Protein

UniProt accession
A0AAD1PU32 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MLKDKARVVENTLSYIPKPGTMVIFNNSYGCGHGHVAWVLSANQNQIIVIENNWLGGGWTWGDAQGGGGWEKATIRAHGYDFPMWFIEPNFKDDVQTTWNWRGKFTADRTIKVRRTPGLSGSIVGAESFIYSGQYVNFDQVIKADGYWWIRFKYPTNPSAGNFYMAVCKITDKWERMLKEKYWGRINWK
Physico‐chemical
properties
protein length:189 AA
molecular weight:21819,00000 Da
isoelectric point:9,39312
aromaticity:0,16402
hydropathy:-0,46878

Domains

Domains [InterPro]
IPR003646
129–153
IPR003646 IPR007921
IPR007921
14–53
IPR007921
IPR038765
8–94
IPR038765
Protein sequence: A0AAD1PU32
1 189
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage phiRNIID
[NCBI] 		3092518 Herelleviridae > Silviavirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
BEU75234.1 [NCBI]
Genbank nucleotide accession
LC788703 [NCBI]
CDS location
range 14978 -> 15547
strand +
CDS
ATGTTAAAAGATAAAGCTAGAGTAGTAGAAAATACACTATCCTACATTCCTAAACCAGGCACTATGGTTATCTTTAATAATTCATACGGGTGTGGTCATGGTCATGTCGCATGGGTACTAAGTGCAAACCAAAACCAAATTATAGTAATTGAAAATAATTGGTTAGGTGGAGGTTGGACTTGGGGAGATGCTCAAGGAGGCGGTGGCTGGGAAAAAGCTACTATTAGAGCCCATGGTTACGACTTTCCTATGTGGTTTATAGAACCTAATTTCAAAGACGATGTACAAACAACTTGGAATTGGAGAGGTAAATTTACTGCTGATAGAACGATTAAGGTAAGACGAACACCAGGTTTAAGTGGTTCAATCGTAGGAGCTGAATCATTTATTTATAGTGGTCAATATGTAAACTTTGACCAAGTTATTAAAGCAGATGGCTATTGGTGGATTAGATTTAAATATCCTACAAACCCGTCAGCTGGGAACTTCTATATGGCAGTATGTAAAATCACTGACAAGTGGGAACGTATGCTAAAAGAGAAGTATTGGGGTCGTATTAATTGGAAATAA

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.