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P00806

- ENLYS_BPT7

UniProt

P00806 - ENLYS_BPT7

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Protein

Endolysin

Gene

3.5

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

Functioni

Plays an important role in the switch between viral transcription and T7 genome replication. Once produced in sufficient amount, interacts with and inhibits T7 RNA polymerase that becomes unable to produce additional transcripts. This lysozyme-polymerase complex in turn plays an active role in T7 genome replication and packaging.
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.

Catalytic activityi

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

Cofactori

Zinc; required for amidase activity.

Enzyme regulationi

Binding of T7 RNA polymerase inhibits amidase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Zinc
Sitei47 – 471Essential for amidase activity and zinc hydrate coordination
Metal bindingi123 – 1231Zinc
Metal bindingi131 – 1311Zinc

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
  3. peptidoglycan catabolic process Source: InterPro
  4. viral release from host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Hydrolase

Keywords - Biological processi

Cytolysis, Host cell lysis by virus, Virus exit from host cell

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Endolysin (EC:3.5.1.28)
Alternative name(s):
N-acetylmuramoyl-L-alanine amidase
T7 lysozyme
Gene namesi
Ordered Locus Names:3.5
OrganismiEnterobacteria phage T7 (Bacteriophage T7)
Taxonomic identifieri10760 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000000840: Genome

Subcellular locationi

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

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host
Chaini2 – 151150EndolysinPRO_0000164410Add
BLAST

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with T7 RNA polymerase/Pol.

Binary interactionsi

WithEntry#Exp.IntActNotes
1P005731EBI-1026942,EBI-1026948

Protein-protein interaction databases

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

Structurei

Secondary structure

1
151
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196
Helixi30 – 3910
Beta strandi48 – 514
Beta strandi53 – 553
Beta strandi57 – 593
Beta strandi68 – 703
Helixi74 – 763
Beta strandi77 – 837
Beta strandi90 – 923
Helixi98 – 11417
Turni115 – 1173
Beta strandi119 – 1224
Helixi123 – 1253
Beta strandi127 – 1293
Helixi136 – 1427

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AROX-ray2.80L1-151[»]
1LBAX-ray2.20A7-151[»]
ProteinModelPortaliP00806.
SMRiP00806. Positions 3-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00806.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901G → V in AAB32819. (PubMed:7801634)Curated
Sequence conflicti119 – 1191V → G(PubMed:6864790)Curated
Sequence conflicti119 – 1191V → G(PubMed:7310871)Curated
Sequence conflicti119 – 1191V → G(PubMed:7801634)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ARO X-ray 2.80 L 1-151 [» ]
1LBA X-ray 2.20 A 7-151 [» ]
ProteinModelPortali P00806.
SMRi P00806. Positions 3-151.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6090N.
IntActi P00806. 1 interaction.
MINTi MINT-1513681.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1261077.

Miscellaneous databases

EvolutionaryTracei P00806.

Family and domain databases

Gene3Di 3.40.80.10. 1 hit.
InterProi IPR002502. Amidase_domain.
IPR015510. PGRP.
[Graphical view ]
PANTHERi PTHR11022. PTHR11022. 1 hit.
Pfami PF01510. Amidase_2. 1 hit.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
[Graphical view ]
SUPFAMi SSF55846. SSF55846. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements."
    Dunn J.J., Studier F.W.
    J. Mol. Biol. 166:477-535(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4."
    Dunn J.J., Studier F.W.
    J. Mol. Biol. 148:303-330(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of T7 lysozyme gene and construction of the vector for transgenic plants resistant to bacterial infection."
    Huang W., Cui X., Tian Y., Lin M., Peng X.
    Wei Sheng Wu Xue Bao 34:261-265(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "T7 lysozyme inhibits transcription by T7 RNA polymerase."
    Moffatt B.A., Studier F.W.
    Cell 49:221-227(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme."
    Zhang X., Studier F.W.
    J. Mol. Biol. 269:10-27(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation."
    Stano N.M., Patel S.S.
    J. Biol. Chem. 279:16136-16143(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase."
    Cheng X., Zhang X., Pflugrath J.W., Studier F.W.
    Proc. Natl. Acad. Sci. U.S.A. 91:4034-4038(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SEQUENCE REVISION TO 119.
  8. "Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme."
    Jeruzalmi D., Steitz T.A.
    EMBO J. 17:4101-4113(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH POLYMERASE.

Entry informationi

Entry nameiENLYS_BPT7
AccessioniPrimary (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: October 29, 2014
This is version 102 of the entry and version 4 of the sequence. [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

External Data

Dasty 3