Protein

UniProt accession
A0AAX4JIW8 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MKSQQQAKEWIYNHEGTGVDFDGAYGFQCMDLAVAYVYYITDGKVRMWGNAKDAINNDFKGLATVYENTPSFKPQLGDVAVYTNSQYGHIQCVISGNLDYYTCLEQNWLGGGFDGWEKATIRTHYYDGVTHFIRPKFSNSDSQVLEQNIQKTNNWKQNQYGTYYRNENGTFTCGFLPIFARVGSPKLSEPNGYWFQPNGYTPYDEVCLSDGLVWIGYNWQGTRYYLPVRQWNGKTGNSYSIGLPWGVFS
Physico‐chemical
properties
protein length:249 AA
molecular weight:28548,00000 Da
isoelectric point:5,78970
aromaticity:0,17671
hydropathy:-0,59759

Domains

Domains [InterPro]
IPR007921
22–107
IPR007921 IPR003646
IPR007921
4–134
IPR007921
IPR038765
17–140
IPR038765
Protein sequence: A0AAX4JIW8
1 249
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage vB_SauR_SW25
[NCBI] 		3117415 Rountreeviridae > Rosenblumvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
WVH10356.1 [NCBI]
Genbank nucleotide accession
PP135470 [NCBI]
CDS location
range 5815 -> 6564
strand +
CDS
ATGAAATCACAACAACAAGCTAAAGAATGGATATATAATCATGAGGGTACTGGTGTTGATTTTGATGGTGCATATGGATTTCAATGTATGGACTTAGCTGTTGCTTATGTGTATTACATAACAGACGGTAAAGTTCGTATGTGGGGTAATGCCAAAGACGCGATCAATAACGACTTTAAAGGTTTAGCAACGGTGTATGAAAATACACCGAGCTTTAAACCTCAATTAGGTGACGTTGCTGTTTATACTAATTCTCAATATGGTCACATTCAATGTGTAATAAGTGGTAATTTAGATTATTATACATGCTTAGAGCAAAACTGGTTAGGTGGAGGTTTTGACGGTTGGGAAAAAGCAACAATCAGAACACATTATTATGATGGTGTTACACATTTCATTCGTCCAAAATTTTCAAATAGTGATAGTCAAGTATTAGAACAAAATATTCAAAAAACTAACAACTGGAAACAAAATCAATACGGTACATATTACAGAAATGAAAATGGAACATTTACATGTGGCTTTTTACCAATATTTGCACGTGTTGGAAGTCCTAAATTAAGTGAACCGAATGGTTATTGGTTCCAACCAAACGGGTATACACCATATGATGAGGTTTGTTTATCCGATGGACTAGTGTGGATTGGTTATAATTGGCAAGGCACACGTTATTATTTACCAGTGAGACAATGGAACGGTAAAACGGGTAATAGTTATAGCATTGGTTTACCTTGGGGGGTGTTCTCATAA

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.