Protein

UniProt accession
P00806 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MARVQFKQRESTDAIFVHCSATKPSQNVGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDEMAVGSHAKGYNHNSIGVCLVGGIDDKGKFDANFTPAQMQSLRSLLVTLLAKYEGAVLRAHHEVAPKACPSFDLKRWWEKNELVTSDRG
Physico‐chemical
properties
protein length:151 AA
molecular weight:16979,00000 Da
isoelectric point:8,80820
aromaticity:0,08609
hydropathy:-0,48212

Domains

Domains [InterPro]
Protein sequence: P00806
1 151
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage T7 (Bacteriophage T7)
[NCBI]
10760 Autographiviridae > Teseptimavirus > Teseptimavirus T7
Host Escherichia coli
[NCBI]
562 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Escherichia

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AAB32819.1 [NCBI]
Genbank nucleotide accession
S75616 [NCBI]
CDS location
range 1 -> 456
strand +
CDS
ATGGCTCGTGTACAGTTTAAACAACGTGAATCTACTGACGCAATCTTTGTTCACTGCTCGGCTACCAAGCCAAGTCAGAATGTTGGTGTCCGTGAGATTCGCCAGTGGCACAAAGAGCAGGGTTGGCTCGATGTGGGATACCACTTCATCATCAAGCGAGACGGTACTGTGGAGGCAGGACGAGATGAGATGGCTGTAGGCTCTCACGCTAAGGGTTACAACCACAACTCTATCGGCGTCTGCCTTGTTGGTGGTATCGACGATAAAGTTAAGTTCGACGCTAACTTTACGCCAGCCCAAATGCAATCCCTTCGCTCACTGCTGGTCACACTGCTGGCTAAGTACGAAGGCGCTGGTCTTCGCGCCCATCATGAGGTGGCGCCGAAGGCTTGCCCTTCGTTCGACCTTAAGCGTTGGTGGGAGAAGAACGAACTGGTCACTTCTGACCGTGGATAA

Genbank protein accession
CAA24346.1 [NCBI]
Genbank nucleotide accession
V01127 [NCBI]
CDS location
range 10706 -> 11161
strand +
CDS
ATGGCTCGTGTACAGTTTAAACAACGTGAATCTACTGACGCAATCTTTGTTCACTGCTCGGCTACCAAGCCAAGTCAGAATGTTGGTGTCCGTGAGATTCGCCAGTGGCACAAAGAGCAGGGTTGGCTCGATGTGGGATACCACTTTATCATCAAGCGAGACGGTACTGTGGAGGCAGGACGAGATGAGATGGCTGTAGGCTCTCACGCTAAGGGTTACAACCACAACTCTATCGGCGTCTGCCTTGTTGGTGGTATCGACGATAAAGGTAAGTTCGACGCTAACTTTACGCCAGCCCAAATGCAATCCCTTCGCTCACTGCTTGTCACACTGCTGGCTAAGTACGAAGGCGCTGGTCTTCGCGCCCATCATGAGGTGGCGCCGAAGGCTTGCCCTTCGTTCGACCTTAAGCGTTGGTGGGAGAAGAACGAACTGGTCACTTCTGACCGTGGATAA

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

Gene Ontology

Description Category Evidence (source)
GO:0008270 zinc ion binding Molecular function Inferred from Electronic Annotation (UniProt)
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0009253 peptidoglycan catabolic process Biological process Inferred from Electronic Annotation (InterPro)
GO:0030430 host cell cytoplasm Cellular component Inferred from Electronic Annotation (UniProt)
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 (UniProt)
GO:0044659 viral release from host cell by cytolysis Biological process Inferred from Electronic Annotation (InterPro)

Enzymatic activity

EC Number Entry Name Reaction Catalyzed Classification Evidence Source
3.5.1.28 N-acetylmuramoyl-L-alanine amidase residues in certain cell-wall glycopeptides
Hydrolases
Acting on carbon-nitrogen bonds, other than peptide bonds
In linear amides
match to sequence model evidence used in automatic assertion
ECO:0000255
HAMAP-Rule:MF_04111

Tertiary structure

PDB ID: 1LBA

Method: X-ray crystallography

Resolution: 2.2

Chain position: A

View on RCSB