Protein

UniProt accession
A0A068CDE9 [UniProt]
Protein name
Lysozyme
PhaLP type
endolysin

evidence: ML prediction

probability: 99 % (predicted by ML model)

Protein sequence
MSIKNFFDAAREIAGGKLTQAQVDDLNKVIDRLSPSGMTTSDTGINLISTFEGTRLTAYDDGVGVWTIGIGTTVYPNGTKVKKGDTCTSEQAKTYFKHDLIKFENVVNESVKVPLSQNQFDALVSLTYNIGSGAFKNSTLLKLLNNGDYQGAADQFPAWKKAGGRVLEGLVKRRAAERSLFLKK
Physico‐chemical
properties
protein length:184 AA
molecular weight:20047,00000 Da
isoelectric point:9,25458
aromaticity:0,08696
hydropathy:-0,30870

Domains

Domains [InterPro]
IPR023347
36–184
IPR023347
IPR033907
44–182
IPR033907
IPR043688
3–184
IPR043688
IPR051018
34–183
IPR051018
IPR023346
35–183
IPR023346
IPR034690
11–184
IPR034690
IPR002196
50–177
IPR002196
Protein sequence: A0A068CDE9
1 184
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Acinetobacter phage YMC-13-01-C62
[NCBI] 		1505225 Obolenskvirus > Obolenskvirus AbC62
Host Acinetobacter baumannii
[NCBI] 		470 Bacteria > Proteobacteria > Gammaproteobacteria > Pseudomonadales > Moraxellaceae > Acinetobacter

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AID17956.1 [NCBI]
Genbank nucleotide accession
KJ817802 [NCBI]
CDS location
range 17354 -> 17908
strand -
CDS
ATGAGTATTAAGAATTTCTTTGATGCTGCGCGTGAAATTGCTGGTGGCAAGCTTACACAAGCGCAGGTTGACGATCTAAACAAAGTGATTGATCGCCTTTCACCTTCTGGAATGACCACAAGTGACACTGGCATCAATCTAATTTCTACTTTTGAAGGAACTAGATTAACTGCATATGATGATGGTGTTGGCGTATGGACCATCGGCATAGGTACAACCGTCTACCCCAATGGTACAAAAGTTAAGAAAGGCGATACATGTACATCTGAACAAGCAAAAACCTACTTCAAACATGATTTAATTAAGTTTGAAAATGTTGTAAATGAATCTGTTAAAGTTCCACTTAGTCAAAATCAATTTGACGCTCTAGTATCACTGACCTACAACATTGGCTCAGGTGCTTTTAAAAATTCAACTTTACTCAAACTTCTTAATAATGGCGATTATCAAGGTGCTGCCGATCAATTCCCAGCGTGGAAAAAAGCTGGTGGTCGAGTTCTTGAAGGTTTAGTTAAGCGCCGTGCTGCTGAAAGAAGTTTATTTCTAAAGAAGTAA

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:0030430 host cell cytoplasm 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:0000256 		ARBA:ARBA00000632

Tertiary structure

No tertiary structures available.