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Protein

Endolysin

Gene

3.5

Organism
Enterobacteria phage T7 (Bacteriophage T7)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Publications
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 annotation1 Publication

Catalytic activityi

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation1 PublicationNote: Zn2+ is required for amidase activity.UniRule annotation1 Publication

Enzyme regulationi

Binding to the viral RNA polymerase inhibits amidase activity.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi18ZincUniRule annotationCombined sources1 Publication1
Sitei47Essential for amidase activity and zinc hydrate coordinationUniRule annotation1 Publication1
Metal bindingi123ZincUniRule annotationCombined sources1 Publication1
Sitei129Important for catalytic activityCombined sources1 Publication1
Metal bindingi131ZincUniRule annotationCombined sources1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • cytolysis by virus of host cell Source: UniProtKB
  • defense response to bacterium Source: UniProtKB-KW
  • negative regulation of viral transcription Source: UniProtKB
  • peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Hydrolase
Biological processCytolysis, Host cell lysis by virus, Virus exit from host cell
LigandMetal-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
Gene namesi
Ordered Locus Names:3.5
OrganismiEnterobacteria phage T7 (Bacteriophage T7)
Taxonomic identifieri10760 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7virus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000000840 Componenti: Genome

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

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi18H → N, Q or R: Complete loss of amidase activity. 1 Publication1
Mutagenesisi47Y → D, F or L: Complete loss of amidase activity. 1 Publication1
Mutagenesisi129K → I, M, Q, W or Y: Complete loss of amidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by host
ChainiPRO_00001644102 – 151EndolysinAdd BLAST150

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with the viral RNA polymerase.UniRule annotation2 Publications

Protein-protein interaction databases

DIPiDIP-6090N.
IntActiP00806. 1 interactor.
MINTiMINT-1513681.

Structurei

Secondary structure

1151
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 19Combined sources6
Helixi30 – 39Combined sources10
Beta strandi48 – 51Combined sources4
Beta strandi53 – 55Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi68 – 70Combined sources3
Helixi74 – 76Combined sources3
Beta strandi77 – 83Combined sources7
Beta strandi90 – 92Combined sources3
Helixi98 – 114Combined sources17
Turni115 – 117Combined sources3
Beta strandi119 – 122Combined sources4
Helixi123 – 125Combined sources3
Beta strandi127 – 129Combined sources3
Helixi136 – 142Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AROX-ray2.80L1-151[»]
1LBAX-ray2.20A7-151[»]
ProteinModelPortaliP00806.
SMRiP00806.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00806.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

CDDicd06583. PGRP. 1 hit.
Gene3Di3.40.80.10. 1 hit.
HAMAPiMF_04111. ENDOLYSIN_T7. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00806-1 [UniParc]FASTAAdd 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 23, 2007 - v4
Checksum:iC36BC018754A4146
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90G → V in AAB32819 (PubMed:7801634).Curated1
Sequence conflicti119V → G (PubMed:6864790).Curated1
Sequence conflicti119V → G (PubMed:7310871).Curated1
Sequence conflicti119V → G (PubMed:7801634).Curated1

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.
PIRiC94615. MUBPA7.
RefSeqiNP_041973.1. NC_001604.1.

Genome annotation databases

GeneIDi1261077.
KEGGivg:1261077.

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.
PIRiC94615. MUBPA7.
RefSeqiNP_041973.1. NC_001604.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AROX-ray2.80L1-151[»]
1LBAX-ray2.20A7-151[»]
ProteinModelPortaliP00806.
SMRiP00806.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6090N.
IntActiP00806. 1 interactor.
MINTiMINT-1513681.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1261077.
KEGGivg:1261077.

Miscellaneous databases

EvolutionaryTraceiP00806.

Family and domain databases

CDDicd06583. PGRP. 1 hit.
Gene3Di3.40.80.10. 1 hit.
HAMAPiMF_04111. ENDOLYSIN_T7. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENLYS_BPT7
AccessioniPrimary (citable) accession number: P00806
Secondary accession number(s): Q38567
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 18, 2017
This is version 116 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.