Protein

UniProt accession
A0AB39CF83 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: ML prediction

probability: 99 % (predicted by ML model)

Protein sequence
MRFIPAAHHSAGSNSPVNRVVIHATCPDVGFPSASRKGRAVSTANYFASPSSGGSAHYVCDIGETVQCLSESTIGWHAPPNPHSLGIEICADGGSHASFRVPGHAYTREQWLSPQVWPAVEKAAILCRRLCDKYNVPKRKLSAADLKAGRRGVCGHADVTDAWHQSDHDDPGPWFPWDRFMAVVNGGSGSEELTVADVKALHDQIKQLSAQLTGSVNKLHHDVGVVQVQNGDLGKRVDALSWVKNPVTGKLWRTKDALWSVWYYVLECRSRISRLESAVNDLKK
Physico‐chemical
properties
protein length:284 AA
molecular weight:31018,00000 Da
isoelectric point:8,75515
aromaticity:0,07746
hydropathy:-0,35106

Domains

Domains [InterPro]

No domain annotations available.

Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Cutibacterium phage vB_CacS-HV1
[NCBI] 		3236917 Pahexavirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
XDJ26094.1 [NCBI]
Genbank nucleotide accession
PQ037195 [NCBI]
CDS location
range 15035 -> 15889
strand +
CDS
GTGAGGTTTATTCCTGCGGCGCATCATTCTGCCGGTTCTAATTCTCCGGTGAATAGGGTTGTGATTCATGCGACGTGCCCGGATGTGGGGTTTCCGTCCGCGTCCCGTAAGGGTAGGGCGGTGTCTACAGCGAACTATTTTGCTTCCCCATCGTCTGGTGGTTCTGCGCACTATGTGTGCGATATTGGGGAGACGGTGCAGTGCCTGTCTGAGTCTACGATTGGTTGGCATGCCCCGCCGAATCCGCATAGTTTGGGTATAGAGATTTGCGCGGATGGGGGTTCGCACGCCTCGTTTAGGGTGCCAGGGCATGCTTACACTCGGGAGCAGTGGCTGTCCCCGCAGGTGTGGCCCGCGGTGGAGAAGGCCGCCATCCTGTGTAGACGTTTGTGTGACAAATATAATGTTCCGAAGAGGAAGCTTAGTGCAGCCGATTTGAAGGCTGGCAGGCGGGGTGTGTGCGGGCATGCGGATGTTACGGATGCGTGGCATCAGTCGGATCATGATGATCCGGGGCCGTGGTTTCCGTGGGACAGGTTTATGGCCGTTGTCAACGGCGGTAGTGGTAGTGAGGAGTTAACGGTGGCTGATGTGAAAGCCTTACATGATCAGATTAAACAATTGTCTGCTCAGCTTACTGGTTCGGTGAATAAGCTGCACCATGATGTTGGTGTGGTACAGGTGCAGAATGGTGATTTGGGTAAACGTGTTGATGCCCTGTCGTGGGTGAAGAATCCGGTAACCGGGAAGCTGTGGCGCACCAAGGACGCCCTGTGGAGTGTCTGGTATTACGTGTTGGAGTGTCGCAGCCGCATCAGTAGGCTTGAGTCTGCTGTCAACGATTTAAAGAAGTGA

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.