Protein
- UniProt accession
- A0A067XGV1 [UniProt]
- Protein name
- N-acetylmuramoyl-L-alanine amidase
- PhaLP type
-
endolysin
evidence: GO annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
METYSNLTTSVNQNAMYCEPRQGRIEYIILHHNATTNKNVAMSTWYTTSGNWTSAHYEITDNEIIGCVGENYTAYHAGGTGGSDVPTIPNVNHRSIGLEHVNSSGAPYWSVSDATLRNSAKLIVDICNRYGLSINRNTIKGHNEVTATACPGGINVNKVVKMAQELANGKQPESPKPPLPTPKKEDDKMFIYLKKQKNGNTEQWFVCGDKRMYLPTMTYVNEANALIKRYGGSTNQTVYNHDNFGLKMIEKAYTEVKV
- Physico‐chemical
properties -
protein length: 258 AA molecular weight: 28736,00000 Da isoelectric point: 8,46355 aromaticity: 0,08527 hydropathy: -0,60659
Domains
Taxonomy
Name | Taxonomy ID | Lineage | |
---|---|---|---|
Phage |
Enterococcus phage vB_Efae230P-4 [NCBI] |
1161939 | Rountreeviridae > Copernicusvirus > Copernicusvirus Efae230P4 |
Host |
Enterococcus faecium [NCBI] |
1352 | Bacteria > Firmicutes > Bacilli > Lactobacillales > Enterococcaceae > Enterococcus |
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
AFF27942.1
[NCBI]
Genbank nucleotide accession
JQ309827
[NCBI]
CDS location
range 8318 -> 9094
strand +
strand +
CDS
ATGGAGACTTATTCTAATTTAACAACAAGCGTTAATCAAAACGCTATGTATTGTGAACCTCGTCAAGGAAGAATAGAATACATCATTCTTCATCACAACGCAACAACAAACAAGAATGTTGCAATGTCAACATGGTACACAACCTCAGGAAATTGGACCTCCGCTCATTATGAAATTACAGATAATGAAATTATCGGGTGTGTTGGTGAGAATTACACCGCTTATCACGCTGGAGGAACTGGAGGGAGTGACGTTCCAACCATTCCTAATGTTAACCATCGTTCTATTGGTTTAGAACACGTAAACAGCTCAGGAGCACCTTATTGGAGCGTTAGTGATGCAACACTTAGAAATAGCGCTAAATTGATTGTAGATATTTGTAATCGTTACGGTTTGTCAATTAACAGAAACACTATTAAAGGCCACAACGAAGTCACAGCTACGGCATGCCCTGGAGGTATCAACGTTAACAAAGTTGTAAAAATGGCACAAGAATTAGCAAACGGTAAACAACCAGAATCACCAAAACCACCACTACCAACACCAAAGAAAGAGGATGATAAAATGTTTATTTATTTAAAAAAACAAAAGAACGGAAATACAGAACAATGGTTTGTATGCGGAGATAAACGCATGTACTTACCAACTATGACTTATGTAAATGAAGCAAACGCCTTAATTAAACGTTACGGAGGGTCTACAAACCAAACAGTATACAATCATGACAACTTTGGTTTAAAAATGATCGAGAAAGCTTATACAGAAGTTAAAGTATAA
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.