Protein

UniProt accession
A0A170PBB1 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MPKVQFKERTATDYLVVHCAATKASMDIGVREIRQWHVQKGWLDIGYHFVIRRNGTVEDGRPHNVIGAHVEGFNARSLGICLAGGIDDKGNPQNNFTPEQFASLKLLLLAQKRTYPNAKIVGHHDLFAGKACPSFKVADWLKSVGI
Physico‐chemical
properties
protein length:146 AA
molecular weight:16222,00000 Da
isoelectric point:9,40454
aromaticity:0,08904
hydropathy:-0,24178

Domains

Domains [InterPro]
IPR002502
11–134
IPR002502
IPR002502
13–133
IPR002502
IPR036505
10–143
IPR036505
IPR036505
6–145
IPR036505
IPR002502
1–134
IPR002502
IPR034689
1–146
IPR034689
IPR006619
1–127
IPR006619
IPR015510
10–134
IPR015510
Protein sequence: A0A170PBB1
1 146
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Pseudomonas phage shl2
[NCBI] 		1729933 Autographiviridae > Ghunavirus > Ghunavirus shl2
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
CUR50697.1 [NCBI]
Genbank nucleotide accession
LN889756 [NCBI]
CDS location
range 5650 -> 6090
strand -
CDS
ATGCCAAAAGTTCAATTCAAGGAGCGCACCGCAACCGACTATCTCGTGGTCCACTGTGCTGCAACCAAAGCGTCCATGGACATCGGTGTCCGTGAGATCCGTCAATGGCACGTCCAGAAAGGCTGGCTCGACATCGGCTATCACTTTGTGATTCGTCGTAACGGCACGGTCGAGGATGGTCGCCCACACAACGTGATCGGCGCACACGTCGAAGGGTTCAACGCTCGCTCGCTTGGCATCTGCCTCGCTGGTGGCATCGACGATAAAGGCAACCCTCAGAACAACTTCACGCCTGAGCAATTCGCTTCGCTCAAGCTGCTGCTGCTGGCCCAGAAGCGCACCTACCCGAACGCCAAGATCGTGGGACACCATGACCTGTTCGCTGGCAAAGCGTGCCCTTCCTTCAAGGTCGCTGACTGGCTCAAGTCGGTCGGGATTTAA

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.