Protein

UniProt accession
Q2I8E6 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MEIQKKLVDPSKYGTKCPYTMKPKYITVHNTYNDAPAENEVSYMISNNNEVSFHIAVDDKKAIQGIPLERNAWACGDGNGSGNRQSISVEICYSKSGGDRYYKAEDNAVDVVRQLMSMYNIPIENVRTHQSWSGKYCPHRMLAEGRWGAFIQKVKNGNVATTSPTKQNIIQSGAFSPYETPDVMGALTSLKMTADFILQSDGLTYFISKPTSDAQLKAMKEYLDRKGWWYEVK
Physico‐chemical
properties
protein length:233 AA
molecular weight:26267,00000 Da
isoelectric point:8,50926
aromaticity:0,10300
hydropathy:-0,59485

Domains

Domains [InterPro]
Protein sequence: Q2I8E6
1 233
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage Fah
[NCBI]
345922 Wbetavirus >
Host Bacillus anthracis
[NCBI]
1392 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus
Host Bacillus cereus
[NCBI]
1396 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ABA42708.1 [NCBI]
Genbank nucleotide accession
DQ150593 [NCBI]
CDS location
range 17646 -> 18347
strand +
CDS
ATGGAAATCCAAAAAAAATTAGTTGATCCAAGTAAGTATGGTACAAAGTGTCCGTATACAATGAAGCCTAAATATATCACTGTTCACAACACATATAATGATGCTCCAGCTGAAAATGAAGTGAGTTACATGATTAGTAACAATAATGAGGTGTCGTTTCATATTGCAGTAGATGACAAGAAAGCGATTCAAGGTATTCCGTTGGAACGTAATGCATGGGCTTGCGGAGACGGCAATGGTTCGGGGAATCGTCAATCCATTTCTGTAGAAATCTGTTATTCAAAATCAGGAGGAGATAGATACTATAAAGCTGAGGATAATGCTGTTGATGTTGTACGACAACTTATGTCTATGTACAATATTCCGATTGAAAATGTTCGAACTCATCAATCCTGGTCAGGTAAATATTGTCCGCATAGAATGTTAGCTGAGGGAAGGTGGGGAGCATTCATTCAGAAGGTTAAGAATGGGAATGTGGCGACTACTTCACCAACAAAACAAAACATCATCCAATCAGGGGCTTTCTCACCGTATGAAACCCCTGATGTTATGGGAGCATTAACGTCACTTAAAATGACAGCTGATTTTATCTTACAATCGGATGGATTAACTTATTTTATTTCCAAACCGACTTCAGATGCACAACTAAAAGCAATGAAAGAATACCTTGACCGTAAAGGTTGGTGGTATGAAGTTAAATAA

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:0030420 establishment of competence for transformation Biological process Inferred from Electronic Annotation (InterPro)
GO:0030435 sporulation resulting in formation of a cellular spore 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.