UniProtKB - P00806 (ENLYS_BPT7)
Endolysin
3.5
Functioni
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 annotation3 PublicationsEndolysin 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 annotation1 PublicationCatalytic activityi
- Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.UniRule annotation1 Publication EC:3.5.1.28
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 18 | ZincUniRule annotationCombined sources1 Publication | 1 | |
Sitei | 47 | Essential for amidase activity and zinc hydrate coordinationUniRule annotation1 Publication | 1 | |
Metal bindingi | 123 | ZincUniRule annotationCombined sources1 Publication | 1 | |
Sitei | 129 | Important for catalytic activityCombined sources1 Publication | 1 | |
Metal bindingi | 131 | ZincUniRule annotationCombined sources1 Publication | 1 |
GO - Molecular functioni
- N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB
- zinc ion binding Source: InterPro
GO - Biological processi
- cytolysis Source: UniProtKB-KW
- defense response to bacterium Source: UniProtKB-KW
- negative regulation of viral transcription Source: UniProtKB
- peptidoglycan catabolic process Source: UniProtKB-UniRule
- viral release from host cell by cytolysis Source: UniProtKB
Keywordsi
Molecular function | Antimicrobial, Bacteriolytic enzyme, Hydrolase |
Biological process | Cytolysis, Host cell lysis by virus, Viral release from host cell |
Ligand | Metal-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: EndolysinUniRule annotation (EC:3.5.1.28UniRule annotation1 Publication)Alternative name(s): N-acetylmuramoyl-L-alanine amidaseUniRule annotation T7 endolysinCurated |
Gene namesi | Ordered Locus Names:3.5 |
Organismi | Escherichia phage T7 (Bacteriophage T7) |
Taxonomic identifieri | 10760 [NCBI] |
Taxonomic lineagei | Viruses › Duplodnaviria › Heunggongvirae › Uroviricota › Caudoviricetes › Caudovirales › Autographiviridae › Studiervirinae › Teseptimavirus › |
Virus hosti | Escherichia coli [TaxID: 562] |
Proteomesi |
|
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
Keywords - Cellular componenti
Host cytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 18 | H → N, Q or R: Complete loss of amidase activity. 1 Publication | 1 | |
Mutagenesisi | 47 | Y → D, F or L: Complete loss of amidase activity. 1 Publication | 1 | |
Mutagenesisi | 129 | K → I, M, Q, W or Y: Complete loss of amidase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by host | |||
ChainiPRO_0000164410 | 2 – 151 | EndolysinAdd BLAST | 150 |
Interactioni
Subunit structurei
Interacts with the viral RNA polymerase.
UniRule annotation2 PublicationsProtein-protein interaction databases
DIPi | DIP-6090N |
IntActi | P00806, 1 interactor |
MINTi | P00806 |
Structurei
Secondary structure
3D structure databases
SMRi | P00806 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P00806 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 10 – 132 | N-acetylmuramoyl-L-alanine amidaseSequence analysisAdd BLAST | 123 |
Sequence similaritiesi
Family and domain databases
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 |
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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 90 | G → V in AAB32819 (PubMed:7801634).Curated | 1 | |
Sequence conflicti | 119 | V → G (PubMed:6864790).Curated | 1 | |
Sequence conflicti | 119 | V → G (PubMed:7310871).Curated | 1 | |
Sequence conflicti | 119 | V → G (PubMed:7801634).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01146 Genomic DNA Translation: CAA24403.1 V01127 Genomic DNA Translation: CAA24346.1 S75616 Genomic DNA Translation: AAB32819.1 |
PIRi | C94615, MUBPA7 |
RefSeqi | NP_041973.1, NC_001604.1 |
Genome annotation databases
GeneIDi | 1261077 |
KEGGi | vg:1261077 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V01146 Genomic DNA Translation: CAA24403.1 V01127 Genomic DNA Translation: CAA24346.1 S75616 Genomic DNA Translation: AAB32819.1 |
PIRi | C94615, MUBPA7 |
RefSeqi | NP_041973.1, NC_001604.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ARO | X-ray | 2.80 | L | 1-151 | [»] | |
1LBA | X-ray | 2.20 | A | 7-151 | [»] | |
SMRi | P00806 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-6090N |
IntActi | P00806, 1 interactor |
MINTi | P00806 |
Genome annotation databases
GeneIDi | 1261077 |
KEGGi | vg:1261077 |
Miscellaneous databases
EvolutionaryTracei | P00806 |
Family and domain databases
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 |
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 |
MobiDBi | Search... |
Entry informationi
Entry namei | ENLYS_BPT7 | |
Accessioni | P00806Primary (citable) accession number: P00806 Secondary accession number(s): Q38567 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 138 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families