Protein
- UniProt accession
- P27380 [UniProt]
- Protein name
- Transglycosylase
- PhaLP type
-
VAL
evidence: GO annotation
probability: 99 % (predicted by ML model)
- Protein sequence
-
MSGALQWWETIGAASAQYNLDPRLVAGVVQTESSGNPRTTSGVGAMGLMQLMPATAKSLGVTNAYDPTQNIYGGAALLRENLDRYGDVNTALLAYHGGTNQANWGAKTKSYPGKVMKNINLLFGNSGPVVTPAAGIAPVSGAQEMTAVNISDYTAPDLTGLTMGAGSPDFTGGASGSWGEENIPWYRVDKHVANAAGSAYDAVTDAVSAPVEAAGNYALRGVVIIAAVAIVVVGLYFLFQDEINSAAMKMIPAGKAAGAAAKALA
- Physico‐chemical
properties -
protein length: 265 AA molecular weight: 27074,00000 Da isoelectric point: 5,12838 aromaticity: 0,07547 hydropathy: 0,10981
Domains
Domains [InterPro]
Taxonomy
Coding sequence (CDS)
Coding sequence (CDS)
Genbank protein accession
AAX45925.1
[NCBI]
Genbank nucleotide accession
AY848689
[NCBI]
CDS location
range 12190 -> 12987
strand +
strand +
CDS
ATGTCTGGTGCGCTGCAATGGTGGGAAACTATCGGCGCGGCTTCGGCGCAATATAACCTTGACCCGCGCCTAGTGGCCGGGGTTGTTCAAACGGAATCTTCCGGCAACCCCCGCACCACTTCCGGCGTGGGCGCTATGGGTTTAATGCAGCTTATGCCAGCGACCGCCAAAAGTTTAGGCGTAACAAACGCCTATGACCCGACACAAAACATTTATGGTGGCGCTGCCCTTTTGCGTGAAAACCTTGATAGATACGGCGATGTTAATACGGCGTTGCTTGCTTATCACGGCGGAACTAATCAAGCAAATTGGGGCGCTAAAACTAAATCCTATCCGGGTAAGGTTATGAAAAATATCAATTTGCTTTTCGGTAATAGCGGCCCGGTAGTAACGCCAGCGGCTGGAATCGCGCCAGTATCCGGGGCGCAAGAAATGACCGCCGTTAATATCAGCGACTATACCGCGCCTGATTTAACGGGGCTTACTATGGGGGCGGGTAGTCCTGACTTTACAGGCGGGGCTAGTGGTTCATGGGGCGAAGAAAACATTCCGTGGTATCGCGTAGATAAGCACGTTGCGAACGCGGCGGGTTCCGCTTATGACGCTGTTACCGATGCAGTAAGCGCCCCGGTTGAAGCAGCAGGAAACTACGCCTTGCGGGGCGTGGTAATTATTGCGGCGGTGGCAATTGTTGTTGTTGGTTTGTACTTCCTTTTTCAAGATGAAATTAACAGCGCCGCCATGAAAATGATTCCAGCCGGTAAGGCGGCAGGGGCAGCGGCTAAGGCTTTGGCATGA
Genbank protein accession
AAX45907.1
[NCBI]
Genbank nucleotide accession
AY848689
[NCBI]
CDS location
range 12535 -> 12987
strand +
strand +
CDS
ATGAAAAATATCAATTTGCTTTTCGGTAATAGCGGCCCGGTAGTAACGCCAGCGGCTGGAATCGCGCCAGTATCCGGGGCGCAAGAAATGACCGCCGTTAATATCAGCGACTATACCGCGCCTGATTTAACGGGGCTTACTATGGGGGCGGGTAGTCCTGACTTTACAGGCGGGGCTAGTGGTTCATGGGGCGAAGAAAACATTCCGTGGTATCGCGTAGATAAGCACGTTGCGAACGCGGCGGGTTCCGCTTATGACGCTGTTACCGATGCAGTAAGCGCCCCGGTTGAAGCAGCAGGAAACTACGCCTTGCGGGGCGTGGTAATTATTGCGGCGGTGGCAATTGTTGTTGTTGGTTTGTACTTCCTTTTTCAAGATGAAATTAACAGCGCCGCCATGAAAATGATTCCAGCCGGTAAGGCGGCAGGGGCAGCGGCTAAGGCTTTGGCATGA
Gene Ontology
Description | Category | Evidence (source) | |
---|---|---|---|
GO:0000270 | peptidoglycan metabolic process | Biological process | Inferred from Electronic Annotation (UniProt) |
GO:0003796 | lysozyme activity | Molecular function | Inferred from Electronic Annotation (UniProt) |
GO:0008933 | peptidoglycan lytic transglycosylase activity | Molecular function | Inferred from Electronic Annotation (TreeGrafter) |
GO:0016020 | membrane | Cellular component | Inferred from Electronic Annotation (UniProt) |
GO:0031640 | killing of cells of another organism | Biological process | Inferred from Electronic Annotation (UniProt) |
GO:0039641 | viral inner membrane | Cellular component | Inferred from Electronic Annotation (UniProt) |
GO:0042742 | defense response to bacterium | Biological process | Inferred from Electronic Annotation (UniProt) |
GO:0055036 | virion membrane | Cellular component | Inferred from Electronic Annotation (UniProt) |
GO:0098932 | symbiont entry into host cell via disruption of host cell wall peptidoglycan | Biological process | Inferred from Electronic Annotation (UniProt) |
GO:0098994 | symbiont entry into host cell via disruption of host cell envelope | Biological process | Inferred from Electronic Annotation (UniProt) |
Enzymatic activity
EC Number | Entry Name | Reaction Catalyzed | Classification | Evidence | Source |
---|---|---|---|---|---|
4.2.2.n1 |
peptidoglycan lytic exotransglycosylase
aka exomuramidase; murein lyase F |
in the MurNAc residue |
Lyases
Carbon-oxygen lyases
Acting on polysaccharides
|
experimental evidence used in manual assertion
ECO:0000269 |
PubMed:10931330 |
Tertiary structure
No tertiary structures available.