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Protein

Lysozyme

Gene

CPL1

Organism
Streptococcus phage Cp-1 (Bacteriophage Cp-1)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei101
Active sitei941

GO - Molecular functioni

  • lysozyme activity Source: CACAO

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-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]
Proteomesi
  • UP000009089 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10D → A, E, H, K or N: Almost complete loss of activity. 1 Publication1
Mutagenesisi37E → A: 95% loss of activity. 1 Publication1
Mutagenesisi37E → D: 63% loss of activity. 1 Publication1
Mutagenesisi37E → K: Almost complete loss of activity. 1 Publication1
Mutagenesisi37E → Q: 13% loss of activity. 1 Publication1
Mutagenesisi92D → A: Almost complete loss of activity. 1 Publication1
Mutagenesisi94E → A or Q: Almost complete loss of activity. 1 Publication1
Mutagenesisi182D → A: Almost complete loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002082591 – 339LysozymeAdd BLAST339

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
udkP674132EBI-11615908,EBI-11615933From a different organism.

Protein-protein interaction databases

IntActiP15057. 1 interactor.

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi13 – 15Combined sources3
Helixi20 – 26Combined sources7
Beta strandi30 – 37Combined sources8
Turni38 – 40Combined sources3
Helixi46 – 51Combined sources6
Beta strandi53 – 61Combined sources9
Helixi68 – 80Combined sources13
Beta strandi87 – 92Combined sources6
Helixi101 – 117Combined sources17
Beta strandi120 – 127Combined sources8
Helixi128 – 134Combined sources7
Helixi137 – 143Combined sources7
Beta strandi148 – 151Combined sources4
Beta strandi157 – 159Combined sources3
Helixi162 – 164Combined sources3
Beta strandi171 – 177Combined sources7
Beta strandi179 – 188Combined sources10
Beta strandi200 – 204Combined sources5
Beta strandi209 – 213Combined sources5
Beta strandi221 – 226Combined sources6
Beta strandi229 – 233Combined sources5
Beta strandi242 – 247Combined sources6
Beta strandi250 – 254Combined sources5
Beta strandi263 – 267Combined sources5
Beta strandi270 – 274Combined sources5
Beta strandi283 – 287Combined sources5
Beta strandi290 – 295Combined sources6
Helixi297 – 299Combined sources3
Beta strandi302 – 309Combined sources8
Beta strandi312 – 316Combined sources5
Turni318 – 320Combined sources3
Beta strandi327 – 330Combined sources4
Beta strandi335 – 337Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15057.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati200 – 219Cell wall-binding 1Add BLAST20
Repeati220 – 239Cell wall-binding 2Add BLAST20
Repeati241 – 260Cell wall-binding 3Add BLAST20
Repeati261 – 280Cell wall-binding 4Add BLAST20
Repeati281 – 300Cell wall-binding 5Add BLAST20
Repeati303 – 322Cell wall-binding 6Add BLAST20

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)DescriptionActionsGraphical viewLength
Sequence conflicti44P → R in AAA32204 (PubMed:8648702).Curated1

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.
KEGGivg:1261221.

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.
PIRiA31086. MUBPCP.
RefSeqiNP_044837.1. NC_001825.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15057. 1 interactor.

Protein family/group databases

CAZyiGH25. Glycoside Hydrolase Family 25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1261221.
KEGGivg:1261221.

Miscellaneous databases

EvolutionaryTraceiP15057.
PROiP15057.

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...

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 30, 2016
This is version 117 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, Reference 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

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 one 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.