Protein

UniProt accession
O64362 [UniProt]
Protein name
SAR-endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MANRAKLSAAVLSLILAGASAPQILDQFLDEKEGNSLTAYKDGSGIWTICRGATMVDGKPVMQGMKLTQAKCNQVNAIERNKALAWVDRNIKVPLTEPQKAGIASFCPYNIGPGKCFPSTFYKRLNAGDRHGACEAIRWWIKDGGRDCRLTKGQKNGCYGQVERRDQESALTCWEIDQ
Physico‐chemical
properties
protein length:178 AA
molecular weight:19597,00000 Da
isoelectric point:9,04422
aromaticity:0,07303
hydropathy:-0,42247

Domains

Domains [InterPro]
IPR002196
31–168
IPR002196
IPR023347
2–175
IPR023347
IPR043688
8–175
IPR043688
IPR023346
6–170
IPR023346
IPR051018
6–176
IPR051018
IPR034690
9–175
IPR034690
Protein sequence: O64362
1 178
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage N15 (Bacteriophage N15)
[NCBI] 		1604876 Ravinvirus > Ravinvirus N15
Host Escherichia coli
[NCBI] 		562 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Escherichia

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AAC19069.1 [NCBI]
Genbank nucleotide accession
AF064539 [NCBI]
CDS location
range 42915 -> 43451
strand +
CDS
ATGGCTAACAGGGCAAAATTAAGCGCAGCCGTTCTAAGTTTGATTCTTGCTGGCGCGTCAGCCCCACAAATTCTCGACCAGTTTTTGGATGAGAAAGAGGGAAATAGCCTTACTGCTTACAAAGATGGCAGCGGCATCTGGACGATATGCCGTGGTGCCACAATGGTTGATGGCAAGCCAGTAATGCAGGGCATGAAGTTGACGCAGGCCAAATGCAATCAGGTAAACGCCATCGAACGCAATAAGGCTCTTGCGTGGGTTGACCGCAATATCAAAGTTCCTCTGACCGAACCGCAGAAAGCCGGTATCGCATCTTTCTGCCCGTACAACATAGGCCCAGGCAAATGCTTCCCATCGACGTTCTATAAGCGTCTTAATGCTGGCGACCGCCACGGGGCTTGTGAGGCGATCCGATGGTGGATAAAGGATGGTGGCCGCGACTGTCGACTGACCAAGGGCCAGAAGAATGGATGCTATGGGCAAGTTGAGCGGCGTGACCAGGAAAGTGCGTTGACGTGCTGGGAGATAGACCAGTGA

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:0016020 membrane Cellular component Inferred from Electronic Annotation (UniProt)
GO:0016998 cell wall macromolecule catabolic process Biological process Inferred from Electronic Annotation (InterPro)
GO:0020002 host cell plasma membrane Cellular component Inferred from Electronic Annotation (UniProt)
GO:0031640 killing of cells of another organism Biological process Inferred from Electronic Annotation (UniProt)
GO:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation (UniProt)

Enzymatic activity

EC Number Entry Name Reaction Catalyzed Classification Evidence Source
3.2.1.17 lysozyme
aka muramidase 		D-glucosamine residues in chitodextrins
Hydrolases
Glycosylases
Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
 match to sequence model evidence used in automatic assertion
ECO:0000255 		HAMAP-Rule:MF_04136

Tertiary structure

PDB ID: upi000012ea42_model

Method: AlphaFold3 Non-commercial

Resolution: –

Chain position: A