSEWLKDNEK
260 270 280 290 300
WYYLKDNGAM VTGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN
310 320 330
MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA
Length:339
Mass (Da):39,151
Last modified:November 1, 1990 - v1
Checksum:iA2143F05BDED4EDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34780 Genomic DNA. Translation: AAA72845.1.
PIRiJQ0438. MUBPC9.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34780 Genomic DNA. Translation: AAA72845.1.
PIRiJQ0438. MUBPC9.

3D structure databases

ProteinModelPortaliP19386.
SMRiP19386. Positions 2-339.
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.
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]
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(1989) [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

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.