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]
Protein sequence: A3F665
1 258
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

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 +
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.