Protein

UniProt accession
A0AB39U261 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: ML prediction

probability: 99 % (predicted by ML model)

Protein sequence
MKSQKQAKQWIYNHEGAGVDFDGAYGFQCMDLAVAYVYYITDGKVRMWGNAKDAINNNFKGLATVYENTPSFKPQLGDIAVYTNSQYGHIQCVISGNLDYYTCLEQNWLGGGIDGWEKATIRTHYYDGVTHFIRPKFSDSNSQVLEQKIQETNSWNKNQYGTLYKSENGTFTCGFLPIFAREGSPKLSEPNGYWFQPNGYTPYDEVCLSDRLVWIGYNWQGKRYYLPVRQWNGKTGNSYRIGLPWGVFS
Physico‐chemical
properties
protein length:249 AA
molecular weight:28590,00000 Da
isoelectric point:7,57814
aromaticity:0,16867
hydropathy:-0,61165

Domains

Domains [InterPro]

No domain annotations available.

Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage vB_SauP_PSK
[NCBI]
3240362 Rountreeviridae > Rosenblumvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
XDR06074.1 [NCBI]
Genbank nucleotide accession
PQ110032 [NCBI]
CDS location
range 5858 -> 6607
strand +
CDS
ATGAAATCACAAAAACAAGCAAAACAATGGATATATAATCATGAGGGTGCAGGTGTTGACTTTGATGGTGCATATGGATTTCAATGTATGGACTTAGCTGTTGCTTATGTGTATTACATAACAGACGGTAAAGTTCGTATGTGGGGCAATGCCAAAGACGCTATCAATAACAACTTTAAAGGTTTAGCAACGGTGTATGAAAATACACCGAGTTTTAAACCACAATTAGGTGACATAGCTGTTTATACTAATTCTCAATATGGTCATATCCAATGTGTAATAAGTGGTAATTTAGATTATTATACATGCTTAGAGCAAAACTGGTTAGGTGGTGGTATTGACGGTTGGGAAAAAGCAACAATCAGAACACATTATTATGATGGTGTTACACATTTCATTCGTCCTAAATTTTCAGACAGTAATAGTCAAGTATTAGAACAAAAAATACAAGAAACAAATTCATGGAATAAAAATCAATATGGTACATTATATAAATCTGAAAATGGTACATTTACATGTGGTTTTTTACCAATATTTGCACGTGAAGGAAGTCCTAAATTAAGTGAACCGAATGGTTATTGGTTCCAACCAAACGGGTATACACCATATGATGAGGTTTGTTTATCCGATAGACTAGTGTGGATTGGTTATAATTGGCAAGGCAAACGTTATTATTTACCAGTGAGACAATGGAACGGTAAAACGGGTAATAGTTATAGAATTGGTTTACCTTGGGGGGTGTTCTCATAA

Gene Ontology

No Gene Ontology terms available.

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.