Protein
- UniProt accession
- D3W0F3 [UniProt]
- Protein name
- N-acetylmuramoyl-L-alanine amidase
- PhaLP type
-
endolysin
evidence: GO annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MVNQAQVKQWIDTHVGKWVDFDGMYGAQCMDLAVQYAHDLWGFRLTGNAENLRNQALPAGWQRIKNSRGFVPQQGDIFVWYGTKHPYGHTGIVISATLNNYTALEQNMVTGKGQAADKAAINTRPYPSEFWGVVRPPITSGGNITPPDQNGTGGKLTAQRGTFKANSAVNIRRAPNTKTGTVAGVLKAGQTVNYDNIIDADGWRWVSWVGASGNRNYSAVRRLSDNFRTGLCY
- Physico‐chemical
properties -
protein length: 233 AA molecular weight: 25624,00000 Da isoelectric point: 9,69258 aromaticity: 0,10730 hydropathy: -0,47425
Domains
Domains [InterPro]
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Lactococcus phage 1358 [NCBI] |
741942 | Whiteheadvirus > Whiteheadvirus wv1358 |
Host |
Lactococcus lactis [NCBI] |
1358 | Bacteria > Firmicutes > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
ADD25719.1
[NCBI]
Genbank nucleotide accession
GQ403788
[NCBI]
CDS location
range 20162 -> 20863
strand +
strand +
CDS
ATGGTAAATCAAGCACAGGTCAAGCAATGGATTGACACACACGTCGGCAAATGGGTCGACTTCGACGGCATGTACGGCGCGCAATGCATGGACTTAGCCGTCCAATATGCACACGACCTTTGGGGCTTTCGCCTTACAGGTAACGCCGAAAACTTGCGAAATCAAGCTTTGCCCGCAGGGTGGCAACGCATTAAGAATTCGCGCGGCTTCGTTCCACAGCAGGGCGACATCTTCGTGTGGTACGGCACTAAGCACCCGTACGGGCACACAGGTATCGTCATCAGCGCGACGTTGAACAACTACACCGCGCTCGAGCAAAACATGGTTACAGGTAAAGGACAAGCCGCTGACAAAGCGGCAATCAACACACGCCCTTATCCAAGCGAATTTTGGGGCGTTGTGCGCCCGCCGATTACTTCGGGGGGAAATATTACCCCACCCGACCAAAACGGCACAGGCGGCAAACTGACGGCACAGCGGGGTACATTCAAGGCAAACAGCGCCGTGAATATCCGCCGCGCACCGAATACAAAAACAGGAACAGTCGCAGGCGTCCTCAAAGCAGGTCAGACCGTGAACTATGATAATATCATTGACGCGGACGGCTGGCGTTGGGTTTCATGGGTCGGCGCTTCGGGCAACCGAAATTATAGCGCAGTCCGCCGCTTGTCTGACAATTTCCGAACAGGGTTGTGCTATTAA
Gene Ontology
Description | Category | Evidence (source) | |
---|---|---|---|
GO:0001897 | symbiont-mediated cytolysis of host cell | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0003824 | catalytic activity | Molecular function | 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 |
ARBA:ARBA00001561 |
Tertiary structure
No tertiary structures available.