Protein

UniProt accession
A0AAX4PP73 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKTQAEINKRLDAYAKGTVDSPYRIKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYQQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASKTPAPKKKATLKVSKNHINYTMDKRGKKPEGMVIHNDAGRSSGQQYENSLANAGYARYANGIAHYYGSEGYVWEAIDAKNQIAWHTGDGTGANSGNFRFAGIEVCQSMSASDAQFLKNEQAVFQFTAEKFKEWGLTPNRKTVRLHMEFVPTACPHRSMVLHTGFNPVTQGRPSQAIMNKLKDYFIKQIKNYMDKGTSSSTVVKDGKTSSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGNRVYCPVRTCQGVPPNHIPGVAWGVFK
Physico‐chemical
properties
protein length:495 AA
molecular weight:54763,00000 Da
isoelectric point:9,53289
aromaticity:0,11313
hydropathy:-0,58949

Domains

Domains [InterPro]
IPR007921
46–136
IPR007921 IPR003646 IPR002502
IPR007921
29–160
IPR007921 IPR036505 IPR003646
IPR036505
197–369
IPR036505 IPR038765
IPR002502
207–335
IPR002502
IPR002502
196–349
IPR002502
Protein sequence: A0AAX4PP73
1 495
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage vB_SauM-SDQ
[NCBI] 		3141262 Herelleviridae > Kayvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
WZN67553.1 [NCBI]
Genbank nucleotide accession
PP661519 [NCBI]
CDS location
range 28714 -> 30201
strand -
CDS
ATGGCTAAGACTCAAGCAGAAATAAATAAACGTTTAGACGCTTATGCAAAAGGTACAGTAGACAGTCCTTATAGAATTAAAAAAGCTACAAGCTATGACCCATCGTTTGGTGTAATGGAAGCAGGAGCAATTGACGCAGATGGTTACTATCATGCACAGTGCCAAGACTTAATTACTGATTATGTATTATGGTTAACAGATAATAAAGTTAGAACTTGGGGTAATGCTAAAGACCAAATCAAACAAAGTTATGGTACTGGATTTAAAATACATGAAAATAAACCTTCTACAGTACCTAAAAAAGGATGGATTGCTGTATTTACATCCGGTAGTTATCAGCAATGGGGTCACATAGGTATTGTATATGATGGAGGTAATACTTCTACATTTACTATTTTAGAGCAAAACTGGAACGGTTACGCTAATAAAAAACCTACAAAACGTGTAGATAATTATTACGGATTAACTCATTTTATTGAGATACCTGTAAAAGCAGGAACTACTGTTAAAAAAGAAACAGCTAAGAAAAGTGCAAGTAAAACACCTGCACCTAAAAAGAAAGCAACACTAAAAGTTTCTAAGAACCATATTAACTATACAATGGATAAACGTGGTAAGAAACCTGAAGGAATGGTAATACACAACGATGCAGGTCGTTCTTCAGGGCAACAATACGAGAATTCATTAGCTAACGCAGGTTATGCTAGATATGCTAATGGTATTGCTCATTACTATGGCTCTGAAGGTTATGTATGGGAAGCAATAGATGCTAAGAATCAAATTGCTTGGCACACAGGAGATGGAACAGGAGCAAACTCAGGTAACTTTAGATTTGCAGGTATTGAAGTCTGTCAATCAATGAGTGCTAGTGATGCTCAATTCCTTAAAAACGAACAAGCAGTATTCCAATTTACTGCAGAGAAATTTAAAGAATGGGGTCTTACTCCTAATCGTAAAACTGTAAGATTGCATATGGAATTTGTTCCAACAGCTTGTCCTCATCGTTCTATGGTTCTTCATACAGGATTTAATCCAGTAACACAAGGAAGACCATCTCAAGCAATAATGAATAAACTAAAAGATTATTTCATTAAACAAATTAAAAACTACATGGATAAAGGAACTTCAAGTTCTACAGTAGTTAAAGACGGTAAAACAAGTAGCGCAAGTACACCGGCAACTAGACCAGTAACAGGCTCTTGGAAAAAGAACCAGTACGGAACTTGGTACAAACCGGAAAATGCAACATTTGTTAATGGTAACCAACCTATAGTAACTAGAATAGGTTCTCCATTCTTAAATGCTCCAGTAGGAGGTAACTTACCGGCAGGAGCTACAATTGTATATGACGAAGTTTGTATCCAAGCAGGTCACATTTGGATAGGTTACAATGCTTACAATGGTAACAGAGTATATTGCCCTGTTAGAACTTGTCAAGGAGTTCCACCTAATCATATACCTGGGGTTGCTTGGGGAGTATTCAAATAG

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.