Protein

UniProt accession
A0AAX4PPI7 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAGEVFSSLITSVNPNPMNAGSRNGIPIDTIILHHNATTNKDVAMNTWLLGGGAGTSAHYECTPTEIIGCVGEQYSAFHAGGTGGIDVPKIANPNQRSIGIENVNSSGAPNWSVDPRTITNCARLVADICTRYGIPCDRQHVLGHNEVTATACPGGMDVDEVVRQAQQFMAGGSNNAVKPEPSKPTPSKPSNNKNKEGVATMYCLYERPINSKTGVLEWNGDAWTVMFCNGVNCRRVSHPDEMKVIEDIYRKNNGKDIPFYSQKEWNKNAPWYNRLETVCPVVGITKKS
Physico‐chemical
properties
protein length:289 AA
molecular weight:31366,00000 Da
isoelectric point:7,01964
aromaticity:0,06574
hydropathy:-0,45813

Domains

Domains [InterPro]
Protein sequence: A0AAX4PPI7
1 289
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Enterococcus phage vB_Efs8_KEN04
[NCBI]
3138311 Herelleviridae > Kochikohdavirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
WZP34868.1 [NCBI]
Genbank nucleotide accession
PP582180 [NCBI]
CDS location
range 48525 -> 49394
strand +
CDS
ATGGCAGGAGAAGTATTTAGTAGCTTGATTACAAGTGTAAATCCTAACCCAATGAACGCAGGTAGTCGTAATGGTATCCCTATCGACACCATTATCCTACATCACAATGCAACAACAAATAAAGATGTTGCTATGAACACATGGCTATTAGGCGGTGGCGCAGGTACATCTGCTCATTATGAATGTACACCAACAGAAATTATTGGATGTGTCGGTGAGCAGTATTCAGCATTCCATGCCGGAGGTACAGGTGGTATAGACGTTCCTAAGATTGCTAACCCTAATCAACGTTCAATAGGTATTGAAAATGTAAACTCGTCAGGAGCACCTAATTGGTCTGTAGACCCTAGAACAATTACAAATTGTGCTCGTTTAGTGGCAGATATTTGTACACGTTATGGTATTCCATGTGACCGACAACATGTGTTAGGACATAACGAAGTAACTGCAACAGCATGTCCCGGAGGTATGGATGTAGACGAAGTTGTACGTCAAGCTCAACAGTTCATGGCAGGAGGCTCTAACAATGCAGTTAAGCCGGAGCCAAGTAAGCCTACACCAAGCAAACCAAGTAATAATAAAAATAAAGAAGGAGTGGCAACTATGTATTGTTTATACGAAAGACCTATTAACTCAAAAACAGGAGTATTAGAGTGGAATGGTGATGCATGGACAGTTATGTTTTGTAATGGGGTAAACTGTCGCAGAGTATCTCATCCAGATGAAATGAAAGTAATTGAGGATATTTACAGAAAAAATAACGGAAAAGACATTCCATTTTACAGTCAAAAAGAATGGAATAAAAATGCACCATGGTACAACAGATTAGAGACAGTATGTCCAGTAGTAGGTATTACTAAAAAATCTTAA

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)
GO:0009253 peptidoglycan catabolic process Biological process Inferred from Electronic Annotation (InterPro)
GO:0009254 peptidoglycan turnover Biological process Inferred from Electronic Annotation (TreeGrafter)
GO:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation (UniProt)
GO:0071555 cell wall organization Biological process 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.