Protein

UniProt accession
A0A143FL68 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MNINTQYLVTDPDRLEVIGPYPLNPTEITFHNTYNDASASAEVRNVRNNSKGTSFHTAVDDFEVQQVVPFNRNAWHAGDGNGAGNRNSIGVEICYSMSGGERYRKAELNAIEHISDLMVRFNIPISKVKTHQERNGKYCPHRMLDEGRVGWFKAECERRANEKRNGGGGTPTPEPKPKDPAPAPKPPSGDYDSSWFTKETGTFVTNTSIKLRTAPFTSAGVIATLPAGSTVNYNGFGIEYDGYVWIRQPRSNGYGYLATGESKGGKRVNYWGTFK
Physico‐chemical
properties
protein length:275 AA
molecular weight:30479,00000 Da
isoelectric point:8,83509
aromaticity:0,10545
hydropathy:-0,75455

Domains

Domains [InterPro]
Protein sequence: A0A143FL68
1 275
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage DIGNKC
[NCBI]
1805948 Herelleviridae > Wphvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AMW62699.1 [NCBI]
Genbank nucleotide accession
KU737349 [NCBI]
CDS location
range 26715 -> 27542
strand -
CDS
ATGAATATCAATACACAGTACTTGGTAACTGACCCTGACCGTTTAGAAGTCATTGGACCTTACCCGTTAAATCCTACAGAGATTACGTTCCATAACACGTATAATGATGCATCCGCTTCAGCTGAAGTACGTAACGTCCGTAACAACTCTAAGGGTACGTCGTTCCATACAGCAGTCGATGATTTCGAAGTTCAACAAGTAGTTCCATTTAACCGTAACGCGTGGCACGCAGGAGATGGTAATGGTGCAGGTAACCGTAACTCTATCGGTGTTGAAATCTGTTACTCTATGAGTGGAGGAGAACGTTATCGTAAAGCTGAGTTGAACGCTATCGAACATATCTCAGATTTAATGGTACGTTTCAATATCCCAATCTCTAAAGTTAAGACGCACCAAGAGCGTAACGGTAAATATTGCCCACACCGTATGTTAGACGAAGGTCGTGTAGGTTGGTTTAAGGCAGAATGTGAACGTCGTGCTAATGAGAAACGAAACGGTGGCGGCGGTACACCAACTCCAGAACCAAAACCTAAAGACCCAGCACCAGCTCCAAAGCCACCATCTGGTGACTACGATTCTAGCTGGTTCACTAAAGAGACAGGAACTTTCGTAACAAATACTTCAATCAAGTTACGTACAGCACCATTCACAAGTGCAGGAGTAATCGCTACACTTCCGGCTGGTTCTACAGTTAACTACAATGGTTTCGGTATCGAATACGATGGTTATGTCTGGATTCGTCAACCACGTAGTAATGGCTACGGCTACTTAGCTACTGGTGAATCTAAAGGCGGTAAACGTGTGAACTACTGGGGTACGTTTAAGTAA

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.