Protein

UniProt accession
F1AH96 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MQAKLTIKEFIEWLKTSEGKQFNVDLWYGFLRFDYANAAWKVLFGLLLKGLGAKDIPFANNFDGLATVYQNTPDFLAKPGDTVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDGIEQPGWGWAKVTRRQHAYDFPMWFIRPKFKSETAPRSVQSPTQAPKKETAKPQPKAVELKIIKDVVKGYDLPKRGSNPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRLEAGIAHSYVSGNTVCQALDESQVGWHTANQIGNKYYYGIEVCQSMGADNATFLKNEQATFQECARLLKKWGLPANRNTIRLHNEFTSTSCPHRSSVLHTGFDPVTRGLLPEDKQLQLKDYFIKQIRVYMDGKIPVATVSNESSASSNTVKPVASAWKRNKYGTYYMEESARFTNGNQPITVRKIGPFLSCPVAYQFQPGGYCDYTEVMLQDGHVWVGYTWEGQRYYLPIRTWNGSGPPNQILGDLWGEIS
Physico‐chemical
properties
protein length:481 AA
molecular weight:53938,00000 Da
isoelectric point:8,90671
aromaticity:0,12682
hydropathy:-0,42578

Domains

Domains [InterPro]
Protein sequence: F1AH96
1 481
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage 006
[NCBI]
980978 No lineage information
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ADW95277.1 [NCBI]
Genbank nucleotide accession
GU722131 [NCBI]
CDS location
range 10 -> 1455
strand +
CDS
ATGCAAGCAAAATTAACTATAAAAGAGTTTATAGAGTGGTTGAAAACTTCTGAAGGAAAACAATTCAATGTGGACTTATGGTATGGATTTCTACGCTTTGATTATGCCAATGCTGCTTGGAAAGTTCTGTTTGGATTACTTCTGAAAGGTTTAGGTGCAAAAGACATACCATTTGCAAACAATTTTGATGGACTAGCCACTGTATATCAAAATACGCCGGACTTTTTGGCAAAACCCGGCGATACGGTTGTGTTCGGTAGTAATTACGGTGCAGGATACGGACACGTAGCATGGGTAATTGAAGCAACTTTAGATTATATCATTGTATATGAGCAGAATTGGCTAGGCGGTGGCTGGACTGACGGAATCGAACAACCCGGCTGGGGTTGGGCAAAAGTTACAAGACGACAACATGCTTATGATTTCCCTATGTGGTTTATCCGTCCGAAGTTTAAAAGTGAGACAGCGCCACGATCAGTTCAATCTCCTACACAAGCACCTAAAAAAGAAACAGCTAAGCCACAACCTAAAGCAGTAGAACTTAAAATCATCAAAGATGTGGTTAAAGGTTATGACCTACCTAAGCGTGGTAGTAATCCTAAAGGTATAGTTATACACAACGACGCAGGGAGCAAAGGGGCGACTGCTGAAGCATATCGTAACGGATTAGTAAATGCACCTTTATCAAGATTAGAAGCGGGCATTGCGCATAGTTACGTATCAGGCAACACAGTTTGCCAAGCCTTAGATGAATCACAAGTAGGTTGGCATACCGCTAATCAAATAGGTAATAAATATTATTACGGTATTGAAGTATGTCAATCAATGGGCGCAGATAACGCGACATTCTTAAAAAATGAACAGGCAACTTTCCAAGAATGCGCTAGATTGTTGAAAAAATGGGGATTACCAGCAAACAGAAATACAATCAGATTGCACAATGAATTTACTTCAACATCATGCCCTCATAGAAGTTCGGTTTTACACACTGGTTTTGACCCAGTAACTCGCGGTCTATTGCCGGAAGATAAACAATTACAACTTAAAGACTACTTTATCAAGCAAATCAGAGTGTATATGGACGGTAAGATACCAGTTGCCACTGTCTCTAATGAGTCAAGCGCTTCAAGTAATACAGTTAAACCAGTTGCGAGTGCATGGAAACGTAATAAATATGGTACTTACTACATGGAAGAAAGTGCTAGATTCACAAACGGTAATCAACCAATCACTGTAAGAAAAATAGGACCATTCTTATCATGCCCGGTAGCTTACCAATTCCAACCTGGTGGATATTGTGATTATACAGAAGTGATGTTACAAGATGGTCATGTTTGGGTAGGATATACATGGGAGGGGCAACGTTATTACTTGCCTATTAGAACATGGAATGGTTCTGGCCCACCTAATCAGATATTAGGTGACTTATGGGGAGAAATCAGTTAG

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:0042742 defense response to bacterium 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.