Protein
- UniProt accession
- A0A0F7LBY8 [UniProt]
- Protein name
- Endolysin
- PhaLP type
-
endolysin
evidence: UniProt function annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MAKVQFTKRQETSQIFVHCSATKATMDVGVREIRQWHKEQGWLDVGYHFIIRRDGTVEAGRDQDAVGSHVKGYNSTSVGVCLVGGIDAKGNPEANFTPAQMQSLRSLLVELKVQYAGAVLMAHHDVAPKACPSFDLKRWWEKNELVTSDRG
- Physico‐chemical
properties -
protein length: 151 AA molecular weight: 16828,00000 Da isoelectric point: 8,46736 aromaticity: 0,07947 hydropathy: -0,39205
Domains
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Klebsiella phage K5 [NCBI] |
1647374 | Autographiviridae > Przondovirus > Przondovirus K5 |
Host |
Klebsiella pneumoniae [NCBI] |
573 | Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Klebsiella |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
AKH49558.1
[NCBI]
Genbank nucleotide accession
KR149291
[NCBI]
CDS location
range 10239 -> 10694
strand +
strand +
CDS
ATGGCCAAGGTTCAATTCACTAAGCGACAGGAGACCTCTCAGATTTTCGTTCACTGTTCCGCCACCAAGGCAACCATGGACGTAGGTGTTCGTGAGATTCGCCAGTGGCATAAAGAGCAGGGCTGGCTTGACGTTGGGTATCACTTCATCATCCGTCGTGATGGTACCGTTGAGGCGGGCCGTGACCAAGATGCTGTTGGTTCACACGTCAAGGGATACAACTCGACCTCTGTCGGTGTATGTCTGGTAGGCGGTATCGACGCCAAGGGTAACCCTGAGGCAAACTTCACGCCAGCCCAGATGCAGTCGCTGCGCTCACTGCTGGTAGAACTGAAGGTGCAATACGCTGGGGCCGTTCTGATGGCACACCACGACGTAGCGCCCAAAGCCTGCCCGAGCTTCGACCTGAAGCGTTGGTGGGAGAAGAACGAACTGGTCACTTCAGACCGTGGGTAA
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.