Protein

UniProt accession
J9PU17 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MNINTQYLVTDPERLKVIGPNWMNPTEITFHNTYNDASASAEVRNVRNNSTGTSFHTAVDDFEVQQVVPFDRNAWHAGDGTYGAGNRNSIGVEICYSMSGGERYRKAELNAIEHISDLMVRFNIPISKVKTHQERNGKYCPHRMLDEGRVGWFKEQCERRANEKRNGGGGAPIEQPKPKPEPTPTPKPPTGDYDSSWFTKETGTFVTNTTIKLRTAPFTSAGVIATLPAGSTVNYNGFGIEYDGYVWIRQPRSNGYGYLATGESRNGKRVNYWGTFK
Physico‐chemical
properties
protein length:277 AA
molecular weight:31028,00000 Da
isoelectric point:8,84656
aromaticity:0,10830
hydropathy:-0,78051

Domains

Domains [InterPro]
IPR003646
200–255
IPR003646 IPR002502
IPR002502
24–144
IPR002502 IPR003646
IPR051206
23–222
IPR051206
IPR002502
23–142
IPR002502
IPR036505
21–158
IPR036505
IPR036505
15–167
IPR036505
Protein sequence: J9PU17
1 277
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage BPS13
[NCBI] 		1136731 Herelleviridae > Wphvirus > Wphvirus BPS13
Host Bacillus cereus
[NCBI] 		1396 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AEZ50187.1 [NCBI]
Genbank nucleotide accession
JN654439 [NCBI]
CDS location
range 3921 -> 4754
strand +
CDS
ATGAATATCAATACACAATACTTGGTAACGGACCCTGAGCGTTTAAAGGTTATTGGACCGAACTGGATGAACCCTACCGAGATTACATTCCACAATACGTATAACGATGCATCCGCTTCAGCAGAAGTACGTAACGTGCGAAATAACTCTACAGGTACTTCATTCCATACAGCTGTCGATGACTTTGAAGTTCAACAAGTAGTGCCATTTGACCGTAATGCTTGGCATGCTGGAGACGGAACGTACGGAGCAGGTAACCGTAACTCTATCGGTGTAGAAATCTGTTACTCTATGAGTGGTGGAGAGCGTTACCGTAAAGCTGAGTTGAATGCTATCGAGCATATCTCTGACTTAATGGTACGATTTAATATCCCAATCTCTAAAGTTAAGACTCACCAAGAGCGTAATGGTAAATACTGTCCTCACCGTATGTTAGATGAAGGACGTGTAGGTTGGTTTAAAGAGCAATGTGAACGACGTGCTAATGAAAAACGTAATGGTGGCGGTGGAGCTCCAATCGAACAACCTAAACCTAAACCAGAACCAACTCCGACTCCAAAACCACCAACTGGTGACTACGATTCTAGCTGGTTCACAAAAGAGACAGGAACTTTCGTAACAAATACTACAATCAAGTTACGTACAGCACCATTCACAAGTGCAGGAGTAATCGCTACACTTCCAGCTGGTTCTACAGTTAACTATAATGGTTTCGGTATCGAATACGACGGTTATGTCTGGATTCGTCAACCACGCAGTAATGGCTACGGCTATCTTGCTACAGGTGAATCTAGAAACGGTAAACGAGTGAACTACTGGGGTACATTTAAGTAA

Gene Ontology

Description Category Evidence (source)
GO:0001897 symbiont-mediated cytolysis of host cell Biological process Inferred from Electronic Annotation (InterPro)
GO:0006508 proteolysis Biological process Inferred from Electronic Annotation (InterPro)
GO:0008233 peptidase activity Molecular function 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:0030420 establishment of competence for transformation Biological process Inferred from Electronic Annotation (InterPro)
GO:0030435 sporulation resulting in formation of a cellular spore 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

PDB ID: upi00028707c4_model

Method: AlphaFold3 Non-commercial

Resolution: –

Chain position: A