Protein

UniProt accession
A0A024B2H2 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MNINTQYLVTDPERLKVIGPNWMNPTEITFHNTYNDASASAEVRNVRNNSTGTSFHTAVDDFEVQQVVPFDRNAWHAGDGTYGAGNRNSIGVEICYSMSGGERYRKAELNAIEHISDLMVRFNIPISKVKTHQERNGKYCPHRMLDEGRVGWFKAECERRANEKRNGGGGTPNPEPKPDPKPEPTPKPPSGDYDSSWFTKETGTFVTNTTIKLRTAPFTSAGVIATLPAGSTVNYNGFGIEYDGYVWIRQPRSNGYGYLATGESKGGKRVNYWGTFK
Physico‐chemical
properties
protein length:277 AA
molecular weight:30886,00000 Da
isoelectric point:8,62692
aromaticity:0,10830
hydropathy:-0,78953

Domains

Domains [InterPro]
IPR036505
15–166
IPR036505 IPR003646
IPR002502
24–144
IPR002502 IPR003646
IPR002502
23–142
IPR002502
IPR051206
23–219
IPR051206
IPR002502
10–151
IPR002502
IPR036505
21–157
IPR036505
Protein sequence: A0A024B2H2
1 277
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage Megatron
[NCBI] 		1486661 Herelleviridae > Wphvirus > Wphvirus megatron
Host Bacillus thuringiensis
[NCBI] 		1428 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AHZ10650.1 [NCBI]
Genbank nucleotide accession
KJ489401 [NCBI]
CDS location
range 26692 -> 27525
strand -
CDS
ATGAATATCAATACACAATACTTGGTAACGGACCCAGAACGCTTGAAAGTTATCGGACCTAACTGGATGAATCCTACCGAGATTACGTTCCATAACACGTATAACGATGCATCAGCTTCAGCAGAAGTACGTAACGTTCGTAATAACTCTACAGGTACATCATTCCATACAGCAGTCGATGATTTCGAAGTTCAACAAGTCGTACCATTTGACCGCAATGCATGGCACGCTGGAGACGGAACGTACGGAGCTGGTAACCGTAACTCTATCGGTGTAGAAATCTGTTACTCTATGAGTGGTGGAGAGCGTTATCGTAAAGCTGAGTTAAATGCTATCGAGCATATCTCAGATTTAATGGTACGTTTTAATATCCCAATCTCTAAAGTTAAGACTCACCAAGAGCGTAATGGTAAATATTGCCCACACCGTATGTTAGATGAAGGTCGTGTAGGTTGGTTTAAAGCAGAATGTGAACGTCGTGCTAATGAGAAACGTAACGGAGGCGGCGGTACACCAAACCCAGAACCAAAACCAGACCCTAAACCAGAACCTACTCCAAAGCCACCATCTGGTGACTACGATTCCAGCTGGTTCACTAAAGAGACAGGAACTTTCGTAACAAATACTACAATCAAGTTACGTACAGCACCATTCACAAGTGCAGGAGTAATCGCTACACTTCCGGCTGGTTCTACAGTTAACTACAATGGTTTTGGTATCGAATACGATGGTTATGTCTGGATTCGTCAACCACGTAGTAATGGCTACGGCTACTTAGCTACTGGTGAATCTAAAGGCGGTAAACGCGTGAACTACTGGGGTACATTTAAGTAA

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

No tertiary structures available.