Protein

UniProt accession
A0A0E3M152 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKVQFKPRATTEAIFVHCSATKPSQNIGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDELAVGSHVKGYNHNSVGVCLVGGIDDKGKFDANFTPAQMQALRSLLVTLLAKYEGSVLRAHHDVAPKACPSFDLNRWWEKNELVTSDRG
Physico‐chemical
properties
protein length:151 AA
molecular weight:16872,00000 Da
isoelectric point:8,80833
aromaticity:0,08609
hydropathy:-0,39868

Domains

Domains [InterPro]
IPR002502
1–151
IPR002502
IPR006619
1–124
IPR006619
IPR036505
11–146
IPR036505
IPR002502
13–132
IPR002502
IPR002502
12–132
IPR002502
IPR015510
14–133
IPR015510
IPR034689
1–149
IPR034689
IPR036505
7–151
IPR036505
Protein sequence: A0A0E3M152
1 151
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Citrobacter phage phiCFP-1
[NCBI] 		1610508 Autographiviridae > Teetrevirus > Teetrevirus CFP1
Host Citrobacter freundii
[NCBI] 		546 Bacteria > Proteobacteria > Gammaproteobacteria > Enterobacteriales > Enterobacteriaceae > Citrobacter

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AKA62134.1 [NCBI]
Genbank nucleotide accession
KP313531 [NCBI]
CDS location
range 10596 -> 11051
strand +
CDS
ATGGCTAAAGTTCAATTCAAACCACGAGCAACCACGGAGGCAATCTTTGTGCATTGCTCAGCAACCAAGCCAAGCCAGAACATTGGCGTTCGTGAGATTCGTCAGTGGCACAAAGAGCAGGGCTGGTTAGACGTAGGATATCACTTCATCATCAAGCGTGATGGCACTGTGGAAGCAGGCCGCGATGAACTGGCTGTAGGTTCCCACGTGAAAGGTTACAACCACAACTCCGTAGGCGTATGCCTCGTGGGTGGGATTGATGATAAAGGCAAGTTCGACGCCAACTTTACACCTGCGCAAATGCAAGCGCTGCGTAGTCTGCTGGTCACGCTGCTGGCGAAGTATGAGGGTTCAGTCCTTCGTGCTCACCATGACGTTGCACCCAAAGCCTGCCCGTCCTTCGACTTGAATCGCTGGTGGGAGAAGAACGAACTGGTTACATCTGACCGAGGGTGA

Gene Ontology

Description Category Evidence (source)
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

No tertiary structures available.