Protein
- UniProt accession
- A0A097PAT3 [UniProt]
- Protein name
- N-acetylmuramoyl-L-alanine amidase
- PhaLP type
-
endolysin
evidence: GO annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MATVSEVISYWRGLADTNQGYDADLAWGWQCADVTNGTTTNFFGVTLWGNAIDLLDSAKAQGLEVIYDAPGINPKAGDLFVMYTYAHPYGHTGIVIADSDGYTIQTIEQNVDGYSDNNGDGINDQFQVGGPARYVTRAFSDGDGYIVGWIRPPYSDTSSEKQSQSQAPSGFRKLKDEVGTFEVMVPALNVRREPSLNGEIVACYQYGMTGTYDSVYVGDGYIWVSYVGASGMRNYMAVGDADGDYNVNPYCKFY
- Physico‐chemical
properties -
protein length: 254 AA molecular weight: 27772,00000 Da isoelectric point: 4,18872 aromaticity: 0,13780 hydropathy: -0,31772
Domains
Domains [InterPro]
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Streptococcus pyogenes phage T12 (Bacteriophage T12) [NCBI] |
35344 | No lineage information |
Host |
Streptococcus pyogenes [NCBI] |
1314 | Bacteria > Firmicutes > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
AIU44402.1
[NCBI]
Genbank nucleotide accession
KM289195
[NCBI]
CDS location
range 33491 -> 34255
strand +
strand +
CDS
ATGGCAACAGTTAGCGAAGTAATTAGCTATTGGCGTGGATTAGCTGATACAAATCAAGGTTATGATGCCGACCTTGCGTGGGGCTGGCAATGTGCTGATGTGACTAATGGGACAACTACTAACTTTTTTGGAGTGACGCTTTGGGGGAATGCGATTGACTTGCTAGACAGTGCAAAGGCGCAAGGGTTAGAGGTTATCTATGACGCCCCTGGAATAAATCCCAAAGCTGGTGATTTGTTTGTTATGTACACTTATGCTCATCCTTATGGTCATACAGGAATTGTGATTGCTGATAGTGATGGTTATACTATCCAAACAATTGAGCAAAATGTAGATGGATACTCAGATAATAATGGAGATGGCATTAATGACCAGTTCCAAGTTGGCGGACCAGCACGATATGTCACTCGTGCCTTTTCAGACGGTGACGGTTATATTGTCGGTTGGATTAGACCGCCTTATAGCGATACCTCATCTGAAAAGCAATCACAATCACAAGCGCCATCAGGATTCCGGAAATTAAAAGACGAGGTCGGAACATTTGAGGTTATGGTCCCAGCGCTAAACGTTCGCCGTGAACCAAGCTTAAATGGCGAGATTGTAGCTTGTTACCAATACGGCATGACAGGAACTTATGATTCTGTCTATGTTGGCGATGGGTATATTTGGGTGTCTTATGTCGGTGCATCTGGCATGAGAAATTATATGGCTGTTGGAGACGCTGATGGCGATTACAATGTCAATCCATATTGTAAATTTTATTAA
Gene Ontology
Description | Category | Evidence (source) | |
---|---|---|---|
GO:0001897 | symbiont-mediated cytolysis of host cell | Biological process | Inferred from Electronic Annotation (InterPro) |
GO:0003824 | catalytic activity | Molecular function | Inferred from Electronic Annotation (InterPro) |
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.