Protein

UniProt accession
A0A059PAL4 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MTKNINGDVYSDLITSADSRAMASGSIPRKKIDRIVIHHNATTNKDVAINTWLASGSAQTSAHYEVANNEIIGIVGEGTTAWHAGNGDMNARSIGIENLNSAGEPNWPVSSQTFESLSKLVADIANRYGFPIDSTHVIPHNAVVGTRCPGGIDVAKVIARAREIAGGNGGSNTNTGNNTNGLDQVLHVGEYFKARKAYRVDEMKFVNGVWQVVNYELAGGKDFSWVYNGFGVASTDKVDTNGNITKDQELSVGAYFRLHSDRIKVVDANDSGVALDTRYGRVWVDASTLTEVK
Physico‐chemical
properties
protein length:293 AA
molecular weight:31517,00000 Da
isoelectric point:6,06167
aromaticity:0,07509
hydropathy:-0,32935

Domains

Domains [InterPro]
IPR036505
30–152
IPR036505 IPR038263
IPR036505
21–165
IPR036505 IPR031898
IPR002502
30–150
IPR002502
IPR002502
22–150
IPR002502
IPR051206
27–192
IPR051206
IPR002502
31–151
IPR002502
Protein sequence: A0A059PAL4
1 293
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Leuconostoc phage LN25
[NCBI] 		1262518 Unaquatrovirus > Unaquatrovirus LN25
Host Leuconostoc mesenteroides
[NCBI] 		1245 Bacteria > Firmicutes > Bacilli > Lactobacillales > Leuconostocaceae > Leuconostoc

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AFY98405.1 [NCBI]
Genbank nucleotide accession
KC013026 [NCBI]
CDS location
range 23878 -> 24759
strand -
CDS
ATGACAAAGAACATTAATGGTGATGTATACAGTGACTTGATTACCAGCGCAGATAGTCGTGCAATGGCAAGTGGTAGTATCCCTCGTAAGAAAATCGACCGTATCGTTATCCATCACAACGCAACAACAAATAAAGACGTGGCAATTAATACGTGGTTGGCGTCTGGTTCTGCACAAACATCGGCTCATTATGAAGTTGCTAATAACGAAATTATTGGTATTGTTGGTGAGGGGACAACTGCATGGCACGCTGGTAACGGAGACATGAACGCTCGATCGATTGGTATTGAAAACCTTAATAGTGCTGGAGAACCCAACTGGCCAGTGTCATCACAAACGTTTGAAAGTCTATCTAAATTAGTAGCTGACATTGCAAATCGTTACGGTTTCCCTATTGACAGCACCCACGTTATCCCTCATAATGCTGTTGTTGGTACTCGTTGCCCCGGTGGTATTGATGTTGCTAAGGTTATCGCTCGTGCTCGTGAAATTGCTGGTGGTAATGGTGGATCAAATACAAACACTGGAAACAACACAAATGGATTAGACCAAGTATTGCACGTGGGAGAATACTTCAAAGCACGTAAAGCATATCGAGTTGACGAAATGAAGTTTGTTAACGGCGTATGGCAAGTGGTAAACTACGAACTAGCCGGTGGAAAAGATTTCTCATGGGTATACAACGGGTTTGGTGTTGCTTCTACCGATAAGGTTGATACCAATGGTAATATCACAAAAGACCAAGAGTTGTCCGTAGGTGCCTATTTCAGATTACACAGCGACCGCATTAAGGTTGTTGACGCAAATGATAGTGGTGTTGCATTAGACACTCGTTATGGTCGTGTTTGGGTAGACGCTTCGACATTAACAGAAGTAAAATAG

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: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.