Protein

UniProt accession
A0A1I9SE91 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MVSKVQFNPRSRTDAIFVHCSATKPDMDIGVETIRMWHKQQGWLDVGYHFVIKRDGTVEEGRPVNVVGSHVKDWNSRSVGVCLVGGINANGKFEANFTPAQMDSLRIKLDDLKVLYPQAEIKAHHDVAPKACPSFDLQRWLTTNELVTSDRG
Physico‐chemical
properties
protein length:152 AA
molecular weight:17075,00000 Da
isoelectric point:7,77819
aromaticity:0,07895
hydropathy:-0,37237

Domains

Domains [InterPro]
IPR002502
14–133
IPR002502
IPR034689
2–150
IPR034689
IPR002502
11–134
IPR002502
IPR015510
16–139
IPR015510
IPR036505
11–146
IPR036505
IPR006619
2–128
IPR006619
IPR036505
8–152
IPR036505
IPR002502
2–134
IPR002502
Protein sequence: A0A1I9SE91
1 152
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage JSS1
[NCBI] 		1897443 Autographiviridae > Kayfunavirus > Kayfunavirus PE31
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AOZ65168.1 [NCBI]
Genbank nucleotide accession
KX689784 [NCBI]
CDS location
range 28280 -> 28738
strand -
CDS
ATGGTGAGTAAGGTTCAGTTCAACCCACGGTCACGGACTGACGCTATCTTCGTTCACTGTTCGGCTACCAAGCCAGATATGGACATCGGGGTAGAGACAATCCGTATGTGGCACAAGCAGCAAGGCTGGCTGGACGTAGGCTACCACTTCGTCATCAAGCGTGATGGCACTGTGGAAGAAGGCCGCCCGGTCAATGTCGTAGGGTCACACGTTAAGGACTGGAACTCCCGGTCCGTAGGCGTCTGCCTTGTAGGTGGGATCAACGCTAATGGCAAGTTTGAAGCTAACTTCACTCCAGCCCAGATGGACTCCCTGCGCATCAAGCTGGATGACCTGAAGGTCCTGTATCCTCAGGCAGAAATCAAAGCACACCATGACGTAGCACCTAAGGCCTGTCCAAGTTTTGACTTGCAACGCTGGTTGACTACCAACGAACTGGTCACTTCCGACCGTGGTTAA

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.