PhaLP - Phage Lytic Protein database

Protein

Uniprot accession

Q3V7D1 [UniProt]

Proten name

Endolysin

PhaLP type

endolysin
evidence:	GO annotation
probability:	100 %	(predicted by ML model)

Protein sequence

MARVQFKQRESTDAIFVHCSATKPSQNVGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDEMAVGSHAKGYNHNSIGVCLVGGIDDKGKFDANFTPAQMQSLRSLLVTLLAKYEGAVLRAHHEVAPKACPSFDLKRWWEKNELVTSDRG

Physical properties

protein length:	151 AA
molecular weight:	16979.07550 Da
isoelectric point:	8.80817	(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	Enterobacteria phage T7.1 [NCBI]	338882	Caudovirales> Podoviridae> Teseptimavirus > Escherichia virus T7

Identical PhaLPs

	Accession	Protein Name	Phage
UniRef100_P00806	D1LVD8 [UniProt]	Endolysin	Enterobacteria phage T7 [NCBI]
	P00806 [UniProt]	Endolysin	Enterobacteria phage T7 [NCBI]
	Q3V7D1 [UniProt]	Endolysin	Enterobacteria phage T7.1 [NCBI]

Coding Domain Sequence

Genbank protein accession

AAZ32839.1 [NCBI]

Genbank nucleotide accession

DQ100055.1 [NCBI]

CDS location

range	2510 -> 2965
strand	1

CDS

ATGGCTCGTGTACAGTTTAAACAACGTGAATCTACTGACGCAATCTTTGTTCACTGCTCGGCTACCAAGCCAAGTCAGAATGTTGGTGTCCGTGAGATTCGCCAGTGGCACAAAGAGCAGGGTTGGCTCGATGTGGGATACCACTTTATCATCAAGCGAGACGGTACTGTGGAGGCAGGACGAGATGAGATGGCTGTAGGCTCTCACGCTAAGGGTTACAACCACAACTCTATCGGCGTCTGCCTTGTTGGTGGTATCGACGATAAAGGTAAGTTCGACGCTAACTTTACGCCAGCCCAAATGCAATCCCTTCGCTCACTGCTTGTCACACTGCTGGCTAAGTACGAAGGCGCTGTGCTTCGCGCCCATCATGAGGTGGCGCCGAAGGCTTGCCCTTCGTTCGACCTTAAGCGTTGGTGGGAGAAGAACGAACTGGTCACTTCTGACCGTGGATAA

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 Electronic Annotation (UniProtKB-UniRule)
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 Electronic Annotation (InterPro)
GO:0042742	defense response to bacterium	Biological process	Inferred from Electronic Annotation (UniProtKB-KW)
GO:0044659	cytolysis by virus of host cell	Biological process	Inferred from Electronic Annotation (UniProtKB-UniRule)

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