Protein

UniProt accession
R9TQ04 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MGRGVTRMSYKIVQKGNKHTNSSSRDGHVPYVIVNHISAGSMGSMDNWFTSSGNKVSSAHFGVSKKGEIHQYVPIERMAWANGLSKWEQEKADAAVVRNNPSLNPNKYTVSIEHEGTDGQLTDAQFAASVWLHKYIQSEIKRLYGRDMKLDEYHVIGHFQVDPKRKPNCPGPKFPWDQLYKELKKVGAAKVEQQKVKVLVNGKKVADGYLDGGTTYTPSRAVAEALGASVRWDKENLTVLITKEEK
Physico‐chemical
properties
protein length:246 AA
molecular weight:27502,00000 Da
isoelectric point:9,47178
aromaticity:0,08537
hydropathy:-0,66220

Domains

Domains [InterPro]
Protein sequence: R9TQ04
1 246
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Paenibacillus phage PG1
[NCBI]
754053 No lineage information
Host Paenibacillus glucanolyticus
[NCBI]
59843 Bacteria > Firmicutes > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AGN33742.1 [NCBI]
Genbank nucleotide accession
HQ332138 [NCBI]
CDS location
range 13882 -> 14622
strand +
CDS
GTGGGGAGGGGAGTGACAAGGATGTCGTACAAGATAGTACAGAAGGGGAACAAACACACAAACAGCAGCAGTAGAGATGGACATGTGCCTTATGTGATCGTGAACCACATTTCAGCCGGTTCTATGGGAAGCATGGATAATTGGTTCACTTCTTCAGGTAACAAGGTAAGTAGCGCACACTTCGGCGTTTCTAAGAAAGGTGAGATCCATCAATACGTTCCGATTGAGCGGATGGCATGGGCCAACGGTCTGAGTAAGTGGGAACAGGAAAAAGCTGATGCCGCTGTTGTGCGAAACAATCCTAGCCTTAACCCGAATAAATACACTGTTAGTATCGAGCATGAAGGCACTGACGGGCAACTGACGGACGCACAGTTCGCCGCATCGGTTTGGTTGCACAAATACATCCAGTCCGAAATAAAACGGCTGTATGGGCGCGATATGAAGCTTGACGAGTATCATGTGATTGGACATTTCCAAGTGGATCCTAAACGAAAGCCGAATTGCCCTGGTCCTAAGTTCCCATGGGATCAGTTATACAAAGAATTAAAGAAAGTTGGTGCTGCTAAAGTGGAGCAACAGAAAGTGAAGGTCCTTGTAAACGGCAAGAAGGTTGCAGATGGATACTTAGACGGTGGAACAACGTACACGCCTTCTAGGGCGGTTGCAGAAGCTCTAGGAGCGTCCGTTAGATGGGATAAAGAGAACTTAACAGTGCTTATCACAAAGGAGGAAAAATAA

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:0009254 peptidoglycan turnover Biological process Inferred from Electronic Annotation (TreeGrafter)
GO:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation (UniProt)
GO:0071555 cell wall organization 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

PDB ID: upi00034282bf_model

Method: AlphaFold3 Non-commercial

Resolution:

Chain position: A