Protein

UniProt accession
Q4ZAU2 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MQAKLTKKEFIEWLKTSEGKQFNADLWYGFQCFDYANAAWKVLFGLLLKGLGAKDIPFANNFDGLATVYQNTPDFLAQPGDMVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDGIEQPGWGWEKVTRRQHAYDFPMWFIRPNFKSEIAPRSVQSPTQAPKKETAKPQPKAVELKIIKDVVKGYDLPKRGSNPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRLEAGIAHSYVSGNTVWQALDESQVGWHTANQLGNKYYYGIEVCQSMGADNATFLKNEQATFQECARLLKKWGLPANRNTIRLHNEFTSTSCPHRSSVLHTGFDPVTRGLLPEDKRLQLKDYFIKQIRAYMDGKIPVATVSNDSSASSNTVKPVASAWKRNKYGTYYMEESARFTNGNQPITVRKVGPFLYCPVGYQFQPGGYCDYTEVMLQDGHVWVGYTWEGQRYYLPIRTWNGSAPPNQILGDLWGEIS
Physico‐chemical
properties
protein length:481 AA
molecular weight:54104,00000 Da
isoelectric point:8,72723
aromaticity:0,13098
hydropathy:-0,45925

Domains

Domains [InterPro]
Protein sequence: Q4ZAU2
1 481
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Phietavirus pv52a
[NCBI]
320847 Phietavirus >
Host Staphylococcus aureus
[NCBI]
1280 Bacteria > Firmicutes > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AAX91801.1 [NCBI]
Genbank nucleotide accession
AY954965 [NCBI]
CDS location
range 23837 -> 25282
strand +
CDS
ATGCAAGCAAAATTAACTAAAAAAGAGTTTATAGAGTGGTTGAAAACTTCTGAGGGAAAACAATTCAATGCGGACTTATGGTATGGATTTCAATGCTTTGATTATGCCAATGCTGCTTGGAAAGTTTTGTTTGGATTACTTCTAAAAGGTTTAGGTGCAAAAGATATACCATTTGCAAACAATTTCGATGGACTAGCTACTGTATACCAAAATACACCGGACTTTTTGGCACAACCCGGCGACATGGTTGTGTTCGGTAGTAATTACGGTGCAGGATACGGACACGTAGCATGGGTAATTGAAGCAACTTTAGATTATATCATTGTATATGAGCAGAATTGGCTAGGCGGTGGCTGGACTGACGGAATCGAACAACCCGGCTGGGGTTGGGAAAAAGTTACAAGACGACAACATGCTTACGATTTCCCTATGTGGTTTATCCGCCCGAACTTCAAAAGCGAAATAGCACCACGATCAGTTCAATCTCCTACACAAGCACCTAAAAAGGAAACAGCTAAGCCACAACCTAAAGCAGTAGAACTTAAAATCATCAAAGATGTGGTTAAAGGTTATGACCTACCTAAGCGTGGTAGTAACCCTAAAGGTATAGTTATTCATAACGACGCAGGAAGCAAAGGGGCGACAGCAGAAGCGTATCGAAACGGATTAGTTAACGCGCCTTTATCGAGATTAGAGGCAGGTATTGCACATAGTTATGTATCAGGTAACACAGTGTGGCAAGCTTTAGATGAATCACAAGTAGGTTGGCATACTGCTAACCAATTAGGCAATAAATATTATTACGGTATTGAAGTGTGTCAATCAATGGGCGCAGATAACGCGACATTCTTAAAAAATGAACAGGCAACTTTCCAAGAATGTGCTAGGTTATTAAAAAAGTGGGGATTACCAGCAAACAGAAATACAATCAGATTGCACAATGAATTTACTTCAACATCATGCCCTCATAGAAGTTCGGTTTTACACACTGGTTTTGACCCAGTAACTCGCGGTCTATTGCCAGAAGACAAGCGGTTGCAACTTAAAGACTACTTTATCAAGCAGATTAGGGCGTACATGGATGGTAAAATACCGGTTGCTACTGTCTCAAATGATTCAAGCGCTTCAAGTAATACAGTTAAACCAGTTGCGAGTGCATGGAAACGTAATAAATATGGTACTTACTACATGGAAGAAAGTGCTAGATTCACAAACGGCAATCAACCAATCACAGTAAGAAAAGTGGGGCCATTCTTATATTGTCCAGTGGGTTATCAGTTCCAACCTGGTGGATATTGTGATTATACAGAAGTGATGTTACAAGATGGTCATGTTTGGGTAGGATATACATGGGAGGGGCAACGTTATTACTTGCCTATTAGAACATGGAATGGTTCTGCCCCACCTAATCAGATATTAGGTGACTTATGGGGAGAAATCAGTTAG

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:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation (UniProt)
GO:0046872 metal ion binding Molecular function 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.