Protein

UniProt accession
W0TVU0 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKTQAEINKRLDAYAKGTVDSPYRVKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQNYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASKTPAPKKKATLKVSKNHINYTMDKRGKKPEGMVIHNDAGRSSGQQYENSLANAGYARYANGIAHYYGSEGYVWEAIDAKNQIAWHTGDGTGANSGNFRFAGIEVCQSMSASDAQFLKNEQAVFQFTAEKFKEWGLTPNRKTVRLHMEFVPTACPHRSMVLHTGFNPVTQGRPSQAIMNKLKDYFIKQIKNYMDKGTSSSTVVKDGKTSSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGNRVYCPVRTCQGVPPNQIPGVAWGVFK
Physico‐chemical
properties
protein length:495 AA
molecular weight:54768,00000 Da
isoelectric point:9,50304
aromaticity:0,11313
hydropathy:-0,59616

Domains

Domains [InterPro]
IPR036505
197–369
IPR036505 IPR003646 IPR038765
IPR036505
189–373
IPR036505 IPR003646 IPR007921
IPR002502
196–349
IPR002502 IPR007921
IPR002502
205–334
IPR002502
IPR002502
207–335
IPR002502
Protein sequence: W0TVU0
1 495
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage phiSA12
[NCBI] 		1450142 Herelleviridae > Kayvirus > Kayvirus SA12
Host Staphylococcus aureus
[NCBI] 		1280 Bacteria > Firmicutes > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
BAO47098.1 [NCBI]
Genbank nucleotide accession
AB903967 [NCBI]
CDS location
range 27339 -> 28826
strand -
CDS
ATGGCTAAGACTCAAGCAGAAATAAATAAACGTTTAGATGCTTATGCAAAAGGAACAGTAGATAGCCCTTACAGAGTTAAAAAAGCTACAAGTTATGACCCATCATTTGGTGTAATGGAAGCAGGAGCCATTGACGCAGATGGTTACTATCACGCTCAATGTCAAGACCTTATTACAGACTATGTTTTATGGTTAACAGATAATAAAGTTAGAACTTGGGGTAATGCTAAAGACCAAATTAAACAGAATTATGGTACTGGATTTAAAATACATGAAAATAAACCTTCTACTGTACCTAAAAAAGGTTGGATTGCGGTATTTACATCCGGTAGTTATGAACAGTGGGGTCACATAGGTATTGTATATGATGGAGGTAATACTTCTACGTTTACTATTTTAGAGCAAAACTGGAATGGTTATGCTAATAAAAAACCTACAAAACGTGTAGATAATTATTACGGATTAACTCACTTCATTGAAATACCTGTAAAAGCAGGAACTACTGTTAAAAAAGAAACAGCTAAGAAAAGCGCAAGTAAAACTCCTGCACCTAAAAAGAAAGCAACACTAAAAGTTTCTAAGAATCACATTAACTATACAATGGATAAGCGTGGTAAAAAACCTGAAGGAATGGTAATACACAACGATGCAGGTCGTTCTTCAGGACAACAATACGAGAATTCATTAGCTAATGCAGGTTATGCTAGATACGCTAATGGTATTGCTCATTACTACGGCTCTGAAGGTTATGTATGGGAAGCAATAGATGCTAAGAATCAAATTGCTTGGCACACAGGAGATGGAACAGGAGCAAACTCAGGTAACTTTAGATTTGCAGGTATTGAAGTCTGTCAATCAATGAGTGCTAGTGATGCTCAATTCCTTAAAAATGAACAAGCAGTATTCCAATTTACAGCGGAGAAATTTAAAGAATGGGGTCTTACTCCTAACCGTAAAACTGTAAGATTGCATATGGAATTTGTACCAACTGCCTGCCCTCACCGTTCTATGGTTCTTCATACAGGATTTAATCCAGTAACACAAGGAAGACCATCACAAGCAATAATGAATAAATTAAAAGATTATTTCATTAAACAAATTAAAAACTACATGGATAAAGGGACTTCAAGTTCTACAGTAGTTAAAGATGGTAAAACAAGTAGCGCAAGTACACCGGCAACTAGACCAGTTACAGGCTCTTGGAAAAAGAACCAGTACGGAACTTGGTATAAACCGGAAAATGCAACATTTGTTAATGGTAACCAACCTATAGTAACTAGAATAGGTTCTCCATTCTTAAATGCTCCAGTAGGCGGTAACTTACCGGCAGGGGCTACAATTGTATATGACGAAGTTTGTATCCAAGCAGGTCATATTTGGATAGGTTATAATGCTTACAATGGTAACAGAGTATATTGCCCTGTTAGAACTTGTCAAGGTGTTCCACCTAATCAAATACCTGGTGTTGCTTGGGGAGTATTCAAGTAG

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:0019835 cytolysis 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.