Protein

UniProt accession
A0AAX4FYY2 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MKSQQQAKEWIYKHEGAGVDFDGAYGFQCMDLSVAYVYYITDGKVRMWGNAKDAINNDFKGLATVYKNTPSFKPQLGDVAVYTNGQYGHIQCVLSGNLDYYTCLEQNWLGGGFDGWEKATIRTHYYDGVTHFIRPKFSGSNSKALETSKVNTFGKWKRNQYGTYYRNENGTFTCGFLPIFARVGSPKLSEPNGYWFQPNGYTPYNEVCLSDGYVWIGYNWQGTRYYLPVRQWNGKTGNSYSVGIPWGVFS
Physico‐chemical
properties
protein length:250 AA
molecular weight:28516,00000 Da
isoelectric point:8,76965
aromaticity:0,18400
hydropathy:-0,57880

Domains

Domains [InterPro]
IPR003646
164–229
IPR003646 IPR007921
IPR038765
20–139
IPR038765
IPR007921
4–134
IPR007921
Protein sequence: A0AAX4FYY2
1 250
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage vB_SauP-V4SA02
[NCBI] 		3090829 Rountreeviridae > Rosenblumvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
WOZ17249.1 [NCBI]
Genbank nucleotide accession
OR602701 [NCBI]
CDS location
range 9994 -> 10746
strand -
CDS
ATGAAATCACAACAACAAGCAAAAGAATGGATATATAAGCATGAGGGGGCAGGTGTTGACTTTGATGGTGCATATGGATTTCAATGTATGGACTTATCAGTTGCTTATGTGTATTACATTACTGACGGTAAAGTTCGCATGTGGGGTAATGCTAAAGACGCGATAAATAATGACTTTAAAGGTTTAGCGACGGTGTATAAAAATACACCGAGCTTTAAACCTCAATTAGGGGACGTTGCTGTATATACAAATGGACAATATGGACATATTCAATGTGTGTTAAGTGGAAATCTTGATTATTATACATGCTTAGAACAAAACTGGTTAGGCGGCGGTTTTGACGGTTGGGAAAAAGCAACCATTAGAACACATTATTATGACGGTGTAACTCACTTTATTAGACCTAAATTTTCAGGTAGTAATAGCAAAGCATTAGAAACATCAAAAGTAAATACATTTGGAAAATGGAAACGAAACCAATACGGCACATATTATAGAAATGAAAATGGTACATTTACATGTGGTTTTTTACCAATATTTGCACGTGTCGGTAGTCCAAAATTATCAGAACCTAATGGCTATTGGTTCCAACCAAACGGTTATACACCATATAACGAAGTTTGTTTATCAGATGGTTACGTATGGATTGGTTATAACTGGCAAGGCACACGTTATTATTTACCAGTGCGCCAATGGAATGGAAAAACAGGTAATAGTTACAGTGTTGGTATTCCTTGGGGGGTGTTCTCATAA

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.