Protein

UniProt accession
A0A0F7LBS0 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MPVINTHQNIAAFLDMLAVSEGTANHPLTKNRGYDVIVTGLDGKPEIFTDYSDHPFAHGRPAKVFNRRGEKSTASGRYQQLYLFWPHYRKQLALPDFSPLSQDRLAIQLIRERGALDDIRAGRIERAISRCRNIWASLPGAGYGQREHSLEKLVTVWRTAGGVPA
Physico‐chemical
properties
protein length:165 AA
molecular weight:18538,00000 Da
isoelectric point:9,71250
aromaticity:0,09091
hydropathy:-0,44545

Domains

Domains [InterPro]
IPR034691
1–165
IPR034691
IPR023346
7–162
IPR023346
Protein sequence: A0A0F7LBS0
1 165
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage pro483
[NCBI] 		1649240 Peduoviridae > Peduovirus > Peduovirus pro483
Host Escherichia coli
[NCBI] 		562 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Escherichia

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AKH49381.1 [NCBI]
Genbank nucleotide accession
KR073661 [NCBI]
CDS location
range 14128 -> 14625
strand +
CDS
ATGCCGGTTATTAACACGCATCAGAATATCGCCGCCTTTCTCGACATGCTGGCCGTGTCCGAAGGGACGGCGAATCATCCGCTGACGAAAAACCGGGGCTATGACGTGATAGTCACCGGACTGGACGGGAAGCCGGAAATTTTCACCGACTACAGTGACCACCCGTTCGCACATGGCCGACCGGCGAAGGTGTTTAACCGTCGCGGTGAAAAATCCACGGCCTCCGGTCGCTATCAGCAGCTTTACCTGTTCTGGCCGCATTACCGCAAACAGCTTGCCCTGCCGGATTTCAGTCCGTTGTCACAGGACAGACTTGCCATTCAGTTGATCCGCGAACGCGGTGCACTGGATGACATCCGGGCGGGACGCATTGAGCGAGCCATTTCACGCTGTCGAAATATCTGGGCGTCCCTGCCGGGTGCCGGTTACGGTCAGCGTGAGCATTCACTGGAAAAACTGGTCACCGTCTGGCGTACCGCTGGCGGCGTACCGGCTTAA

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.