Protein

Protein accession
A0A0A0PQA1 [UniProt]
Representative
3ATLj
Source
UniProt (cluster: phalp2_1848)
Protein name
N-acetylmuramoyl-L-alanine amidase
Lysin probability
100%
PhaLP type
endolysin
Probability: 99% (predicted by ML model)
Protein sequence
MVKIKKDLVPSNFAAQVTYKDGVNSCKYIVVHETANTKAGADAQAHANLQKNGNSREASWHYQVDKNGVIQSFDDRKQCWHAGSKFYNQNAIGIELCVDSGGDFKKTVENAAELIKSLMKKYGIPVKNVLTHKETSGWKDCPHFLRSGSKGVTWAQLVSMISSTSSSSGKAPSKPVKAPSTPAKAPSGSGSINFSTNSIVDFLTSAKLDSSFANRKKLADKYGISNYSGTAAQNESLLAKLKKDFKATSKPVSTKPAAKGDQKTNSIVDYLNSIKVDSSFANRKKLAAKHGISNYSGTAAQNSALLKKVRGK
Physico‐chemical
properties
protein length:312 AA
molecular weight:33560,0 Da
isoelectric point:9,83
hydropathy:-0,55
Representative Protein Details
Accession
3ATLj
Protein name
3ATLj
Sequence length
366 AA
Molecular weight
41479,78920 Da
Isoelectric point
8,95513
Sequence
MVKMIDHLSKHDHYYSGTNQKKYIAIHETANRSVGAGAWSHARLQANGNSRQASWNWQVDDEIAIRSYPEDRRTWHAGDSEYGLNSISVEICVNRDGDYDKALQNAAELVAYLRKKFDIPWNRVISHKFITGKQCPAIMLADGRWDEFIKASDPKNAGKVTVASGGSEASAPQQYDKRKVITDDAEIKAGRSRGSETIGTPSKGYRLNIVEDQGSWTKVRWNYGTSDEPDYRNAYIATVDLEKKPAEYPHVALKRTDKHTRASHNAWVTLMAAVDYTDPDLGKNLQSWLNDLTDPRTGRGYYDLSKYRHDGIMGPIAVKGLQRKLYDTSAIGKKHLYYGVADGYRGPLTVRAEIDYLNWQRQFLTN
Other Proteins in cluster: phalp2_1848
Total (incl. this protein): 6 Avg length: 333,8 Avg pI: 9,57

Protein ID Length (AA) pI
3ATLj 366 8,95513
twj5 389 9,10534
A0A076G810 312 9,82016
L0LC28 311 9,82635
A0AA96KRH0 313 9,86065
Similar Clusters (pHMM search)
# Cluster # Members Identity (%) Alignment Length E-value
1 phalp2_4901
5Zr0m
117 27,7% 349 4.011E-26
2 phalp2_26995
4LbNv
19 30,4% 256 5.427E-22
3 phalp2_3935
78x1H
58 28,8% 246 1.085E-08

Domains

Domains [InterPro]
Ami2
Unannotated
Unannotated
Representative sequence (used for alignment): 3ATLj (366 AA)
Member sequence: A0A0A0PQA1 (312 AA)
1 366 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 Bacillus phage Bp8p-C
[NCBI]
1445810 Herelleviridae > Agatevirus > Agatevirus Bp8pC
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
CDS Source ID
CDS Source
KJ010547 [NCBI]
CDS location
range 119255 -> 120193
strand +
CDS
ATGGTAAAAATCAAAAAAGACCTTGTACCATCAAACTTCGCAGCGCAAGTTACATACAAAGATGGCGTTAACTCTTGTAAGTATATCGTAGTCCATGAAACGGCTAACACAAAAGCTGGAGCGGATGCTCAAGCTCACGCTAACTTACAAAAGAACGGTAACTCTCGAGAAGCTTCATGGCATTATCAGGTTGATAAGAACGGCGTCATTCAGTCATTCGATGACCGTAAACAATGCTGGCACGCAGGCTCTAAGTTCTACAATCAGAATGCGATCGGAATTGAACTTTGTGTAGACAGCGGAGGAGACTTCAAAAAGACTGTTGAAAATGCCGCAGAGCTTATTAAGTCTCTGATGAAGAAGTACGGTATCCCTGTTAAGAACGTGCTTACCCACAAGGAAACTAGTGGATGGAAAGACTGTCCTCATTTCTTGCGTAGTGGCAGTAAAGGTGTAACTTGGGCACAGCTTGTAAGTATGATTAGCTCAACTTCTTCATCTAGCGGTAAAGCTCCATCTAAGCCAGTTAAGGCACCTAGTACACCAGCTAAGGCTCCAAGTGGCTCCGGTTCAATTAACTTTAGCACTAACAGCATTGTCGATTTCTTAACATCTGCTAAGCTTGACTCTAGCTTCGCAAACCGTAAGAAACTTGCTGACAAGTATGGTATCTCTAACTACTCAGGTACAGCAGCACAAAATGAGAGTTTACTAGCGAAGTTGAAGAAGGATTTCAAAGCTACTTCCAAGCCTGTATCTACTAAGCCTGCTGCAAAAGGCGATCAAAAAACGAATAGCATTGTTGACTACTTAAACTCTATCAAAGTAGACTCTAGTTTTGCTAACCGTAAGAAGTTAGCCGCTAAGCACGGCATCTCCAACTACTCAGGTACAGCAGCTCAAAATAGTGCATTACTGAAAAAGGTTAGAGGAAAATAA

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:0030420 establishment of competence for transformation biological process None (UniProt)
GO:0030435 sporulation resulting in formation of a cellular spore 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 (3ATLj) rather than this protein.
PDB ID
3ATLj
Method AlphaFoldv2
Resolution 89.21
Chain position -
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50