Protein

UniProt accession
A0A088FBW1 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MSRVQFKQRESTDAIFVHCSATKSSQNVGVREIRQWHKEQGWLDVGYHYIIKRDGTVEEGRDEMAVGSHAKGHNHNSIGVCLVGGIDDKGKFEANFTPAQMQSLRSLLVTLLAKYEGSVLRAHHDVAPKACPSFDLKRWWEKNELVTSDRG
Physico‐chemical
properties
protein length:151 AA
molecular weight:17049,00000 Da
isoelectric point:8,45749
aromaticity:0,07947
hydropathy:-0,58609

Domains

Domains [InterPro]
Protein sequence: A0A088FBW1
1 151
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage CICC 80001
[NCBI]
1527506 Autographiviridae > Teseptimavirus > Teseptimavirus CICC80001
Host Escherichia coli
[NCBI]
562 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Escherichia

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AIM41074.1 [NCBI]
Genbank nucleotide accession
KM242061 [NCBI]
CDS location
range 15370 -> 15825
strand +
CDS
ATGTCTCGTGTACAGTTCAAACAACGTGAATCCACTGACGCAATCTTTGTTCACTGCTCGGCTACCAAGTCAAGTCAGAATGTGGGTGTCCGTGAGATTCGCCAGTGGCACAAAGAGCAGGGTTGGCTTGACGTGGGATACCACTACATTATCAAGCGCGATGGTACTGTGGAGGAAGGCCGAGACGAGATGGCTGTTGGTTCTCACGCCAAGGGTCACAACCATAACTCAATCGGTGTCTGCCTCGTTGGTGGCATTGACGATAAAGGTAAGTTCGAAGCTAACTTTACGCCAGCCCAAATGCAATCCCTTCGCTCACTGCTTGTCACACTACTGGCTAAGTACGAAGGTTCTGTTCTTCGCGCACATCATGATGTGGCACCAAAGGCTTGCCCATCGTTCGACCTTAAGCGTTGGTGGGAGAAGAACGAACTGGTCACTTCTGACCGTGGATAA

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:0000256
HAMAP-Rule:MF_04111

Tertiary structure

No tertiary structures available.