Protein

UniProt accession
A0AAX4M0B1 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MKSQQQAKEWIYKHEGAGVDFDGTYGFQCMDLAVAYIYYITDGKVRMWGNAKDAINNDFKGLATVYENTPSFKPQLADVAVYTNSQYGHIQCVISGNLDYYTCLEQNWLGGGFDGWEKATIRTHYYDGVTHFIRPKFSASNSNVLETSKVNTFGNWKQNQYGTYYRNENATFTCGFLPIFARVGSPKLSEPNGYWFQPNGYTPYDEVCLSDGYVWIGYNWQGTRYYLPVRKWNGKTGNSYSVGIPWGVFS
Physico‐chemical
properties
protein length:250 AA
molecular weight:28590,00000 Da
isoelectric point:6,88095
aromaticity:0,18400
hydropathy:-0,53280

Domains

Domains [InterPro]
IPR038765
20–138
IPR038765 IPR003646
IPR007921
4–134
IPR007921
IPR007921
22–107
IPR007921
Protein sequence: A0AAX4M0B1
1 250
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage 4086-1
[NCBI] 		3135592 Rountreeviridae > Rosenblumvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
WYA77323.1 [NCBI]
Genbank nucleotide accession
PP541615 [NCBI]
CDS location
range 11484 -> 12236
strand -
CDS
ATGAAATCACAACAACAAGCAAAAGAATGGATATATAAGCATGAGGGTGCAGGTGTTGACTTTGATGGTACATATGGATTTCAATGTATGGACTTAGCAGTTGCTTATATATATTACATTACAGACGGTAAAGTTCGTATGTGGGGTAACGCCAAAGATGCGATTAATAATGACTTTAAAGGTTTAGCGACGGTGTATGAAAACACACCGAGCTTTAAACCTCAATTAGCTGATGTTGCAGTATACACAAATTCTCAATATGGACATATCCAATGTGTAATAAGTGGAAATCTTGATTATTATACATGTCTAGAACAAAACTGGTTAGGTGGTGGCTTTGACGGTTGGGAAAAAGCAACAATAAGAACACATTATTATGACGGTGTAACACACTTTATTAGACCTAAATTTTCTGCTAGTAATAGTAATGTATTAGAAACATCAAAAGTAAATACATTTGGAAATTGGAAACAAAACCAATACGGAACATATTACAGAAATGAAAATGCCACATTTACATGTGGATTTTTACCAATATTTGCACGTGTAGGTAGTCCTAAATTAAGTGAACCTAATGGATATTGGTTCCAACCAAATGGTTATACACCATATGACGAAGTTTGTTTATCAGATGGGTATGTATGGATTGGTTACAACTGGCAAGGTACACGTTATTATTTACCAGTAAGAAAATGGAACGGTAAAACGGGTAATAGTTATAGTGTTGGTATTCCTTGGGGGGTGTTCTCATAA

Gene Ontology

Description Category Evidence (source)
GO:0001897 symbiont-mediated cytolysis of host cell Biological process Inferred from Electronic Annotation (InterPro)
GO:0003824 catalytic 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.