Protein

UniProt accession
A0A249Y3A0 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MKSQQQAKEWIYKHEGVGVDFDGAYGFQCMDLAVAYIYYITDGKVRMWGNAKDAINNDFKGLATVYENTSSFKPQLGDVAVYTNSQYGHIQCVISGNLDYYTCLEQNWLNGGYDGWEKATIRTHYYDGVTHFIRPKFSNSESKVLEQNIQLTNNWKQNQYGTYYRNEKGTFTCGFLPIFARVCSPKLSEPNGYWFQPDGYCDYDEVCLSDGLVWIGYNWQGTRYYLPVRQWNGKTGNAYSIGEPWGAFS
Physico‐chemical
properties
protein length:249 AA
molecular weight:28689,00000 Da
isoelectric point:5,57780
aromaticity:0,17671
hydropathy:-0,58795

Domains

Domains [InterPro]
IPR038765
20–140
IPR038765 IPR003646
IPR007921
22–107
IPR007921
IPR007921
4–134
IPR007921
Protein sequence: A0A249Y3A0
1 249
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage SA4
[NCBI] 		930196 Rountreeviridae > Rosenblumvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ASZ78266.1 [NCBI]
Genbank nucleotide accession
MF001367 [NCBI]
CDS location
range 8964 -> 9713
strand -
CDS
ATGAAATCACAACAACAAGCCAAAGAATGGATATATAAACATGAAGGCGTTGGTGTTGACTTTGATGGTGCATATGGTTTTCAATGTATGGACTTAGCTGTTGCTTATATCTATTATATTACTGACGGTAAAGTGCGTATGTGGGGCAATGCCAAAGACGCAATTAATAATGACTTTAAAGGTTTAGCAACGGTGTATGAAAATACATCGAGCTTTAAACCTCAATTAGGTGATGTTGCAGTATACACAAATTCTCAATATGGACATATCCAATGTGTAATAAGTGGAAATCTTGATTATTATACATGTTTAGAACAAAACTGGTTGAATGGTGGATATGACGGTTGGGAAAAAGCAACAATTAGAACACATTATTATGACGGTGTGACACATTTTATTCGCCCAAAATTCTCAAACAGTGAAAGTAAAGTATTAGAACAAAATATTCAACTAACTAATAATTGGAAACAAAACCAATACGGCACATATTATAGAAACGAAAAGGGAACATTTACATGTGGTTTTTTACCAATATTTGCACGTGTCTGTAGTCCTAAATTAAGTGAACCTAATGGCTATTGGTTCCAACCTGACGGATACTGTGATTATGACGAAGTTTGTTTATCAGATGGATTAGTTTGGATTGGTTATAACTGGCAAGGAACTCGTTATTATTTACCAGTTAGACAATGGAACGGAAAAACAGGTAATGCATATAGTATTGGTGAACCTTGGGGCGCGTTCTCATAA

Gene Ontology

Description Category Evidence (source)
GO:0001897 symbiont-mediated cytolysis of host cell Biological process Inferred from Electronic Annotation (InterPro)
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity Molecular function Inferred from Electronic Annotation (UniProt)

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.