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P19386

- LYS_BPCP9

UniProt

P19386 - LYS_BPCP9

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Protein
Lysozyme
Gene
CPL9
Organism
Streptococcus phage Cp-9 (Bacteriophage Cp-9)
Status
Reviewed - 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 – 101 By similarity
Active sitei94 – 941 By similarity

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 – 339339Lysozyme
PRO_0000208261Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP19386.
SMRiP19386. Positions 2-339.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati200 – 21920Cell wall-binding 1
Add
BLAST
Repeati220 – 23920Cell wall-binding 2
Add
BLAST
Repeati241 – 26020Cell wall-binding 3
Add
BLAST
Repeati261 – 28020Cell wall-binding 4
Add
BLAST
Repeati281 – 30020Cell wall-binding 5
Add
BLAST
Repeati303 – 32220Cell wall-binding 6
Add
BLAST

Domaini

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

Sequence similaritiesi

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

MVKKNDLFID VSSHNGYDIT GILEQMGTTN TIVKISESTT YLNPCLSAQV    50
EQSTPIGFYH FARFGGDVAE AEREAQFFLD NVPTQVKYLV LDYEDDPSGN 100
AQANTNACLR FMQMIADAGY TPIYYSYKPF TLDNVDYQQI LAQFPNSLWI 150
AGYGLNDGNA DFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EEDEKPKTAG 200
TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL TSEWLKDNEK 250
WYYLKDNGAM VTGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN 300
MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA 339
Length:339
Mass (Da):39,151
Last modified:November 1, 1990 - v1
Checksum:iA2143F05BDED4EDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34780 Genomic DNA. Translation: AAA72845.1.
PIRiJQ0438. MUBPC9.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34780 Genomic DNA. Translation: AAA72845.1 .
PIRi JQ0438. MUBPC9.

3D structure databases

ProteinModelPortali P19386.
SMRi P19386. 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...

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. "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].

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 16, 2013
This is version 87 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

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