Protein
- Protein accession
- A0AAF0A405 [UniProt]
- Representative
- 1kAuJ
- Source
- UniProt (cluster: phalp2_29719)
- Protein name
- N-acetylmuramoyl-L-alanine amidase
- Lysin probability
- 100%
- PhaLP type
-
endolysin
Probability: 99% (predicted by ML model) - Protein sequence
-
MKIDHIPCNRANYYTSGRSLDSIKYIVIHYTANNGDTARGNAKYFARESVGASANYFVDPNEVICSVKDEYAAWHCGGSLESSHHPLRGICTNKNSIGVELCSIIQNGKYEFKPETIKLAAKFVKELMAKYNIDIDHVVRHYDVTGKNCPAPFVYSEEQWKQFKQMLISKEEEETMSYEQWLAYQKRYEQEKANQHVSDYAKSAMEKAVKHGISDGSNPKSHCTREQVVVMLDRAGIL
- Physico‐chemical
properties -
protein length: 238 AA molecular weight: 27118,3 Da isoelectric point: 7,13 hydropathy: -0,60
Representative Protein Details
- Accession
- 1kAuJ
- Protein name
- 1kAuJ
- Sequence length
- 844 AA
- Molecular weight
- 92804,87940 Da
- Isoelectric point
- 7,70813
- Sequence
-
LEDNVNIIKNTNFTAYRNCRERVEKVKYIVIHYTGGEGTAADQVKYFNNGNRSASAHYFVDRSGEIREYCDPKKWYAWHCGGSLESSHHPYYGKCTNSNSIGVEICTHNNGKTWEFTKEAVAAAKELTKYLMKEYDVSADNVIRHYDVTGKSCPRVPGWGAVGGNAEWEKFKKALGAETVDTPATEKKKWYRVRKSWDDAASQIGAYLILDNAIAEANNSGPKYAVYDWTGKEIYRYVEASGTKEKEIRFFYPGYTRTSSPDDRQGAGCVWHDQHKNCFVYDAYQKNTDAGNNLIQYILDNGLRSIDGCGSHAHGDHLGGFFKMLESGKITIENFYCYDPDSLKLAGTGSANARSAKEDKEYLQSLIDKLKARGTKIHFVKTGDTIVCGEMVFEVCRNQPASFGQYDTGKAWGYLNDGSINLYERACHVLLCGDGGGRKAAQYFNGDIDVCESEHHGNGDGSGKVEEVKSRGCGLAIECNNEKNGPGSCGFTQYGARRFKEAGIPVWMLNADINGIAKGGKLTVTQGSGSKTFDVPFGLVFYRVRKSWADAGSQIGAYTILDKAKECADQHPGYIVFDETGKAVYPVEGSGAAPEPAATKPKTEQEIFIETVGTMARDDMAKNGILACITIAQAILESGWGTSELAVNAKNLFGMKKSLSGNTWSGSTWGGKSYSKLTQEVYTSGPAVVRADFRAYESWAESVGDHSAYLAGAKNGSRLRYAGLIGCTDYRKAAQIIKDGDYATAPDYVEKLCKLIEQYNLTEWNSVAAVPAGSGALDEYHTVKWTGMTKRACSGYMYPDARSKVTVEVHQGVKAGVCKGIGKFYLCKVDDTYGYIHKSHITKL
Other Proteins in cluster: phalp2_29719
| Total (incl. this protein): 6 | Avg length: 530,3 | Avg pI: 7,50 |
|
|
||
| Protein ID | Length (AA) | pI |
|---|---|---|
| 1kAuJ | 844 | 7,70813 |
| 2VjBz | 786 | 9,11140 |
| 3iBYE | 838 | 7,06136 |
| A0A2K9V347 | 238 | 6,83696 |
| A0AAE9UUR2 | 238 | 7,12758 |
Similar Clusters (pHMM search)
| # | Cluster | # Members | Identity (%) | Alignment Length | E-value |
|---|---|---|---|---|---|
| 1 |
phalp2_28540
41m0Z
|
1 | 34,0% | 690 | 1.044E-101 |
| 2 |
phalp2_15411
21scl
|
1 | 28,1% | 750 | 3.013E-63 |
Domains
Domains [InterPro]
1
844 AA (representative)
Domain positions follow the representative sequence above; the member sequence bar is scaled to the same axis.
Legend:
EAD
CBD
Linker
Disordered
Unannotated
Taxonomy
| Name | Taxonomy ID | Lineage | |
|---|---|---|---|
| Phage |
Agathobaculum phage AB434P2 [NCBI] |
2968527 | No lineage information |
| Host | No host information | ||
Coding sequence (CDS)
Coding sequence (CDS)
CDS Source ID
CDS Source
OP172633
[NCBI]
CDS location
range 41240 -> 41956
strand +
strand +
CDS
ATGAAGATTGATCATATTCCTTGCAATAGAGCTAATTATTATACCTCTGGAAGAAGTCTGGATTCTATAAAGTATATAGTTATTCATTACACGGCAAATAATGGCGATACAGCACGTGGCAATGCAAAATACTTTGCAAGAGAAAGTGTAGGAGCTTCTGCTAACTACTTTGTTGATCCAAACGAAGTTATTTGTTCTGTAAAGGATGAATATGCAGCATGGCATTGTGGCGGATCTCTTGAGAGTAGCCATCATCCATTAAGAGGAATCTGTACTAATAAGAATTCCATTGGTGTAGAACTTTGCTCTATAATTCAAAATGGTAAATATGAATTTAAGCCAGAAACTATAAAGCTTGCAGCTAAGTTTGTAAAGGAACTAATGGCAAAATATAATATTGATATTGACCACGTAGTTCGGCATTATGATGTAACAGGTAAAAATTGTCCCGCTCCATTTGTTTATAGTGAAGAACAATGGAAACAATTTAAGCAAATGCTTATTAGTAAGGAGGAAGAAGAAACTATGAGTTATGAGCAATGGTTAGCATATCAAAAGAGATATGAGCAAGAAAAGGCAAATCAACATGTTTCTGATTATGCTAAGTCTGCTATGGAAAAGGCAGTAAAACATGGTATTTCTGACGGATCTAATCCTAAGTCCCATTGCACACGAGAACAAGTAGTAGTTATGCTGGATCGTGCAGGAATCCTCTAA
Gene Ontology
| Description | Category | Evidence (source) | |
|---|---|---|---|
| GO:0001897 | symbiont-mediated cytolysis of host cell | biological process | None (UniProt) |
| GO:0008745 | N-acetylmuramoyl-L-alanine amidase activity | molecular function | None (UniProt) |
| GO:0009253 | peptidoglycan catabolic process | biological process | None (UniProt) |
| GO:0009254 | peptidoglycan turnover | biological process | None (UniProt) |
| GO:0042742 | defense response to bacterium | biological process | None (UniProt) |
| GO:0071555 | cell wall organization | biological process | None (UniProt) |
Enzymatic activity
| EC Number | Entry Name | Reaction Catalyzed | Classification | Evidence | Source |
|---|---|---|---|---|---|
| 3.5.1.28 | None | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. |
match to sequence model evidence used in automatic assertion
ECO:ECO:0000256 |
ARBA:ARBA00001561 |
Tertiary structure
No tertiary structures available for this protein.
The structures below correspond to the cluster representative
(1kAuJ)
rather than this protein.
Model Confidence
Very high
pLDDT > 90
pLDDT > 90
High
90 > pLDDT > 70
90 > pLDDT > 70
Low
70 > pLDDT > 50
70 > pLDDT > 50
Very low
pLDDT < 50
pLDDT < 50