Protein

UniProt accession
I6X5A8 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKTQAEINKRLDAYAKGTVDSPYRVKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASKTPAPKKKATLKVSKNHINYTMDKRGKKPEGMVIHNDAGRSSGQQYENSLANAGYARYANGIAHYYGSEGYVWEAIDAKNQIAWHTGDGTGANSGNFRFAGIEVCQSMSASDAQFLKNEQAVFQFTAEKFKEWGLTPNRKTVRLHMEFVPTACPHRSMVLHTGFNPVTQGRPSQAIMNKLKDYFIKQIKNYMDKGTSSSTVVKDGKTSSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGNRVYCPVRTCQGVPPNQIPGVAWGVFK
Physico‐chemical
properties
protein length:495 AA
molecular weight:54741,00000 Da
isoelectric point:9,50304
aromaticity:0,11313
hydropathy:-0,59071

Domains

Domains [InterPro]
Protein sequence: I6X5A8
1 495
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Staphylococcus phage Fi200W
[NCBI]
1195078 Herelleviridae > Kayvirus > Kayvirus G1
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AFN38507.1 [NCBI]
Genbank nucleotide accession
JX080303 [NCBI]
CDS location
range 34997 -> 37360
strand -
CDS
ATGGCTAAGACTCAAGCAGAAATAAATAAACGTTTAGATGCTTATGCAAAAGGAACAGTAGATAGCCCTTACAGAGTTAAAAAAGCTACAAGTTATGACCCATCATTTGGTGTAATGGAAGCAGGAGCCATTGATGCAGATGGTTACTATCACGCTCAGTGTCAAGACCTTATTACAGACTATGTTTTATGGTTAACAGATAATAAAGTTAGAACTTGGGGTAATGCTAAAGACCAAATTAAACAGAGTTATGGTACTGGATTTAAAATACATGAAAATAAACCTTCTACTGTACCTAAAAAAGGTTGGATTGCGGTATTTACATCCGGTAGTTATGAACAGTGGGGTCACATAGGTATTGTATATGATGGAGGTAATACTTCTACATTTACTATTTTAGAGCAAAACTGGAATGGTTATGCTAATAAAAAACCTACAAAACGTGTAGATAATTATTACGGATTAACTCACTTCATTGAAATACCTGTAAAAGCAGGAACTACTGTTAAAAAAGAAACAGCTAAGAAAAGCGCAAGTAAAACGCCTGCACCTAAAAAGAAAGCAACACTAAAAGTTTCTAAGAATCACATTAACTATACAATGGATAAACGTGGTAAAAAACCTGAAGGAATGGTAATACACAACGATGCAGGTCGTTCTTCAGGACAACAATACGAGAATTCATTAGCTAATGCAGGTTATGCTAGATACGCTAATGGTATTGCTCATTACTACGGCTCTGAAGGTTATGTATGGGAAGCAATAGATGCTAAGAATCAAATTGCTTGGCACACGGGTGATGGAACAGGAGCAAACTCAGGTAACTTTAGATTTGCAGGTATTGAAGTCTGTCAATCAATGAGTGCTAGTGATGCTCAATTCCTTAAAAATGAACAAGCAGTATTCCAATTTACAGCAGAGAAATTTAAAGAATGGGGTCTTACTCCTAACCGTAAAACTGTAAGATTGCATATGGAATTTGTACCAACTGCCTGTCCTCACCGTTCTATGGTTCTTCATACAGGATTTAATCCAGTAACACAAGGAAGACCATCACAAGCAATAATGAATAAATTAAAAGATTATTTCATTAAACAAATTAAAAACTACATGGATAAAGGAACTTCAAGTTCTACAGTAGTTAAAGATGGTAAAACAAGTAGCGCAAGTACACCGGCAACTAGACCAGTTACAGGTTCTTGGAAAAAGAACCAGTACGGAACTTGGTATAAACCGGAAAATGCAACATTTGTCAATGGTAACCAACCTATAGTAACTAGAATAGGTTCTCCATTCTTAAATGCTCCAGTAGGCGGTAACTTACCGGCAGGGGCTACAATTGTATATGACGAAGTTTGTATCCAAGCAGGTCACATTTGGATAGGTTATAATGCTTACAACGGTAACAGAGTATATTGCCCTGTTAGAACTTGTCAAGGTGTTCCACCTAATCAAATACCTGGCGTTGCCTGGGGAGTATTCAAATAG

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

PDB ID: upi000035e423_model

Method: AlphaFold3 Non-commercial

Resolution:

Chain position: A