Protein

Protein accession
A0A6J5PD09 [UniProt]
Representative
18Jwv
Source
UniProt (cluster: phalp2_15283)
Protein name
N-acetylmuramoyl-L-alanine amidase
Lysin probability
100%
PhaLP type
endolysin
Probability: 97% (predicted by ML model)
Protein sequence
MNITKDHWIESAIRKPLDGGADMPIRRALVMHFTSGATAMSSIEFWVSQWATSRGVCAHIVIDRDGTIYQCRPFNRTAGHAGKSIWTDPNTGVKYHNPNSVTIGIEFANAGDSANAEGKAFGGSFTCPSGSDLARHKNGGPLTYWERFPAVQIEAGKRVAAALIERYNLDDVVGHDDIAPGRKNDPGPLFPMTLFKQLLNK
Physico‐chemical
properties
protein length:201 AA
molecular weight:21939,5 Da
isoelectric point:8,46
hydropathy:-0,35
Representative Protein Details
Accession
18Jwv
Protein name
18Jwv
Sequence length
133 AA
Molecular weight
14520,48000 Da
Isoelectric point
9,46907
Sequence
MKIDENHWIDTAIRVPLPGGNTMGVRRFLVMHFTSGATAMSSINFWKSPDAKGACAHFIIDRNGTLYQCRPCNTTCGHAGKSKWTFGGKTYEGLNSCSIGIEFANAGDSTNLIRRYSTLPPLKARHKNGGPVC
Other Proteins in cluster: phalp2_15283
Total (incl. this protein): 4 Avg length: 179,3 Avg pI: 8,82

Protein ID Length (AA) pI
18Jwv 133 9,46907
A0A6J5NVH6 192 8,23263
A0A6J5RYM2 191 9,11269
Similar Clusters (pHMM search)
# Cluster # Members Identity (%) Alignment Length E-value
1 phalp2_13409
4uFYn
31 33,9% 109 1.004E-15
2 phalp2_1287
HV6K
2 35,8% 120 1.882E-15
3 phalp2_11551
100RI
7 28,1% 135 3.859E-10
4 phalp2_20835
6rXam
1 28,8% 97 5.229E-05

Domains

Domains [InterPro]
Representative sequence (used for alignment): 18Jwv (133 AA)
Member sequence: A0A6J5PD09 (201 AA)
1 133 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
Pfam accessions: PF01510

Taxonomy

  Name Taxonomy ID Lineage
Phage uncultured Caudovirales phage
[NCBI]
2100421 No lineage information
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
CDS Source ID
CDS Source
LR796314 [NCBI]
CDS location
range 19497 -> 20102
strand -
CDS
ATGAACATCACAAAAGACCACTGGATCGAATCGGCGATCAGGAAACCACTTGATGGGGGCGCGGATATGCCAATTCGCAGAGCATTGGTCATGCACTTCACATCCGGCGCGACCGCGATGTCATCCATCGAGTTCTGGGTATCTCAATGGGCAACCTCCCGAGGGGTCTGCGCCCACATTGTGATCGACCGCGATGGGACGATCTACCAGTGCCGCCCCTTCAACCGCACCGCTGGACACGCGGGGAAGTCGATATGGACCGACCCTAATACGGGCGTAAAATATCATAATCCAAACTCAGTCACCATCGGAATCGAGTTCGCGAATGCCGGAGACTCGGCCAACGCGGAAGGCAAGGCGTTCGGCGGCAGCTTCACTTGTCCCTCGGGATCTGACCTTGCCCGGCACAAAAACGGAGGCCCGCTAACATATTGGGAGCGCTTTCCGGCGGTCCAGATTGAGGCTGGAAAGAGGGTTGCAGCAGCATTGATTGAGCGCTACAATCTGGACGACGTAGTGGGGCATGACGACATCGCACCCGGACGGAAGAACGACCCAGGCCCGCTATTTCCAATGACATTATTTAAGCAACTACTAAATAAATAA

CDS Source ID
CDS Source
LR796853 [NCBI]
CDS location
range 1787 -> 2392
strand -
CDS
ATGAACATCACAAAAGACCACTGGATCGAATCGGCGATCAGGAAACCACTTGATGGGGGCGCGGATATGCCAATTCGCAGAGCATTGGTCATGCACTTCACATCCGGCGCGACCGCGATGTCATCCATCGAGTTCTGGGTATCTCAATGGGCAACCTCCCGAGGGGTCTGCGCCCACATTGTGATCGACCGCGATGGGACGATCTACCAGTGCCGCCCCTTCAACCGCACCGCTGGACACGCGGGGAAGTCGATATGGACCGACCCTAATACGGGCGTAAAATATCATAATCCAAACTCAGTCACCATCGGAATCGAGTTCGCGAATGCCGGAGACTCGGCCAACGCGGAAGGCAAGGCGTTCGGCGGCAGCTTCACTTGTCCCTCGGGATCTGACCTTGCCCGGCACAAAAACGGAGGCCCGCTAACATATTGGGAGCGCTTTCCGGCGGTCCAGATTGAGGCTGGAAAGAGGGTTGCAGCAGCATTGATTGAGCGCTACAATCTGGACGACGTAGTGGGGCATGACGACATCGCACCCGGACGGAAGAACGACCCAGGCCCGCTATTTCCAATGACATTATTTAAGCAACTACTAAATAAATAA

CDS Source ID
CDS Source
LR797283 [NCBI]
CDS location
range 26768 -> 27373
strand -
CDS
ATGAACATCACAAAAGACCACTGGATCGAATCGGCGATCAGGAAACCACTTGATGGGGGCGCGGATATGCCAATTCGCAGAGCATTGGTCATGCACTTCACATCCGGCGCGACCGCGATGTCATCCATCGAGTTCTGGGTATCTCAATGGGCAACCTCCCGAGGGGTCTGCGCCCACATTGTGATCGACCGCGATGGGACGATCTACCAGTGCCGCCCCTTCAACCGCACCGCTGGACACGCGGGGAAGTCGATATGGACCGACCCTAATACGGGCGTAAAATATCATAATCCAAACTCAGTCACCATCGGAATCGAGTTCGCGAATGCCGGAGACTCGGCCAACGCGGAAGGCAAGGCGTTCGGCGGCAGCTTCACTTGTCCCTCGGGATCTGACCTTGCCCGGCACAAAAACGGAGGCCCGCTAACATATTGGGAGCGCTTTCCGGCGGTCCAGATTGAGGCTGGAAAGAGGGTTGCAGCAGCATTGATTGAGCGCTACAATCTGGACGACGTAGTGGGGCATGACGACATCGCACCCGGACGGAAGAACGACCCAGGCCCGCTATTTCCAATGACATTATTTAAGCAACTACTAAATAAATAA

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 (18Jwv) rather than this protein.
PDB ID
18Jwv
Method AlphaFoldv2
Resolution 92.21
Chain position -
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50