Protein

UniProt accession
A0A068EP83 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MVAWRDDFIRINQYSRPGSKLTAVRKLILHYTANPGASAANHQRYFNNLTDRYASAHLFVDKIDSICIIPLDEVAYQANDGSYRGVAALQPNANFLAIGVEMCQEPDGSFHPDTVTRTVNVMADLCRKFGLSASDIVRHYDVTHKYCPGPYVDNPALFTAFKNRVSDVLGGGSGGGTGGNTGGGTTTPPTGGGDGRIGVAYITGTNVNLRSGPGTGYGVLRQLNAGESYIVWAEQDGWLCLGGDQWVKNDSSFLRFERTSGGSTGGSTGGGVGDTNAGKRVVSKVDGLNFYSRPTWDKSYVVGQCNAGEGFTIVTKVPVDDAYQYKVQNSKGATYYITASSTYVEVR
Physico‐chemical
properties
protein length:347 AA
molecular weight:37172,00000 Da
isoelectric point:7,59746
aromaticity:0,10375
hydropathy:-0,32968

Domains

Domains [InterPro]
IPR002502
14–165
IPR002502 IPR003646 IPR003646
IPR036505
7–165
IPR036505 IPR003646
IPR002502
23–150
IPR002502
IPR036505
4–169
IPR036505
IPR051206
7–301
IPR051206
IPR002502
24–151
IPR002502
Protein sequence: A0A068EP83
1 347
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage CP-51
[NCBI] 		1391188 Herelleviridae > Siminovitchvirus > Siminovitchvirus CP51
Host Bacillus cereus
[NCBI] 		1396 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AID50479.1 [NCBI]
Genbank nucleotide accession
KF554508 [NCBI]
CDS location
range 46646 -> 47689
strand +
CDS
ATGGTAGCATGGAGAGACGACTTTATTCGTATCAATCAGTATTCTAGACCAGGTTCTAAACTTACAGCTGTACGTAAGCTTATCTTACATTATACTGCTAACCCAGGTGCTAGTGCTGCTAACCATCAACGTTATTTCAATAACTTAACTGACCGTTATGCATCTGCACATTTATTCGTGGACAAGATTGACTCTATCTGTATTATTCCGCTTGATGAGGTAGCGTATCAGGCAAATGATGGTTCTTACCGAGGAGTAGCTGCATTGCAACCTAATGCTAACTTCTTAGCTATTGGTGTAGAAATGTGTCAAGAGCCTGATGGTAGCTTCCACCCAGACACAGTAACTCGTACTGTAAATGTTATGGCAGACTTATGCCGTAAGTTCGGTTTATCTGCTTCTGACATTGTACGACACTATGATGTAACCCATAAGTACTGTCCTGGTCCATATGTAGATAACCCTGCATTATTTACAGCTTTCAAGAATCGTGTAAGTGATGTATTAGGTGGTGGCTCTGGTGGAGGTACAGGTGGAAACACTGGTGGCGGTACAACTACACCTCCTACTGGTGGTGGAGATGGACGAATTGGTGTAGCTTACATTACAGGCACTAACGTAAACTTACGTAGTGGTCCAGGTACTGGCTACGGTGTATTACGTCAGCTAAATGCTGGGGAAAGCTATATCGTTTGGGCTGAACAAGATGGATGGTTATGCTTAGGTGGAGACCAATGGGTTAAGAATGACTCTTCATTCTTACGTTTCGAGCGTACTAGTGGAGGTTCTACAGGTGGTTCTACTGGTGGAGGTGTCGGTGATACTAATGCTGGTAAACGAGTGGTATCAAAAGTGGATGGCTTAAACTTCTACAGCCGACCTACATGGGATAAGTCTTATGTTGTTGGTCAATGTAATGCAGGTGAAGGCTTCACTATTGTTACTAAGGTGCCAGTAGATGATGCTTACCAGTACAAAGTACAAAACTCCAAAGGTGCGACTTACTATATCACTGCTAGCTCTACTTATGTAGAGGTTAGATAG

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: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.