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 +
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.