Protein

UniProt accession
Q9T132 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKVQFKPRATTEAIFVHCSATKPSQNIGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDELAVGSHVKGYNHNSVGVCLVGGIDDKGKFDANFTPAQMQALRSLLVTLLAKYEGSILRAHHDVAPKACPSFDLKRWWEKNELVTSDRG
Physico‐chemical
properties
protein length:151 AA
molecular weight:16900,00000 Da
isoelectric point:9,03055
aromaticity:0,08609
hydropathy:-0,39934

Domains

Domains [InterPro]
IPR034689
1–149
IPR034689
IPR015510
14–133
IPR015510
IPR036505
7–151
IPR036505
IPR006619
1–124
IPR006619
IPR002502
12–132
IPR002502
IPR002502
1–151
IPR002502
IPR036505
11–146
IPR036505
IPR002502
13–132
IPR002502
Protein sequence: Q9T132
1 151
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Yersinia phage phiYeO3-12
[NCBI] 		110457 Autographiviridae > Teetrevirus > Teetrevirus YeO312
Host Yersinia enterocolitica (type O:3)
[NCBI] 		34051 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Yersinia

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
CAB63605.1 [NCBI]
Genbank nucleotide accession
AJ251805 [NCBI]
CDS location
range 10771 -> 11226
strand +
CDS
ATGGCTAAAGTTCAATTCAAACCACGAGCAACCACGGAGGCAATCTTTGTGCATTGCTCAGCAACCAAGCCAAGCCAGAACATTGGCGTTCGTGAGATTCGTCAGTGGCACAAAGAGCAGGGCTGGTTAGACGTAGGATATCACTTCATCATCAAGCGTGATGGCACTGTGGAAGCAGGCCGCGATGAACTGGCTGTAGGTTCCCACGTGAAAGGTTACAACCACAACTCCGTAGGCGTATGCCTCGTGGGTGGGATTGATGATAAAGGCAAGTTCGACGCCAACTTTACACCTGCGCAAATGCAAGCGCTGCGTAGTCTGCTGGTCACGCTGCTGGCGAAGTATGAGGGTTCAATCCTTCGTGCTCACCATGACGTTGCACCCAAAGCCTGCCCGTCCTTCGACTTGAAGCGCTGGTGGGAGAAGAACGAACTGGTTACATCTGACCGAGGGTGA

Gene Ontology

Description Category Evidence (source)
GO:0004386 helicase activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0004519 endonuclease activity Molecular function Inferred from Electronic Annotation (InterPro)
GO:0004527 exonuclease activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0008270 zinc ion binding Molecular function Inferred from Electronic Annotation (UniProt)
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:0030430 host cell cytoplasm Cellular component Inferred from Electronic Annotation (UniProt)
GO:0032897 negative regulation of viral transcription Biological process Inferred from Electronic Annotation (InterPro)
GO:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation (UniProt)
GO:0044659 viral release from host cell by cytolysis Biological process Inferred from Electronic Annotation (InterPro)

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 		HAMAP-Rule:MF_04111

Tertiary structure

PDB ID: upi000009bc1b_model

Method: AlphaFold3 Non-commercial

Resolution: –

Chain position: A