Protein

UniProt accession
A8E261 [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]
IPR002502
27–157
IPR002502
IPR036505
14–174
IPR036505
IPR002502
18–155
IPR002502
IPR051206
23–167
IPR051206
IPR002502
26–155
IPR002502
IPR036505
18–157
IPR036505
Protein sequence: A8E261
1 289
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Enterococcus phage phiEF24C (Enterococcus bacteriophage phi-EF24C)
[NCBI] 		442493 Herelleviridae > Kochikohdavirus > Kochikohdavirus EF24C
Host Enterococcus faecalis
[NCBI] 		1351 Bacteria > Firmicutes > Bacilli > Lactobacillales > Enterococcaceae > Enterococcus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
BAF81277.1 [NCBI]
Genbank nucleotide accession
AP009390 [NCBI]
CDS location
range 5409 -> 6278
strand +
CDS
ATGGCAGGAGAAGTATTTAGTAGCTTGATTACAAGTGTAAATCCTAACCCAATGAACGCAGGTAGTCGTAATGGTATCCCTATCGACACCATTATCCTACATCACAATGCAACAACAAATAAAGATGTTGCTATGAACACATGGCTATTAGGTGGTGGCGCAGGTACATCTGCTCATTATGAATGTACACCAACAGAAATTATTGGATGTGTCGGTGAGCAGTATTCAGCATTCCATGCCGGAGGTACAGGTGGTATAGATGTTCCTAAGATTGCTAACCCTAACCAACGTTCAATAGGTATTGAAAATGTAAACTCGTCAGGAGCACCTAATTGGTCTGTAGACCCTAGAACAATTACAAATTGTGCTCGTTTAGTGGCAGATATTTGTACACGTTATGGTATTCCATGTGACCGACAACACGTGTTAGGACATAACGAAGTAACTGCAACAGCGTGCCCCGGAGGTATGGACGTAGACGAAGTTGTACGTCAAGCTCAACAGTTCATGGCAGGAGGCTCTAACAATGCAGTTAAGCCGGAGCCAAGTAAGCCTACACCAAGCAAACCAAGTAATAATAAAAATAAAGAAGGAGTGGCAACTATGTATTGTTTATACGAAAGACCTATTAACTCAAAAACAGGAGTACTAGAGTGGAATGGTGATGCATGGACAGTTATGTTCTGTAATGGGGTAAACTGTCGCAGAGTATCTCATCCAGATGAAATGAAAGTAATTGAGGATATTTACAGAAAAAATAACGGAAAAGACATTCCATTTTACAGTCAAAAAGAATGGAATAAAAATGCACCATGGTATAACAGATTAGAGACAGTATGTCCAGTAGTAGGTATTACTAAAAAATCTTAA

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.