Protein

UniProt accession
A0A0A0P1Q4 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKFEVTPQRKAFLDAIAVGEGTDNGRQQTKNHGYDVIVGGSLFSDYSKHPGRLVKLPKLGINSTAAGRYQVLKKYAEHYIDQLNLPDFSPASQDQIALQQISERKALADIDAGRIREAVAKVNNIWASLPGSKYGQRTETIDDFLKYFRAAGGKVAGE
Physico‐chemical
properties
protein length:159 AA
molecular weight:17470,00000 Da
isoelectric point:9,24523
aromaticity:0,08805
hydropathy:-0,48616

Domains

Domains [InterPro]
Protein sequence: A0A0A0P1Q4
1 159
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Enterobacteria phage IME_EC2
[NCBI]
1414766 Murrayvirus > Murrayvirus EC2
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AGZ17797.1 [NCBI]
Genbank nucleotide accession
KF591601 [NCBI]
CDS location
range 1805 -> 2284
strand +
CDS
ATGGCAAAATTTGAAGTCACGCCACAGCGCAAGGCGTTTCTGGACGCGATCGCGGTAGGAGAGGGAACAGACAACGGTCGCCAGCAGACCAAAAATCACGGCTACGACGTGATCGTGGGCGGCTCGCTGTTCTCCGACTATTCGAAGCATCCGGGGCGGCTGGTGAAGCTGCCGAAGCTCGGCATTAACTCCACGGCGGCGGGCCGCTATCAGGTGCTTAAGAAGTATGCGGAGCATTACATCGACCAGCTAAACCTCCCCGACTTCTCCCCAGCGTCACAGGACCAGATCGCCCTCCAGCAGATCAGCGAGCGTAAAGCGCTGGCGGATATTGACGCGGGCCGGATCCGCGAAGCCGTGGCAAAGGTCAATAACATCTGGGCCTCCCTGCCGGGTTCGAAGTATGGACAACGGACGGAGACGATCGACGACTTCCTGAAATATTTCCGCGCTGCTGGCGGTAAGGTAGCCGGAGAATGA

Gene Ontology

Description Category Evidence (source)
GO:0003796 lysozyme activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0009253 peptidoglycan catabolic process Biological process Inferred from Electronic Annotation (InterPro)
GO:0016829 lyase activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0030430 host cell cytoplasm Cellular component Inferred from Electronic Annotation (UniProt)
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
4.2.2.n2 peptidoglycan lytic endotransglycosylase MurNAc residue
Lyases
Carbon-oxygen lyases
Acting on polysaccharides
match to sequence model evidence used in automatic assertion
ECO:0000256
HAMAP-Rule:MF_04109

Tertiary structure

No tertiary structures available.