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
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 +
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.