Protein

UniProt accession
A0A7I6HJW2 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MMVSKVQFNPRSRTDAIFVHCSATKPSQDIGVDTIRMWHKQQGWLDVGYHFVIKRDGTVEEGRPVDVVGSHVKDWNSRSVGVCLVGGIDAKGKFEANFTPAQMNALRNKLAELKALYPQADIKAHHDVAPKACPSFDLQLWLSTNELVTSDHG
Physico‐chemical
properties
protein length:153 AA
molecular weight:17013,00000 Da
isoelectric point:7,78677
aromaticity:0,07843
hydropathy:-0,33203

Domains

Domains [InterPro]
IPR002502
15–134
IPR002502
IPR002502
12–135
IPR002502
IPR015510
15–135
IPR015510
IPR034689
3–151
IPR034689
IPR006619
3–129
IPR006619
IPR036505
9–153
IPR036505
IPR036505
12–147
IPR036505
IPR002502
3–135
IPR002502
Protein sequence: A0A7I6HJW2
1 153
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage CLB_P1
[NCBI] 		1262524 Autographiviridae > Kayfunavirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AGD81047.1 [NCBI]
Genbank nucleotide accession
KC109329 [NCBI]
CDS location
range 9887 -> 10348
strand +
CDS
ATGATGGTGAGTAAGGTGCAATTCAACCCACGGTCCCGGACTGACGCTATCTTCGTTCACTGTAGTGCAACCAAACCGTCTCAGGACATCGGGGTAGACACTATCCGCATGTGGCACAAGCAGCAGGGATGGCTGGACGTAGGCTACCACTTCGTCATCAAGCGAGATGGTACTGTGGAAGAGGGTCGCCCGGTAGATGTAGTGGGGTCCCACGTTAAGGATTGGAACTCCCGGTCCGTAGGCGTCTGCCTTGTTGGTGGAATCGACGCTAAGGGCAAGTTTGAAGCCAACTTCACGCCTGCTCAGATGAACGCTCTACGAAACAAGCTGGCTGAACTGAAGGCCCTGTACCCTCAGGCAGACATCAAGGCTCACCACGATGTAGCACCAAAGGCTTGCCCAAGTTTTGACTTACAACTCTGGCTGTCTACCAATGAACTGGTAACTTCCGACCACGGTTAA

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.