Protein
- UniProt accession
- A0A059VJW5 [UniProt]
- Protein name
- Endolysin
- PhaLP type
-
endolysin
evidence: UniProt function annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MAKVQFKPRPATDFIVVHCAATKASMDIGVREIRQWHVQQGWLDIGYHFVIRRNGTVENGRPHDVIGSHVKNYNSRALGICLAGGIDDKGQPQNNFTPEQFASLKLLLIANKRQYPQAQIVGHHDLDSGKACPSFKVSDWLKTAGI
- Physico‐chemical
properties -
protein length: 146 AA molecular weight: 16259,00000 Da isoelectric point: 9,43625 aromaticity: 0,08219 hydropathy: -0,35205
Domains
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Pseudomonas phage phiPSA2 [NCBI] |
1500756 | Autographiviridae > Ghunavirus > Ghunavirus PSA2 |
Host |
Pseudomonas syringae pv. actinidiae [NCBI] |
103796 | Bacteria > Proteobacteria > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
AHZ95000.1
[NCBI]
Genbank nucleotide accession
KJ507099
[NCBI]
CDS location
range 11919 -> 12359
strand +
strand +
CDS
ATGGCCAAGGTTCAATTCAAACCGCGTCCAGCCACGGACTTCATCGTGGTTCACTGTGCGGCTACCAAGGCCAGCATGGACATAGGCGTCCGTGAGATTCGCCAGTGGCACGTCCAGCAAGGCTGGCTCGACATTGGTTACCACTTCGTCATTCGTCGTAACGGCACCGTCGAGAACGGTCGTCCTCACGATGTCATCGGGTCCCACGTCAAGAACTACAACAGCCGAGCGCTGGGCATCTGCCTCGCTGGCGGTATCGACGACAAGGGTCAACCCCAGAACAACTTCACGCCTGAGCAGTTCGCATCGCTCAAGCTGCTGCTGATCGCCAACAAGCGTCAGTACCCACAAGCCCAGATCGTTGGTCATCACGACCTCGACTCTGGCAAAGCCTGCCCTTCCTTCAAGGTCTCTGACTGGCTCAAGACGGCTGGCATTTAA
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.