Protein

UniProt accession
D2XQ00 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MEIKQMLVPRSRYDALCPYEMNPTEITFHNTYNDAPAINERNNVANNSTGTSFHIAVDDKEAIQLIPFNRNAWHAGDGNGRGNRHSIGVEICYSQSGGARYRKAELNAIEVIAQLMIQFDIPISKVKTHQERNGKYCPHRMLDEGRVQWFKNQCANRASSMKNLNKLQDAGKVEIIVNKFNKVVTYEFGTALVPEMLGMMDALGYESRIISYGDKQGLVRFETAYRQGNELDRATAWLDAKGLKYYYTKE
Physico‐chemical
properties
protein length:250 AA
molecular weight:28499,00000 Da
isoelectric point:8,54962
aromaticity:0,09600
hydropathy:-0,59120

Domains

Domains [InterPro]
IPR036505
3–155
IPR036505 IPR021976
IPR002502
22–139
IPR002502
IPR002502
22–141
IPR002502
IPR002502
13–154
IPR002502
IPR051206
5–154
IPR051206
IPR036505
1–163
IPR036505
Protein sequence: D2XQ00
1 250
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Cecivirus cv250
[NCBI] 		701257 Cecivirus >
Host Bacillus cereus
[NCBI] 		1396 Bacteria > Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ADB28383.1 [NCBI]
Genbank nucleotide accession
GU229986 [NCBI]
CDS location
range 27039 -> 27791
strand +
CDS
ATGGAAATCAAACAAATGTTAGTGCCAAGAAGTCGATACGATGCCTTATGCCCGTATGAGATGAATCCAACAGAAATCACATTTCATAACACGTACAACGACGCACCGGCTATAAATGAGCGTAATAATGTCGCTAACAATAGCACTGGAACATCATTTCATATCGCTGTGGATGATAAAGAAGCTATTCAGTTAATTCCTTTTAACAGAAATGCATGGCACGCTGGAGATGGTAATGGGAGAGGGAATCGTCATAGTATTGGGGTGGAAATTTGTTATTCACAATCAGGCGGAGCGAGATATCGCAAGGCTGAATTAAATGCAATTGAAGTAATCGCCCAATTAATGATTCAGTTTGATATTCCAATCAGTAAAGTTAAGACTCATCAAGAGAGAAACGGGAAGTACTGTCCGCATCGAATGTTAGATGAAGGACGTGTTCAGTGGTTTAAAAATCAATGTGCAAATAGAGCATCTAGCATGAAAAATTTAAATAAATTACAAGACGCAGGAAAGGTGGAAATTATAGTGAATAAATTTAATAAAGTTGTTACGTATGAATTCGGAACAGCGTTAGTACCAGAAATGTTAGGAATGATGGATGCTCTTGGGTATGAATCTCGTATTATCTCATATGGAGATAAACAGGGATTAGTTAGATTTGAAACAGCATATCGCCAAGGGAATGAACTAGATCGAGCAACTGCATGGTTAGATGCGAAAGGTCTTAAATACTACTATACAAAAGAATAG

Gene Ontology

Description Category Evidence (source)
GO:0001897 symbiont-mediated cytolysis of host cell Biological process 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.