Protein

UniProt accession
A0A0K2FL53 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MMNINTQYLVTDPERLKVIGPNWMNPTEITFHNTYNDASASAEVRNVRNNSTGTSFHTAVDDFEVQQVVPFDRNAWHAGDGTYGAGNRNSIGVEICYSMSGGERYRKAELNAIEHISDLMVRFNIPISKVKTHQERNGKYCPHRMLDEGRVGWFKAECERRANEKRNGGGGTPNPEPKPDPKPEPTPKPPSGDYDSSWFTKETGTFVTNTTIKLRTAPFTSAGVIATLPAGSTVNYNGFGIEYDGYVWIRQPRSNGYGYLATGESKGGKRVNYWGTFK
Physico‐chemical
properties
protein length:278 AA
molecular weight:31017,00000 Da
isoelectric point:8,62692
aromaticity:0,10791
hydropathy:-0,77986

Domains

Domains [InterPro]
IPR003646
201–256
IPR003646 IPR002502
IPR051206
23–220
IPR051206
IPR003646
202–268
IPR003646 IPR036505
IPR002502
24–143
IPR002502
IPR036505
22–158
IPR036505
IPR002502
11–152
IPR002502
Protein sequence: A0A0K2FL53
1 278
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage Eyuki
[NCBI] 		1690431 Herelleviridae > Wphvirus > Wphvirus megatron
Host Bacillus thuringiensis serovar kurstaki
[NCBI] 		29339 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ALA46732.1 [NCBI]
Genbank nucleotide accession
KT207918 [NCBI]
CDS location
range 26992 -> 27828
strand -
CDS
TTGATGAATATCAATACACAATACTTGGTAACGGACCCAGAACGCTTGAAAGTTATCGGACCTAACTGGATGAATCCTACCGAGATTACGTTCCATAACACGTATAACGATGCATCAGCTTCAGCAGAAGTACGTAACGTTCGTAATAACTCTACAGGTACATCATTCCATACAGCAGTCGATGATTTCGAAGTTCAACAAGTCGTACCATTTGACCGCAATGCATGGCACGCTGGAGACGGAACGTACGGAGCTGGTAACCGTAACTCTATCGGTGTAGAAATCTGTTACTCTATGAGTGGTGGAGAGCGTTATCGTAAAGCTGAGTTAAATGCTATCGAGCATATCTCAGATTTAATGGTACGTTTTAATATCCCAATATCTAAAGTTAAGACTCACCAAGAGCGTAATGGTAAATATTGCCCACACCGTATGTTAGATGAAGGTCGTGTAGGTTGGTTTAAAGCAGAATGTGAACGTCGTGCTAATGAGAAACGTAACGGAGGCGGCGGTACACCAAACCCAGAACCAAAACCAGACCCTAAACCAGAACCTACTCCAAAGCCACCATCTGGTGACTACGATTCCAGCTGGTTCACTAAAGAGACAGGAACTTTCGTAACAAATACTACAATCAAGTTACGTACAGCACCATTCACAAGTGCAGGAGTAATCGCTACACTTCCGGCTGGTTCTACAGTTAACTACAATGGTTTTGGTATCGAATACGATGGTTATGTCTGGATTCGTCAACCACGTAGTAATGGCTACGGCTACTTAGCTACTGGTGAATCTAAAGGCGGTAAACGCGTGAACTACTGGGGTACATTTAAGTAA

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.