Protein

UniProt accession
B1ABI9 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MTISSLTNIKKYEWQSSGHFGGITRKPIDMIVLHHNGGTGSNVVPNCWIEREASAHYQIENGQIINCLDEDITAWHCGAYGVDNNSHTIGIEHQNSTGAPDWLVSNENQEKSAQLVADIAKRYGIPLDRNHIVRHREMPNCNTDCSGGLDIDWVVTRAKQIAGQGGIPAPTPTPTPSNSNPVNPVVTVSYGLRQIGAGWLGTITDFNNSNGNGFAGNSNHEHDMLFASVSHGSLRYRVHTVKSGWLGWVNQGNKNDLVNGCAGNPNEAIDGVQFYYTTPNGEVYKQAYYRSQTSKRAGWLPSVEDDKDFAGILGEPLDRLQIAIRSSNPF
Physico‐chemical
properties
protein length:330 AA
molecular weight:36141,00000 Da
isoelectric point:5,98210
aromaticity:0,08182
hydropathy:-0,53000

Domains

Domains [InterPro]
IPR036505
17–161
IPR036505
IPR051206
26–247
IPR051206
IPR002502
17–147
IPR002502
IPR036505
14–148
IPR036505
IPR002502
25–147
IPR002502
IPR002502
27–149
IPR002502
Protein sequence: B1ABI9
1 330
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Lactococcus phage asccphi28
[NCBI] 		503388 Salasmaviridae >
Host Lactococcus lactis
[NCBI] 		1358 Bacteria > Firmicutes > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ACA21494.1 [NCBI]
Genbank nucleotide accession
EU438902 [NCBI]
CDS location
range 13093 -> 14085
strand -
CDS
ATGACAATTTCATCATTGACAAATATCAAAAAATATGAATGGCAAAGTTCAGGACATTTTGGAGGGATTACAAGAAAACCGATTGACATGATTGTTTTACACCATAATGGCGGAACAGGTTCAAACGTTGTTCCTAATTGTTGGATTGAACGGGAAGCGTCAGCGCATTATCAAATTGAAAACGGTCAAATTATAAACTGTTTAGATGAAGATATTACAGCTTGGCATTGTGGCGCTTATGGCGTTGATAATAATTCACATACCATTGGCATTGAACATCAAAACTCTACTGGTGCGCCTGATTGGTTAGTTTCTAATGAAAATCAAGAAAAATCAGCGCAATTAGTTGCGGATATTGCAAAACGCTACGGCATTCCATTAGATAGAAATCACATTGTCAGACACCGTGAAATGCCTAACTGCAATACAGATTGTTCAGGCGGTCTTGATATTGATTGGGTTGTTACCCGTGCAAAACAAATTGCGGGTCAAGGTGGAATACCTGCACCAACACCAACACCAACACCCTCAAACTCTAATCCAGTTAATCCAGTTGTTACTGTTTCCTACGGGTTGCGACAAATTGGTGCGGGTTGGCTTGGAACAATTACCGATTTTAACAACTCAAACGGAAATGGATTTGCTGGAAATTCTAATCATGAGCATGATATGTTATTTGCAAGCGTGTCACATGGTTCTTTAAGATACCGTGTTCATACTGTCAAATCGGGTTGGCTTGGTTGGGTTAATCAAGGAAATAAAAATGACCTTGTTAATGGTTGTGCGGGAAACCCTAATGAAGCAATTGACGGGGTTCAATTCTACTATACGACACCTAATGGAGAAGTTTACAAGCAAGCCTATTATCGCTCACAAACGTCTAAGCGTGCGGGGTGGTTACCTAGTGTAGAAGATGATAAAGACTTTGCGGGAATACTTGGCGAACCGCTTGACCGTTTACAAATTGCTATTCGTAGCTCAAACCCATTTTAA

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.