Protein
- UniProt accession
- A0EWV1 [UniProt]
- Protein name
- N-acetylmuramoyl-L-alanine amidase
- PhaLP type
-
endolysin
evidence: GO annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MQAKLTKKEFIEWLKTSEGKQFNIDLWYAFQCFDYANAGWKALFGLLLKGVGAKDIPFANNFDGLATVYQNTPDFLAQPGDMVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDGIEQPGWGWEKVTRRQHAYDFPMWFIRPNFKSETAPRSVQSPTQAPKKETAKPQPKAVELKIIKDVVKGYDLPKRGSNPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRLEAGIAHSYVSGNTVWQALDESQVGWHTANQIGNKYYYGIEVCQSMGADNATFLKNEQATFQECARLLKKWGLPANRNTIRLHNEFTSTSCPHRSSVLHTGFDPVTRGLLPEDKRLQLKDYFIKQIRAYMDGKIPVATVSNESSASSNTVKPVASAWKRNKYGTYYMEESARFTNGNQPITVRKVGPFLSCPVGYQFQPGGYCDYTEVMLQDGHVWVGYTWEGQRYYLPIRTWNGSSPPNQILGDLWGEIS
- Physico‐chemical
properties -
protein length: 481 AA molecular weight: 54046,00000 Da isoelectric point: 8,73252 aromaticity: 0,12890 hydropathy: -0,47152
Domains
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Dubowvirus NM2 [NCBI] |
387908 | Dubowvirus > |
Host |
Staphylococcus [NCBI] |
1279 | Bacteria > Firmicutes > Bacilli > Bacillales > Staphylococcaceae > |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
ABF73160.1
[NCBI]
Genbank nucleotide accession
DQ530360
[NCBI]
CDS location
range 41027 -> 42472
strand +
strand +
CDS
ATGCAAGCAAAATTGACTAAAAAAGAGTTTATAGAGTGGTTGAAAACTTCTGAGGGAAAACAATTTAATATCGACCTTTGGTATGCATTTCAATGCTTTGATTATGCTAATGCTGGTTGGAAAGCTTTGTTTGGATTACTCCTAAAAGGTGTAGGCGCAAAAGATATTCCGTTCGCTAACAACTTCGACGGATTAGCTACTGTATACCAAAATACACCGGACTTCTTAGCACAACCTGGCGACATGGTGGTATTCGGTAGCAACTACGGTGCTGGATATGGTCACGTTGCATGGGTAATTGAAGCAACTTTAGATTACATCATTGTATATGAGCAGAATTGGCTAGGCGGTGGCTGGACTGACGGAATCGAACAACCCGGCTGGGGTTGGGAAAAAGTTACAAGACGACAACATGCTTATGATTTCCCTATGTGGTTTATCCGTCCGAATTTTAAAAGTGAGACAGCGCCACGATCAGTTCAATCTCCTACACAAGCACCTAAAAAAGAAACAGCTAAGCCACAACCTAAAGCAGTAGAACTTAAAATCATCAAAGATGTGGTTAAAGGTTATGACCTACCTAAGCGTGGTAGTAACCCTAAAGGTATAGTTATACACAACGACGCAGGGAGCAAAGGGGCGACTGCTGAAGCATATCGTAACGGATTAGTAAATGCACCTTTATCAAGATTAGAAGCGGGCATTGCGCATAGTTACGTATCAGGCAACACAGTTTGGCAAGCCTTAGATGAATCACAAGTAGGTTGGCATACCGCTAATCAAATAGGTAATAAATATTATTACGGTATTGAAGTATGTCAATCAATGGGCGCAGATAACGCGACATTCTTAAAAAATGAACAGGCAACTTTCCAAGAATGTGCTAGGTTATTAAAAAAGTGGGGATTACCAGCAAACAGAAATACAATCAGATTGCACAATGAATTTACTTCAACATCATGCCCTCATAGAAGTTCGGTTTTACACACTGGTTTTGACCCAGTAACTCGCGGTCTATTGCCAGAAGACAAGCGGTTGCAACTTAAAGACTACTTTATCAAGCAGATTAGGGCGTACATGGATGGTAAAATACCGGTTGCCACTGTCTCTAATGAGTCAAGCGCTTCAAGTAATACAGTTAAACCAGTTGCGAGTGCATGGAAACGTAATAAATATGGTACTTACTACATGGAAGAAAGTGCTAGATTCACAAACGGCAATCAACCAATCACAGTAAGAAAAGTGGGGCCATTCTTATCTTGTCCAGTGGGTTATCAGTTCCAACCTGGTGGATATTGTGATTATACAGAAGTGATGTTACAAGATGGTCATGTTTGGGTAGGATATACATGGGAGGGGCAACGTTATTACTTGCCTATTAGAACATGGAATGGTTCTTCCCCACCTAATCAGATATTAGGTGACTTATGGGGAGAAATCAGTTAG
Gene Ontology
Description | Category | Evidence (source) | |
---|---|---|---|
GO:0001897 | symbiont-mediated cytolysis of host cell | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0006508 | proteolysis | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0008233 | peptidase activity | Molecular function | 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:0042742 | defense response to bacterium | Biological process | Inferred from Electronic Annotation (UniProt) |
GO:0046872 | metal ion binding | Molecular function | 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.