E - Endolysin - Enterobacteria phage T4

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

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

pH dependenceⁱ

Optimum pH is 7.3.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	11	Proton donorUniRule annotation1 Publication	1
Active siteⁱ	20	NucleophileUniRule annotation2 Publications	1
Binding siteⁱ	32	N-acetyl-D-glucosamine; via amide nitrogenUniRule annotation1 Publication	1
Binding siteⁱ	104	N-acetyl-D-glucosamine; via amide nitrogenUniRule annotation1 Publication	1
Siteⁱ	117	Substrate-binding1 Publication	1
Siteⁱ	132	Substrate-binding1 Publication	1

GO - Molecular functionⁱ

lysozyme activity
Source: UniProtKB
Inferred from direct assayⁱ
- 4865643

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell wall macromolecule catabolic process Source: InterPro
cytolysis Source: UniProtKB-KW
defense response to bacterium Source: UniProtKB-KW
peptidoglycan catabolic process Source: InterPro
viral release from host cell Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase
Biological process	Cytolysis, Host cell lysis by virus, Viral release from host cell

Enzyme and pathway databases

BRENDAⁱ	3.2.1.17 732

BRENDAⁱ

3.2.1.17 732

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GH24 Glycoside Hydrolase Family 24

CAZyⁱ

GH24 Glycoside Hydrolase Family 24

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: EndolysinUniRule annotation (EC:3.2.1.17UniRule annotation1 Publication) Alternative name(s): Lysis proteinUniRule annotation LysozymeUniRule annotation MuramidaseUniRule annotation
Gene namesⁱ	Name:E
Organismⁱ	Enterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifierⁱ	10665 [NCBI]
Taxonomic lineageⁱ	Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4virus
Virus hostⁱ	Escherichia coli [TaxID: 562]
Proteomesⁱ	UP000009087 Componentⁱ: Genome

Subcellular locationⁱ

Host cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_04110

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

host cell cytoplasm Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Host cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	11	E → A, F, H, M or N: Almost complete loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	11	E → N: Loss of 84% of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	11	E → Q: Complete loss of activity. 1 Publication	1
Mutagenesisⁱ	20	D → A, N, S or T: Almost complete loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	20	D → C: Nearly no effet on specific enzymatic activity. 1 Publication	1
Mutagenesisⁱ	20	D → E or Q: Loss of 99% of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	26	T → E: Covalently bound substrate. 1 Publication	1
Mutagenesisⁱ	30	G → A: Almost complete loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	30	G → F: Almost complete loss of enzymatic activity. The enzyme is destabilized by 1.5 kcal/ mol. 1 Publication	1
Mutagenesisⁱ	117	S → F: 10-fold decrease in enzymatic activity. 1 Publication	1
Mutagenesisⁱ	117	S → I: 500-fold decrease in enzymatic activity. 1 Publication	1
Mutagenesisⁱ	117	S → V: 50-fold decrease in enzymatic activity. 1 Publication	1
Mutagenesisⁱ	132	N → I: 5-fold decrease in enzymatic activity. 1 Publication	1
Mutagenesisⁱ	132	N → M or F: 2-fold decrease in enzymatic activity. 1 Publication	1

Chemistry databases

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

ChEMBLⁱ

CHEMBL5206

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

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000218107	1 – 164	EndolysinAdd BLAST		164

Expressionⁱ

Inductionⁱ

Expressed late in the viral replication.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 11	Combined sources	9
Beta strandⁱ	14 – 19	Combined sources	6
Beta strandⁱ	21 – 23	Combined sources	3
Beta strandⁱ	25 – 28	Combined sources	4
Beta strandⁱ	31 – 37	Combined sources	7
Helixⁱ	39 – 50	Combined sources	12
Beta strandⁱ	55 – 57	Combined sources	3
Helixⁱ	62 – 64	Combined sources	3
Helixⁱ	68 – 79	Combined sources	12
Turnⁱ	82 – 84	Combined sources	3
Helixⁱ	85 – 90	Combined sources	6
Helixⁱ	93 – 106	Combined sources	14
Helixⁱ	108 – 112	Combined sources	5
Helixⁱ	115 – 122	Combined sources	8
Turnⁱ	123 – 125	Combined sources	3
Helixⁱ	126 – 133	Combined sources	8
Beta strandⁱ	134 – 136	Combined sources	3
Helixⁱ	137 – 141	Combined sources	5
Helixⁱ	143 – 155	Combined sources	13
Beta strandⁱ	156 – 158	Combined sources	3
Turnⁱ	159 – 161	Combined sources	3
Helixⁱ	162 – 164	Combined sources	3

Show more details

3D structure databases

SMRⁱ	P00720
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P00720

EvolutionaryTraceⁱ

P00720

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 24 family.UniRule annotation

Phylogenomic databases

Database of Orthologous Groups More...OrthoDBⁱ	VOG090000CE

OrthoDBⁱ

VOG090000CE

Family and domain databases

HAMAPⁱ	MF_04110 ENDOLYSIN_T4, 1 hit
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
PRINTSⁱ	PR00684 T4LYSOZYME
SUPFAMⁱ	SSF53955 SSF53955, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P00720-1 [UniParc]FASTA Add 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

Checksum:ⁱ02D568CC8FC81CF1

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	12	R → G AA sequence (PubMed:5470817).Curated		1
Sequence conflictⁱ	137	I → R AA sequence (PubMed:5470817).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X04567 Genomic DNA Translation: CAA28212.1 AF158101 Genomic DNA Translation: AAD42568.1
PIRⁱ	A92896 LZBPT4
NCBI Reference Sequences More...RefSeqⁱ	NP_049736.1, NC_000866.4

Genome annotation databases

GeneIDⁱ	1258585
KEGGⁱ	vg:1258585

Protein	Similar proteins		Species	Score	Length	Source
P00720	Endolysin	)	BPR51		164	UniRef90_P00720
Endolysin		Shigella phage Sf21		164
Endolysin		Escherichia phage slur04		164
Endolysin		Escherichia phage slur02		164
Endolysin		Escherichia phage EC121		164
+428

Protein	Similar proteins		Species	Score	Length	Source
P00720	Endolysin		Yersinia phage phiD1		164	UniRef50_P00720
Endolysin		Escherichia phage UFV-AREG1		164
Endolysin		BPR27		164
Endolysin	)	BPR51		164
Endolysin		Shigella phage Sf21		164
+502

Entry informationⁱ

Entry nameⁱ	ENLYS_BPT4
Accessionⁱ	P00720Primary (citable) accession number: P00720 Secondary accession number(s): Q38170, Q94N07
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	May 14, 2014
	Last modified:	September 12, 2018
	This is version 178 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

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UniRef

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Annotation systems

Supporting data

UniProtKB - P00720 (ENLYS_BPT4)

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Endolysin

E

Select a section on the left to see content.

<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

<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

Sites

<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

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<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 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

GO - Cellular componenti

Keywords - Cellular componenti

<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

Chemistry databases

<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

<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 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

3D structure databases

Miscellaneous databases

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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 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

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Functionⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ