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UniProtKB - P00720 (ENLYS_BPT4)

Protein

Endolysin

Gene

E

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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.UniRule annotation1 Publication EC:3.2.1.17

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 7.3.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei11Proton donorUniRule annotation1 Publication1
Active sitei20NucleophileUniRule annotation2 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei32N-acetyl-D-glucosamine; via amide nitrogenUniRule annotation1 Publication1
Binding sitei104N-acetyl-D-glucosamine; via amide nitrogenUniRule annotation1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei117Substrate-binding1 Publication1
Sitei132Substrate-binding1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • lysozyme activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase
Biological processCytolysis, Host cell lysis by virus, Viral release from host cell

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.2.1.17 732

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GH24 Glycoside Hydrolase Family 24

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
EndolysinUniRule annotation (EC:3.2.1.17UniRule annotation1 Publication)
Alternative name(s):
Lysis proteinUniRule annotation
LysozymeUniRule annotation
MuramidaseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:E
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEnterobacteria phage T4 (Bacteriophage T4)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10665 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4virus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiEscherichia coli [TaxID: 562]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009087 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

  • Host cytoplasm UniRule annotation
    • Note: The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane.UniRule annotation

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Host cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi11E → A, F, H, M or N: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi11E → N: Loss of 84% of enzymatic activity. 1 Publication1
Mutagenesisi11E → Q: Complete loss of activity. 1 Publication1
Mutagenesisi20D → A, N, S or T: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi20D → C: Nearly no effet on specific enzymatic activity. 1 Publication1
Mutagenesisi20D → E or Q: Loss of 99% of enzymatic activity. 1 Publication1
Mutagenesisi26T → E: Covalently bound substrate. 1 Publication1
Mutagenesisi30G → A: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi30G → F: Almost complete loss of enzymatic activity. The enzyme is destabilized by 1.5 kcal/ mol. 1 Publication1
Mutagenesisi117S → F: 10-fold decrease in enzymatic activity. 1 Publication1
Mutagenesisi117S → I: 500-fold decrease in enzymatic activity. 1 Publication1
Mutagenesisi117S → V: 50-fold decrease in enzymatic activity. 1 Publication1
Mutagenesisi132N → I: 5-fold decrease in enzymatic activity. 1 Publication1
Mutagenesisi132N → M or F: 2-fold decrease in enzymatic activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5206

Drug and drug target database

More...DrugBanki		DB06934 (1R)-3-chloro-1-phenylpropan-1-ol
DB07543 (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol
DB03301 2-Allyl-6-Methyl-Phenol
DB02534 2-Allylphenol
DB03842 2-Chloro-6-Methyl-Aniline
DB02403 2-Fluoroaniline
DB02486 2-Hydroxyethyl Disulfide
DB02970 2-Propyl-Aniline
DB01957 3-Chlorophenol
DB01986 3-Fluoro-2-Methyl-Aniline
DB03669 4-Fluorophenethyl Alcohol
DB03660 4-Iodo-L-phenylalanine
DB01932 5-Methylpyrrole
DB04179 Benzofuran
DB03345 Beta-Mercaptoethanol
DB00536 Guanidine
DB04532 Indole
DB02870 N-Allyl-Aniline
DB03255 Phenol
DB00373 Timolol

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002181071 – 164EndolysinAdd BLAST164

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed late in the viral replication.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P00720

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P00720

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 24 family.UniRule annotation

Phylogenomic databases

Database of Orthologous Groups

More...OrthoDBi		VOG090000CE

Family and domain databases

HAMAP database of protein families

More...HAMAPi		MF_04110 ENDOLYSIN_T4, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR034690 Endolysin_T4_type
IPR002196 Glyco_hydro_24
IPR023346 Lysozyme-like_dom_sf
IPR001165 T4-type_lysozyme

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00959 Phage_lysozyme, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00684 T4LYSOZYME

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53955 SSF53955, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P00720-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNIFEMLRID ERLRLKIYKD TEGYYTIGIG HLLTKSPSLN AAKSELDKAI 
        60         70         80         90        100
GRNCNGVITK DEAEKLFNQD VDAAVRGILR NAKLKPVYDS LDAVRRCALI 
       110        120        130        140        150
NMVFQMGETG VAGFTNSLRM LQQKRWDEAA VNLAKSIWYN QTPNRAKRVI 
       160 
TTFRTGTWDA YKNL
Length:164
Mass (Da):18,692
Last modified:May 14, 2014 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i02D568CC8FC81CF1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti12R → G AA sequence (PubMed:5470817).Curated1
Sequence conflicti137I → R AA sequence (PubMed:5470817).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X04567 Genomic DNA Translation: CAA28212.1
AF158101 Genomic DNA Translation: AAD42568.1

Protein sequence database of the Protein Information Resource

More...PIRi		A92896 LZBPT4

NCBI Reference Sequences

More...RefSeqi		NP_049736.1, NC_000866.4

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1258585

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:1258585

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04567 Genomic DNA Translation: CAA28212.1
AF158101 Genomic DNA Translation: AAD42568.1
PIRiA92896 LZBPT4
RefSeqiNP_049736.1, NC_000866.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
102LX-ray1.74A1-164[»]
103LX-ray1.90A1-164[»]
104LX-ray2.80A/B1-164[»]
107LX-ray1.80A1-164[»]
108LX-ray1.80A1-164[»]
109LX-ray1.85A1-164[»]
110LX-ray1.70A1-164[»]
111LX-ray1.80A1-164[»]
112LX-ray1.80A1-164[»]
113LX-ray1.80A1-164[»]
114LX-ray1.80A1-164[»]
115LX-ray1.80A1-164[»]
118LX-ray1.80A1-164[»]
119LX-ray1.65A1-164[»]
120LX-ray1.80A1-164[»]
122LX-ray1.80A1-164[»]
123LX-ray1.80A1-164[»]
125LX-ray1.85A1-164[»]
126LX-ray1.80A1-164[»]
127LX-ray1.85A1-164[»]
128LX-ray1.70A1-164[»]
129LX-ray1.70A1-164[»]
130LX-ray1.70A1-164[»]
131LX-ray1.70A1-164[»]
137LX-ray1.85A/B1-164[»]
138LX-ray1.70A1-164[»]
139LX-ray1.70A1-164[»]
140LX-ray2.10A1-164[»]
141LX-ray2.00A1-164[»]
142LX-ray2.00A1-164[»]
143LX-ray2.00A1-164[»]
144LX-ray2.10A1-164[»]
145LX-ray2.00A1-164[»]
146LX-ray1.85A1-164[»]
147LX-ray2.00A1-164[»]
148LX-ray1.90E1-164[»]
149LX-ray2.60A1-164[»]
150LX-ray2.20A/B/C/D1-164[»]
151LX-ray2.20A1-164[»]
152LX-ray2.00A1-163[»]
155LX-ray1.85A1-164[»]
156LX-ray1.80A1-164[»]
157LX-ray1.85A1-164[»]
158LX-ray1.80A1-164[»]
159LX-ray1.80A1-164[»]
160LX-ray1.80A1-164[»]
161LX-ray1.70A1-164[»]
162LX-ray1.80A1-164[»]
163LX-ray1.80A1-164[»]
164LX-ray1.80A1-164[»]
165LX-ray1.75A1-164[»]
166LX-ray1.75A1-164[»]
167LX-ray2.20A/B1-163[»]
168LX-ray2.90A/B/C/D/E1-164[»]
169LX-ray3.00A/B/C/D/E1-164[»]
170LX-ray2.60A1-164[»]
171LX-ray2.50A1-164[»]
172LX-ray1.90A1-164[»]
173LX-ray1.70A1-164[»]
174LX-ray2.30A/B1-164[»]
175LX-ray2.10A/B1-164[»]
176LX-ray2.20A/B1-164[»]
177LX-ray2.50A1-164[»]
178LX-ray2.71A1-164[»]
180LX-ray1.75A/B1-164[»]
181LX-ray1.80A1-164[»]
182LX-ray1.80A1-164[»]
183LX-ray1.80A1-164[»]
184LX-ray1.80A1-164[»]
185LX-ray1.80A1-164[»]
186LX-ray1.80A1-164[»]
187LX-ray1.80A1-164[»]
188LX-ray1.80A1-164[»]
189LX-ray2.50A1-164[»]
190LX-ray2.00A1-164[»]
191LX-ray1.95A1-164[»]
192LX-ray1.90A1-164[»]
195LX-ray1.90A1-164[»]
196LX-ray2.30A1-164[»]
197LX-ray2.10A1-164[»]
198LX-ray2.00A1-164[»]
199LX-ray1.85A1-164[»]
1B6IX-ray1.90A1-164[»]
1C60X-ray2.00A1-164[»]
1C61X-ray2.00A1-164[»]
1C62X-ray2.30A1-164[»]
1C63X-ray2.00A1-164[»]
1C64X-ray2.00A1-164[»]
1C65X-ray2.00A1-164[»]
1C66X-ray2.10A1-164[»]
1C67X-ray2.20A1-164[»]
1C68X-ray2.50A1-164[»]
1C69X-ray1.80A1-164[»]
1C6AX-ray2.10A1-164[»]
1C6BX-ray2.20A1-164[»]
1C6CX-ray2.00A1-164[»]
1C6DX-ray2.00A1-164[»]
1C6EX-ray1.90A1-164[»]
1C6FX-ray2.00A1-164[»]
1C6GX-ray1.90A1-164[»]
1C6HX-ray1.90A1-164[»]
1C6IX-ray1.90A1-164[»]
1C6JX-ray1.90A1-164[»]
1C6KX-ray1.90A1-164[»]
1C6LX-ray1.90A1-164[»]
1C6MX-ray2.10A1-164[»]
1C6NX-ray2.20A1-164[»]
1C6PX-ray1.90A1-164[»]
1C6QX-ray1.90A1-164[»]
1C6TX-ray2.00A1-164[»]
1CTWX-ray2.10A1-164[»]
1CU0X-ray2.20A1-164[»]
1CU2X-ray1.85A1-164[»]
1CU3X-ray2.12A1-164[»]
1CU5X-ray2.05A1-164[»]
1CU6X-ray2.10A1-164[»]
1CUPX-ray1.89A1-164[»]
1CUQX-ray2.05A1-164[»]
1CV0X-ray2.12A1-164[»]
1CV1X-ray2.10A1-164[»]
1CV3X-ray1.80A1-164[»]
1CV4X-ray1.90A1-164[»]
1CV5X-ray1.87A1-164[»]
1CV6X-ray1.90A1-164[»]
1CVKX-ray1.80A1-164[»]
1CX6X-ray2.01A1-164[»]
1CX7X-ray1.94A1-164[»]
1D2WX-ray1.89A1-164[»]
1D2YX-ray2.06A1-164[»]
1D3FX-ray2.05A1-164[»]
1D3JX-ray1.97A1-164[»]
1D3MX-ray2.12A1-164[»]
1D3NX-ray2.00A1-164[»]
1D9WX-ray1.70A1-164[»]
1DYAX-ray1.90A1-164[»]
1DYBX-ray1.75A1-164[»]
1DYCX-ray2.10A1-164[»]
1DYDX-ray2.10A1-164[»]
1DYEX-ray1.80A1-164[»]
1DYFX-ray1.90A1-164[»]
1DYGX-ray2.10A1-164[»]
1EPYX-ray1.85A1-164[»]
1G06X-ray1.85A1-164[»]
1G07X-ray1.70A1-164[»]
1G0GX-ray1.90A1-164[»]
1G0JX-ray1.80A1-164[»]
1G0KX-ray1.85A1-164[»]
1G0LX-ray1.80A1-164[»]
1G0MX-ray1.70A1-164[»]
1G0PX-ray1.80A1-164[»]
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4W55X-ray1.64A1-164[»]
4W56X-ray1.63A1-164[»]
4W57X-ray1.68A1-164[»]
4W58X-ray1.80A1-164[»]
4W59X-ray1.39A1-164[»]
4W8FX-ray3.54A/B2-161[»]
4WTVX-ray1.90A/B2-164[»]
4XEEX-ray2.90A2-161[»]
4XESX-ray2.60A2-161[»]
4YX7X-ray2.00C/F2-164[»]
4YXAX-ray2.35C/F2-164[»]
4YXCX-ray2.30A2-161[»]
4ZWJX-ray3.30A/B/C/D2-161[»]
5B2GX-ray3.50A/C/E/G2-162[»]
5CGCX-ray3.10A2-161[»]
5CGDX-ray2.60A2-161[»]
5CXVX-ray2.70A2-161[»]
5D5AX-ray2.48A2-161[»]
5D5BX-ray3.80A2-161[»]
5D6LX-ray3.20A2-162[»]
5DGYX-ray7.70A/B/C/D2-161[»]
5DSGX-ray2.60A/B2-11[»]
A/B61-161[»]
5EE7X-ray2.50A2-160[»]
5EUTX-ray2.80A2-163[»]
5EWXX-ray2.60A/B1-35[»]
A/B38-164[»]
5G27X-ray1.61A1-164[»]
5GLHX-ray2.80A2-163[»]
5GLIX-ray2.50A61-163[»]
5I14X-ray1.75A/B1-164[»]
5JDTX-ray1.00A1-164[»]
5JEAX-ray2.65K1-164[»]
5JGNX-ray1.53A1-164[»]
5JGRX-ray1.46A1-164[»]
5JGUX-ray1.47A1-164[»]
5JGVX-ray1.73A1-164[»]
5JGXX-ray1.53A1-164[»]
5JGZX-ray1.53A1-164[»]
5JQHX-ray3.20A/B2-161[»]
5JWSX-ray1.65A1-164[»]
5JWTX-ray1.41A1-164[»]
5JWUX-ray1.70A1-164[»]
5JWVX-ray1.30A1-164[»]
5JWWX-ray1.47A1-164[»]
5KGRX-ray1.47A1-164[»]
5KHZX-ray1.49A1-164[»]
5KI1X-ray1.46A1-164[»]
5KI2X-ray1.50A1-164[»]
5KI3X-ray1.65A1-164[»]
5KI8X-ray1.55A1-164[»]
5KIGX-ray1.50A1-164[»]
5KIIX-ray1.56A1-164[»]
5KIMX-ray1.50A1-164[»]
5KIOX-ray1.63A1-164[»]
5KW2X-ray2.76A2-161[»]
5LWOX-ray1.18A1-164[»]
5LZMX-ray1.80A1-164[»]
5NDDX-ray2.80A2-161[»]
5NDZX-ray3.60A2-161[»]
5T04X-ray3.30A2-161[»]
5T1AX-ray2.81A3-163[»]
5TZRX-ray2.20A2-161[»]
5TZYX-ray3.22A2-161[»]
5V83X-ray2.00A1-164[»]
5V86X-ray1.37A1-164[»]
5V88X-ray1.60A1-164[»]
5VBAX-ray2.27A/B2-162[»]
5VEWX-ray2.70A/B5-161[»]
5VEXX-ray3.00A/B5-161[»]
5VNQneutron diffraction2.20A1-164[»]
5VNRX-ray1.63A1-164[»]
5WF5X-ray2.60A2-161[»]
5WF6X-ray2.90A2-161[»]
5X7DX-ray2.70A2-162[»]
5X93X-ray2.20A61-161[»]
5XEZX-ray3.00A/B4-162[»]
5XF1X-ray3.19A/B4-162[»]
5XPEOther1.65A1-164[»]
5XPFX-ray1.04A1-164[»]
5XPRX-ray3.60A61-161[»]
5XSZX-ray3.20A2-161[»]
5YQRX-ray2.40A2-161[»]
5YQZX-ray3.00R2-161[»]
5ZBHX-ray3.00A3-161[»]
5ZBQX-ray2.70A1-161[»]
5ZKQX-ray2.90A/B61-161[»]
6BG3X-ray1.05A1-164[»]
6BG5X-ray1.10A1-164[»]
6CM4X-ray2.87A2-162[»]
6FFHX-ray2.65A2-162[»]
6FFIX-ray2.20A2-162[»]
6LZMX-ray1.80A1-164[»]
7LZMX-ray1.80A1-164[»]
SMRiP00720
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL5206
DrugBankiDB06934 (1R)-3-chloro-1-phenylpropan-1-ol
DB07543 (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol
DB03301 2-Allyl-6-Methyl-Phenol
DB02534 2-Allylphenol
DB03842 2-Chloro-6-Methyl-Aniline
DB02403 2-Fluoroaniline
DB02486 2-Hydroxyethyl Disulfide
DB02970 2-Propyl-Aniline
DB01957 3-Chlorophenol
DB01986 3-Fluoro-2-Methyl-Aniline
DB03669 4-Fluorophenethyl Alcohol
DB03660 4-Iodo-L-phenylalanine
DB01932 5-Methylpyrrole
DB04179 Benzofuran
DB03345 Beta-Mercaptoethanol
DB00536 Guanidine
DB04532 Indole
DB02870 N-Allyl-Aniline
DB03255 Phenol
DB00373 Timolol

Protein family/group databases

CAZyiGH24 Glycoside Hydrolase Family 24

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258585
KEGGivg:1258585

Phylogenomic databases

OrthoDBiVOG090000CE

Enzyme and pathway databases

BRENDAi3.2.1.17 732

Miscellaneous databases

EvolutionaryTraceiP00720

Family and domain databases

HAMAPiMF_04110 ENDOLYSIN_T4, 1 hit
InterProiView protein in InterPro
IPR034690 Endolysin_T4_type
IPR002196 Glyco_hydro_24
IPR023346 Lysozyme-like_dom_sf
IPR001165 T4-type_lysozyme
PfamiView protein in Pfam
PF00959 Phage_lysozyme, 1 hit
PRINTSiPR00684 T4LYSOZYME
SUPFAMiSSF53955 SSF53955, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiENLYS_BPT4
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00720
Secondary accession number(s): Q38170, Q94N07
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 14, 2014
Last modified: December 5, 2018
This is version 181 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
UniProt is an ELIXIR core data resource
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