Protein
- UniProt accession
- A3F665 [UniProt]
- Protein name
- N-acetylmuramoyl-L-alanine amidase
- PhaLP type
-
endolysin
evidence: GO annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MITGKVNNMATLDEVLSFAKGLADTGQGVDLDNVYGTQCVDLPNWITTKYFGIALWGNAIDLLDSAAAQGMEVVYNAPGVNPRAGAIFVMVTYAHGYGHTGLVIVTSDGYVLHNIEQNVDGNADALYIGGPARYVDRPFEDGTGYILGWFYPPYDNTPVQETEPSAPVVAQSDGTYVVNPETGTFTVRVAALNVRSAPRLDAEIVATYGENMEFNYDGWIDSDGYIWVTYISVTGVRRYVAVGNSQNGRRVTNFGTFR
- Physico‐chemical
properties -
protein length: 258 AA molecular weight: 28025,00000 Da isoelectric point: 4,39265 aromaticity: 0,12016 hydropathy: -0,07481
Domains
Domains [InterPro]
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Streptococcus phage phi3396 [NCBI] |
423476 | No lineage information |
Host |
Streptococcus dysgalactiae subsp. equisimilis [NCBI] |
119602 | Bacteria > Firmicutes > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
ABN10829.1
[NCBI]
Genbank nucleotide accession
EF207558
[NCBI]
CDS location
range 34816 -> 35592
strand +
strand +
CDS
ATGATAACTGGAAAGGTCAATAATATGGCAACTTTAGATGAAGTGTTATCCTTTGCCAAGGGATTGGCAGACACTGGTCAAGGGGTTGACCTCGATAATGTTTACGGTACGCAGTGCGTGGACTTGCCAAACTGGATCACGACAAAATATTTTGGCATTGCCCTTTGGGGAAATGCTATTGACTTACTAGATAGTGCAGCCGCCCAAGGAATGGAAGTGGTCTACAATGCTCCTGGAGTTAATCCACGAGCTGGGGCTATCTTTGTGATGGTAACTTACGCTCACGGCTATGGTCATACAGGGTTAGTTATTGTGACGTCAGATGGGTATGTTCTGCATAACATCGAGCAAAACGTGGATGGTAATGCAGATGCTCTTTATATTGGTGGACCAGCACGTTATGTGGATCGTCCGTTTGAAGATGGTACTGGATATATTTTGGGTTGGTTTTACCCTCCTTACGATAATACACCGGTACAAGAAACAGAACCAAGTGCTCCAGTGGTTGCACAGTCAGATGGTACTTATGTAGTTAACCCTGAAACAGGTACTTTTACCGTTCGTGTTGCTGCTTTAAATGTCCGTTCTGCACCTCGTCTAGATGCAGAAATTGTGGCAACTTATGGTGAAAACATGGAATTTAACTATGATGGTTGGATTGACTCAGACGGCTATATTTGGGTGACATATATCAGCGTGACTGGTGTTAGACGATATGTTGCGGTCGGAAACTCACAAAATGGCCGACGTGTGACTAATTTTGGTACTTTTAGATAG
Gene Ontology
Description | Category | Evidence (source) | |
---|---|---|---|
GO:0001897 | symbiont-mediated cytolysis of host cell | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0016787 | hydrolase 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.