Protein
UniProt accession P00806 [UniProt]
Protein name Endolysin
PhaLP type
endolysin
evidence: GO annotation
probability: 100 % (predicted by ML model)
Protein sequence
Physico-chemical
properties
(ProtParam)
protein length: 151 AA
molecular weight: 16979.07550 Da
isoelectric point: 8.80820 (pH at which protein has a neutral charge)
aromaticity: 0.08609 (relative frequency of aromatic residues)
hydropathy: -0.48212 (GRAVY index: - hydrophillic; + hydrophobic)
Domains [InterPro]


Taxonomy

Name Taxonomy ID Lineage
Phage Escherichia phage T7 [NCBI] 10760 Autographiviridae> Teseptimavirus > Teseptimavirus T7
Host Escherichia coli [NCBI]
562 Proteobacteria > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia


Identical proteins

Accession Protein Name Phage
UPI0000110627 [UniParc] D1LVD8 [UniProt] Endolysin Escherichia phage T7 [NCBI]
P00806 [UniProt] Endolysin Escherichia phage T7 [NCBI]
Q3V7D1 [UniProt] Endolysin Enterobacteria phage T7.1 [NCBI]


Coding sequence (CDS)

Genbank protein accession CAA24403.1 [NCBI]
Genbank nucleotide accession V01146.1 [NCBI]
CDS location
range 10706 -> 11161
strand 1
CDS



Gene Ontologies

Description Category Evidence (source)
GO:0008270 zinc ion binding Molecular function Inferred from Electronic Annotation
(InterPro)
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity Molecular function Inferred from Direct Assay
(UniProtKB)
GO:0030430 host cell cytoplasm Cellular component Inferred from Electronic Annotation
(UniProtKB-SubCell)
GO:0009253 peptidoglycan catabolic process Biological process Inferred from Electronic Annotation
(UniProtKB-UniRule)
GO:0019835 cytolysis Biological process Inferred from Electronic Annotation
(UniProtKB-KW)
GO:0032897 negative regulation of viral transcription Biological process Inferred from Direct Assay
(UniProtKB)
GO:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation
(UniProtKB-KW)
GO:0044659 viral release from host cell by cytolysis Biological process Inferred from Direct Assay
(UniProtKB)


Enzymatic activity

EC Name Reaction catalyzed Source
3.5.1.28 N-acetylmuramoyl-L-alanine amidase. Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acidresidues in certain cell-wall glycopeptides. HAMAP-Rule:MF_04111
PubMed:8171031


3D structures

PDB ID Method Resolution (Å) Chain(s) Range
1ARO X-ray 2.80 A L
 1-151
1LBA X-ray 2.20 A A
 7-151


Experimental evidence

pmid Title Authors Publication date
15223315 Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage T7 infection. Zhang X, Studier FW 2004 Jul 16
14764584 T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation. Stano NM, Patel SS 2004 Apr 16
9192997 Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme. Zhang X, Studier FW 1997 May 30
8171031 The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Cheng X, Zhang X, Pflugrath JW, Studier FW 1994 Apr 26