Protein

UniProt accession
A0A060AHF9 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MVEIINKTVTRGVAGRRPGAVKGVVFHNTWGNSTAKQEANRLAAMNNNQLAAGFAHYYIDKNTIWRTEDTYNAAWHTANSDGNTNYIGYEVCGNDQTPLKDFLQAEENTFWQIAQDLKYYGLPVNRNTVRLHHEFSATQCPKRSLIIHTGFNSTQAQPANVTNTMKDYVIKNVLKYYNNPSLKPDGKAPSTGGQTPPSGANVTPSTPSQHDKAVSASPAKHQGNAWGKLDYFNGHGKDQIRVAGWLVPDKPQGPIGRYAYVIFMQHGTNKELTRVQSAGIKRPDVKKAYGYQGGQELGFDVTVNKNQFKGKKVDVILRRANKSNGEGAVNDVRIDSIYLSL
Physico‐chemical
properties
protein length:341 AA
molecular weight:37728,00000 Da
isoelectric point:9,56983
aromaticity:0,09384
hydropathy:-0,67859

Domains

Domains [InterPro]
IPR036505
15–145
IPR036505
IPR002502
9–159
IPR002502
IPR051206
17–175
IPR051206
IPR036505
3–179
IPR036505
IPR002502
19–142
IPR002502
IPR002502
21–141
IPR002502
Protein sequence: A0A060AHF9
1 341
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Enterococcus phage IME-EFm1
[NCBI] 		1445858 No lineage information
Host Enterococcus faecium
[NCBI] 		1352 Bacteria > Firmicutes > Bacilli > Lactobacillales > Enterococcaceae > Enterococcus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AIA65091.1 [NCBI]
Genbank nucleotide accession
KJ010489 [NCBI]
CDS location
range 21175 -> 22200
strand +
CDS
ATGGTAGAAATCATCAATAAAACAGTCACACGTGGTGTGGCAGGACGTAGACCAGGTGCAGTGAAGGGTGTAGTATTCCACAATACATGGGGCAACTCAACAGCTAAACAAGAAGCCAATCGTTTAGCAGCAATGAACAACAATCAGTTAGCTGCTGGATTTGCTCATTATTACATTGATAAGAATACAATCTGGCGTACTGAGGATACTTACAATGCAGCTTGGCATACAGCTAACTCTGATGGTAATACAAACTATATTGGCTATGAAGTGTGTGGTAACGATCAAACACCATTGAAAGACTTCTTGCAAGCTGAAGAAAATACCTTTTGGCAAATTGCGCAAGATTTGAAATATTATGGTTTACCAGTTAATCGTAATACAGTACGTTTACATCATGAGTTTTCAGCCACACAATGTCCTAAACGTTCGTTAATCATTCATACTGGTTTCAACTCAACACAGGCTCAGCCAGCTAATGTAACTAACACAATGAAAGATTATGTGATTAAAAACGTTCTTAAGTATTACAATAACCCTAGTTTGAAACCAGATGGTAAAGCTCCATCTACAGGTGGACAAACACCTCCAAGTGGTGCTAACGTAACACCTTCAACACCTAGCCAACATGATAAGGCAGTATCTGCAAGCCCAGCAAAACATCAAGGTAATGCTTGGGGTAAACTTGACTACTTTAATGGTCATGGTAAAGATCAGATTCGTGTGGCTGGTTGGTTAGTTCCTGATAAACCACAAGGTCCTATTGGACGATATGCATATGTTATCTTCATGCAACATGGAACAAACAAAGAACTGACACGTGTTCAGTCTGCTGGTATTAAACGCCCAGATGTTAAGAAAGCATATGGCTATCAAGGTGGGCAAGAGCTTGGTTTTGACGTAACAGTCAATAAGAACCAGTTCAAAGGTAAAAAAGTAGACGTGATTTTGCGTAGAGCAAATAAATCTAATGGTGAAGGCGCAGTGAATGACGTGAGAATTGATAGTATCTATTTGAGTCTATAA

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.