Protein

UniProt accession
A0AB39C2W8 [UniProt]
Protein name
Endolysin
PhaLP type
endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence
MAKVQFTKRQETSQIFVHCSATKATMDVGVREIRQWHKEQGWLDVGYHFIIRRDGTVEAGRDQDAVGSHVKGYNSTSVGVCLVGGIDAKGNPEANFTPQQMSALKGLLHELKGTYPKAVIMAHHDVAPKACPSFDLQRWVRTGELVTSDRG
Physico‐chemical
properties
protein length:151 AA
molecular weight:16692,00000 Da
isoelectric point:8,82587
aromaticity:0,07285
hydropathy:-0,41589

Domains

Domains [InterPro]
IPR036505
7–151
IPR036505
IPR034689
1–149
IPR034689
IPR006619
1–127
IPR006619
IPR002502
1–151
IPR002502
IPR015510
11–142
IPR015510
IPR002502
15–132
IPR002502
IPR002502
11–133
IPR002502
IPR036505
11–144
IPR036505
Protein sequence: A0AB39C2W8
1 151
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Klebsiella phage PMBT70
[NCBI] 		3229741 No lineage information
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
XDJ01125.1 [NCBI]
Genbank nucleotide accession
PP926511 [NCBI]
CDS location
range 22913 -> 23368
strand -
CDS
ATGGCTAAGGTTCAATTCACTAAGCGACAGGAGACCTCTCAGATTTTCGTTCACTGTTCGGCCACAAAGGCAACCATGGATGTGGGTGTCCGTGAGATTCGCCAGTGGCACAAGGAGCAAGGCTGGCTGGACGTGGGTTACCACTTCATCATCCGGCGTGACGGCACCGTAGAGGCTGGTCGTGACCAAGACGCCGTAGGTTCACACGTCAAGGGATACAACTCGACTTCTGTTGGTGTGTGTCTGGTGGGTGGTATCGACGCCAAGGGTAACCCTGAAGCAAACTTCACACCTCAGCAGATGAGCGCACTGAAGGGGTTACTGCACGAGCTGAAGGGGACCTACCCAAAGGCTGTCATTATGGCGCACCACGATGTAGCACCGAAGGCTTGTCCGAGCTTCGACCTGCAACGCTGGGTAAGGACTGGCGAACTAGTCACTTCTGACAGAGGCTGA

Gene Ontology

No Gene Ontology terms available.

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.