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P15057

- LYS_BPCP1

UniProt

P15057 - LYS_BPCP1

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Protein

Lysozyme

Gene

CPL1

Organism
Streptococcus phage Cp-1 (Bacteriophage Cp-1)
Status
Reviewed - Annotation score: 5 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. 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
Active sitei94 – 941

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-1 lysin
Endolysin
Muramidase
Gene namesi
Name:CPL1
Synonyms:22
OrganismiStreptococcus phage Cp-1 (Bacteriophage Cp-1)
Taxonomic identifieri10747 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaePicovirinaeunassigned Picovirinae
Virus hostiStreptococcus pneumoniae [TaxID: 1313]
ProteomesiUP000009089: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101D → A, E, H, K or N: Almost complete loss of activity. 1 Publication
Mutagenesisi37 – 371E → A: 95% loss of activity. 1 Publication
Mutagenesisi37 – 371E → D: 63% loss of activity. 1 Publication
Mutagenesisi37 – 371E → K: Almost complete loss of activity. 1 Publication
Mutagenesisi37 – 371E → Q: 13% loss of activity. 1 Publication
Mutagenesisi92 – 921D → A: Almost complete loss of activity. 1 Publication
Mutagenesisi94 – 941E → A or Q: Almost complete loss of activity. 1 Publication
Mutagenesisi182 – 1821D → A: Almost complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339LysozymePRO_0000208259Add
BLAST

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi13 – 153Combined sources
Helixi20 – 267Combined sources
Beta strandi30 – 378Combined sources
Turni38 – 403Combined sources
Helixi46 – 516Combined sources
Beta strandi53 – 619Combined sources
Helixi68 – 8013Combined sources
Beta strandi87 – 926Combined sources
Helixi101 – 11717Combined sources
Beta strandi120 – 1278Combined sources
Helixi128 – 1347Combined sources
Helixi137 – 1437Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 1643Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi179 – 18810Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi242 – 2476Combined sources
Beta strandi250 – 2545Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi290 – 2956Combined sources
Helixi297 – 2993Combined sources
Beta strandi302 – 3098Combined sources
Beta strandi312 – 3165Combined sources
Turni318 – 3203Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi335 – 3373Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP15057.
SMRiP15057. Positions 2-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15057.

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.

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.

P15057-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKKNDLFVD VSSHNGYDIT GILEQMGTTN TIIKISESTT YLNPCLSAQV
60 70 80 90 100
EQSNPIGFYH FARFGGDVAE AEREAQFFLD NVPMQVKYLV LDYEDDPSGD
110 120 130 140 150
AQANTNACLR FMQMIADAGY KPIYYSYKPF THDNVDYQQI LAQFPNSLWI
160 170 180 190 200
AGYGLNDGTA NFEYFPSMDG IRWWQYSSNP FDKNIVLLDD EEDDKPKTAG
210 220 230 240 250
TWKQDSKGWW FRRNNGSFPY NKWEKIGGVW YYFDSKGYCL TSEWLKDNEK
260 270 280 290 300
WYYLKDNGAM ATGWVLVGSE WYYMDDSGAM VTGWVKYKNN WYYMTNERGN
310 320 330
MVSNEFIKSG KGWYFMNTNG ELADNPSFTK EPDGLITVA
Length:339
Mass (Da):39,190
Last modified:January 31, 2002 - v2
Checksum:iE2947566AC676B05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441P → R in AAA32204. (PubMed:8648702)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03586 Genomic DNA. Translation: AAA32204.1.
Z47794 Genomic DNA. Translation: CAA87744.1.
PIRiA31086. MUBPCP.
RefSeqiNP_044837.1. NC_001825.1.

Genome annotation databases

GeneIDi1261221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03586 Genomic DNA. Translation: AAA32204.1 .
Z47794 Genomic DNA. Translation: CAA87744.1 .
PIRi A31086. MUBPCP.
RefSeqi NP_044837.1. NC_001825.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H09 X-ray 2.10 A 2-339 [» ]
1OBA X-ray 2.45 A 1-339 [» ]
2IXU X-ray 2.28 A 1-339 [» ]
2IXV X-ray 1.96 A 1-339 [» ]
2J8F X-ray 1.84 A 1-339 [» ]
2J8G X-ray 1.69 A 1-339 [» ]
ProteinModelPortali P15057.
SMRi P15057. 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...

Genome annotation databases

GeneIDi 1261221.

Miscellaneous databases

EvolutionaryTracei P15057.

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

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiLYS_BPCP1
AccessioniPrimary (citable) accession number: P15057
Secondary accession number(s): Q38009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 31, 2002
Last modified: November 26, 2014
This is version 105 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, Complete proteome

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