EPTG_00019

Functionⁱ

Endolysin with amidase 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 breaking down the peptidoglycan layer.UniRule annotation

Plays an important role in the switch between viral transcription and genome replication. Once produced in sufficient amount, interacts with and inhibits the viral RNA polymerase that becomes unable to produce additional late transcripts. This lysozyme-polymerase complex in turn plays an active role in viral genome replication and packaging.UniRule annotation

Catalytic activityⁱ

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.UniRule annotation

Cofactorⁱ

Zn²⁺UniRule annotationNote: Zn²⁺ is required for amidase activity.UniRule annotation

Enzyme regulationⁱ

Binding to the viral RNA polymerase inhibits amidase activity.UniRule annotation

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	18	ZincUniRule annotation	1
Siteⁱ	47	Essential for amidase activity and zinc hydrate coordinationUniRule annotation	1
Metal bindingⁱ	123	ZincUniRule annotation	1
Metal bindingⁱ	131	ZincUniRule annotation	1

GO - Molecular functionⁱ

N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-UniRule
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cytolysis Source: UniProtKB-KW
cytolysis by virus of host cell Source: UniProtKB-UniRule
defense response to bacterium Source: UniProtKB-KW
negative regulation of viral transcription Source: InterPro
peptidoglycan catabolic process Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Antimicrobial, Bacteriolytic enzymeUniRule annotation, HydrolaseUniRule annotation
Biological process	Cytolysis, Host cell lysis by virusUniRule annotation, Viral release from host cell
Ligand	Metal-bindingUniRule annotation, ZincUniRule annotation

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: EndolysinUniRule annotation (EC:3.5.1.28UniRule annotation) Alternative name(s): N-acetylmuramoyl-L-alanine amidaseUniRule annotation
Gene namesⁱ	ORF Names:EPTG_00019Imported, mT7_p20Imported
Organismⁱ	Enterobacteria phage T7 (Bacteriophage T7)Imported
Taxonomic identifierⁱ	10760 [NCBI]
Taxonomic lineageⁱ	Viruses › dsDNA viruses, no RNA stage › Caudovirales › Podoviridae › Autographivirinae › T7virus › Escherichia virus T7
Virus hostⁱ	Escherichia coli [TaxID: 562]
Proteomesⁱ	UP000244529 Componentⁱ: Genome UP000008856 Componentⁱ: Genome

Subcellular locationⁱ

Host cytoplasm
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_04111

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 cytoplasmUniRule annotation

Expressionⁱ

Keywords - Developmental stageⁱ

Late proteinUniRule annotation

Interactionⁱ

Subunit structureⁱ

Interacts with the viral RNA polymerase.UniRule annotation

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	D1LVD8
SMRⁱ	D1LVD8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 151	Ami_2InterPro annotationAdd BLAST		151
Domainⁱ	1 – 124	PGRPInterPro annotationAdd BLAST		124

Sequence similaritiesⁱ

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.UniRule annotation

Phylogenomic databases

Database of Orthologous Groups More...OrthoDBⁱ	VOG090000Z1

OrthoDBⁱ

VOG090000Z1

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06583 PGRP, 1 hit
Gene3Dⁱ	3.40.80.10, 1 hit
HAMAPⁱ	MF_04111 ENDOLYSIN_T7, 1 hit
InterProⁱ	View protein in InterPro IPR036505 Amidase/PGRP_sf IPR002502 Amidase_domain IPR034689 Endolysin_T7_type IPR015510 PGRP IPR006619 PGRP_domain_met/bac
PANTHERⁱ	PTHR11022 PTHR11022, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01510 Amidase_2, 1 hit
SMARTⁱ	View protein in SMART SM00644 Ami_2, 1 hit SM00701 PGRP, 1 hit
SUPFAMⁱ	SSF55846 SSF55846, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

D1LVD8-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MARVQFKQRE STDAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI 
        60         70         80         90        100
IKRDGTVEAG RDEMAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ 
       110        120        130        140        150
MQSLRSLLVT LLAKYEGAVL RAHHEVAPKA CPSFDLKRWW EKNELVTSDR 

G

Length:151

Mass (Da):16,979

Last modified:January 19, 2010 - v1

Checksum:ⁱC36BC018754A4146

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	GU071091 Genomic DNA Translation: ACY75847.1 MG833025 Genomic DNA Translation: AVH85534.1
NCBI Reference Sequences More...RefSeqⁱ	NP_041973.1, NC_001604.1

Genome annotation databases

GeneIDⁱ	1261077
KEGGⁱ	vg:1261077

Protein	Similar proteins		Species	Score	Length
D1LVD8	Endolysin	)	BPT7		151
Lysozyme		METMZ		151
Endolysin		Enterobacteria phage T7.1		151
Lysozyme (Fragment)		METMZ		113
Lysozyme (Fragment)		BPT7		96

Protein	Similar proteins		Species	Score	Length
D1LVD8	Endolysin	)	BPT7		151
Lysozyme		METMZ		151
Endolysin		Enterobacteria phage T7.1		151
Endolysin		BPT3		151
Endolysin		Enterobacteria phage T7M		151
+36

Protein	Similar proteins		Species	Score	Length
D1LVD8	Endolysin	)	BPT7		151
Lysozyme		METMZ		151
Endolysin		Enterobacteria phage T7.1		151
Endolysin		Serratia phage SM9-3Y		151
Endolysin		Yersinia phage phiYe-F10		151
+121

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	GU071091 Genomic DNA Translation: ACY75847.1 MG833025 Genomic DNA Translation: AVH85534.1
NCBI Reference Sequences More...RefSeqⁱ	NP_041973.1, NC_001604.1

3D structure databases

ProteinModelPortalⁱ	D1LVD8
SMRⁱ	D1LVD8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	1261077
KEGGⁱ	vg:1261077

Phylogenomic databases

Database of Orthologous Groups More...OrthoDBⁱ	VOG090000Z1

OrthoDBⁱ

VOG090000Z1

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06583 PGRP, 1 hit
Gene3Dⁱ	3.40.80.10, 1 hit
HAMAPⁱ	MF_04111 ENDOLYSIN_T7, 1 hit
InterProⁱ	View protein in InterPro IPR036505 Amidase/PGRP_sf IPR002502 Amidase_domain IPR034689 Endolysin_T7_type IPR015510 PGRP IPR006619 PGRP_domain_met/bac
PANTHERⁱ	PTHR11022 PTHR11022, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01510 Amidase_2, 1 hit
SMARTⁱ	View protein in SMART SM00644 Ami_2, 1 hit SM00701 PGRP, 1 hit
SUPFAMⁱ	SSF55846 SSF55846, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	D1LVD8_BPT7
Accessionⁱ	D1LVD8Primary (citable) accession number: D1LVD8 Secondary accession number(s): A0A2P0ZKL2
Entry historyⁱ	Integrated into UniProtKB/TrEMBL:	January 19, 2010
	Last sequence update:	January 19, 2010
	Last modified:	July 18, 2018
	This is version 40 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Unreviewed (UniProtKB/TrEMBL)

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteomeImported

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - D1LVD8 (D1LVD8_BPT7)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Endolysin

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 an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

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

<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 - Biological processi

<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

<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 - Cellular componenti

<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 quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<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

3D structure 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

Domains and Repeats

<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

Sequence databases

Genome annotation databases

<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

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain 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

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ