Protein
- UniProt accession
- H7BUY1 [UniProt]
- Protein name
- N-acetylmuramoyl-L-alanine amidase
- PhaLP type
-
endolysin
evidence: GO annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MNADEKIWRYLKSAGLNDFGVAGLMGNLFAESGLNPKNLQNTYEKKLGMTDEEYTAAVDSGSYSNFVKDSAGYGLAQWTYWSRKDALLASCKAAGASVGDMDAQLNFLLKELSVGYSGLLSTLKSAPSVREASNAVLLQFERPANQGQSVQEKRVSYGQAYYDKFAGKIQINTPEQEGGCKLKIVDNLTTVNFRSGNMTPKYIVIHYFGALGTAKSVSEYFKTPGIQASAHYALDEGDTIYRCVRDKDIAWHCGANKYKHPECRNSNSIGIEARPSKINRKRVMASDTDWYFEPKVVDNLVWLTKKLMAQYNIPADHVIRHYDVTGKLCPRPWCCADMNVYYKTSGDAQWEEFKKRISDGKEEDEDMTLDTFKELMREYRAELQDNDCGTWSKEAREWAISNGLINGTGTEVNGEPNYAWADQLTREQAAALFYRFAKLMGKA
- Physico‐chemical
properties -
protein length: 443 AA molecular weight: 49791,00000 Da isoelectric point: 6,36804 aromaticity: 0,11061 hydropathy: -0,56027
Domains
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Bacteriophage sp [NCBI] |
38018 | No lineage information |
Host | No host information |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
AFB75626.1
[NCBI]
Genbank nucleotide accession
JQ680354
[NCBI]
CDS location
range 42307 -> 43638
strand -
strand -
CDS
ATGAACGCCGACGAAAAAATCTGGCGCTATTTGAAATCTGCTGGTCTGAATGATTTCGGCGTCGCGGGTTTGATGGGGAATCTTTTTGCAGAGAGCGGACTGAATCCCAAGAACCTCCAAAATACATACGAGAAGAAACTTGGCATGACTGATGAAGAATATACTGCCGCTGTCGATAGCGGCAGTTATTCCAACTTTGTGAAAGACAGTGCAGGTTACGGATTAGCTCAGTGGACGTACTGGTCACGCAAGGACGCTCTCCTTGCCTCCTGTAAAGCCGCAGGAGCGTCCGTAGGGGACATGGATGCCCAGCTCAACTTCCTGCTTAAAGAGCTGTCTGTGGGCTATTCTGGGCTGCTGAGCACCCTCAAGAGCGCACCGTCTGTCCGTGAGGCATCCAATGCTGTTCTTCTCCAATTTGAACGTCCTGCCAATCAGGGACAGAGCGTCCAAGAAAAACGAGTCAGCTACGGACAAGCTTATTATGACAAGTTTGCTGGCAAAATCCAAATCAATACACCAGAACAGGAAGGAGGATGCAAGTTGAAAATTGTAGACAACCTGACAACGGTTAACTTCCGTTCAGGCAACATGACTCCGAAGTACATCGTCATCCATTATTTCGGTGCACTCGGAACTGCAAAGAGTGTCTCTGAATATTTCAAGACACCGGGTATTCAAGCGTCTGCCCATTATGCGCTTGACGAGGGCGATACCATCTATCGCTGTGTCCGCGATAAGGACATCGCATGGCACTGTGGTGCGAACAAGTACAAGCACCCTGAGTGCCGCAACTCTAACTCCATCGGGATTGAAGCACGCCCTTCCAAAATCAATCGCAAGAGGGTTATGGCTTCTGATACTGATTGGTATTTCGAACCAAAAGTTGTGGACAACCTCGTATGGTTGACAAAGAAGCTGATGGCTCAGTACAACATTCCTGCAGACCACGTTATCCGTCATTATGATGTGACCGGAAAACTCTGTCCGAGACCGTGGTGTTGCGCCGACATGAATGTCTATTACAAGACGAGTGGCGACGCACAGTGGGAAGAGTTCAAAAAGAGAATCAGCGACGGCAAAGAGGAGGATGAAGATATGACTCTGGACACATTCAAGGAACTGATGAGGGAGTACCGTGCAGAGCTGCAGGACAATGACTGCGGCACTTGGAGCAAGGAAGCTCGTGAGTGGGCTATCTCCAACGGTCTCATCAATGGCACTGGCACTGAGGTGAATGGTGAACCCAACTATGCTTGGGCTGACCAGCTTACCCGTGAACAGGCTGCTGCTTTGTTCTATCGTTTTGCAAAACTGATGGGTAAAGCGTGA
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.