Protein
- Protein accession
- A0A9Y1DSM1 [UniProt]
- Representative
- –
- Source
- UniProt
- Protein name
- Endolysin
- Lysin probability
- 100%
- PhaLP type
- N/A
- Protein sequence
-
MKLSTRGKNLIKSHEGLVLAVYPDPATGGAPYTAGYGHTGSDVKPGMKVTQAMADAWFDKDVAKFESGVSSLITAPTTQGQFDAMVSLAYNIGLGNFGKSTLLKKHNARCYTCAADQFRVWNRANGKVMNGLTKRRAAEREVYMS
- Physico‐chemical
properties -
protein length: 145 AA molecular weight: 15683,0 Da isoelectric point: 9,63 hydropathy: -0,34
Cluster Membership
This protein is the only member recorded for this cluster.
Domains
Domains [InterPro]
No domain annotations available.
Taxonomy
| Name | Taxonomy ID | Lineage | |
|---|---|---|---|
| Phage |
Klebsiella phage vB_Kpn_ZC2 [NCBI] |
2982901 | No lineage information |
| Host | No host information | ||
Coding sequence (CDS)
Coding sequence (CDS)
CDS Source ID
CDS Source
OP481875
[NCBI]
CDS location
range 12195 -> 12632
strand +
strand +
CDS
ATGAAACTATCAACGCGCGGAAAGAATTTAATTAAATCTCATGAGGGGCTGGTGCTTGCAGTCTATCCCGACCCGGCGACCGGAGGCGCTCCGTACACCGCTGGATACGGTCATACCGGAAGCGACGTTAAGCCGGGAATGAAGGTCACGCAGGCAATGGCTGACGCATGGTTTGATAAAGACGTAGCGAAATTTGAAAGCGGCGTCTCATCACTCATCACTGCGCCGACAACTCAGGGCCAGTTTGATGCAATGGTGTCTCTGGCCTATAACATTGGCCTTGGTAACTTTGGCAAATCAACGCTTCTGAAAAAGCATAACGCCCGCTGCTATACCTGCGCTGCCGACCAGTTCCGGGTATGGAATCGTGCGAACGGCAAGGTAATGAACGGACTCACAAAGCGCCGCGCAGCTGAGCGTGAGGTATACATGTCATGA
Gene Ontology
| Description | Category | Evidence (source) | |
|---|---|---|---|
| GO:0003796 | lysozyme activity | molecular function | None (UniProt) |
| GO:0009253 | peptidoglycan catabolic process | biological process | None (UniProt) |
| GO:0016998 | cell wall macromolecule catabolic process | biological process | None (UniProt) |
| GO:0030430 | host cell cytoplasm | cellular component | None (UniProt) |
| GO:0042742 | defense response to bacterium | biological process | None (UniProt) |
| GO:0044659 | viral release from host cell by cytolysis | biological process | None (UniProt) |
Enzymatic activity
| EC Number | Entry Name | Reaction Catalyzed | Classification | Evidence | Source |
|---|---|---|---|---|---|
| 3.2.1.17 | None | Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. |
match to sequence model evidence used in automatic assertion
ECO:ECO:0000256 |
ARBA:ARBA00000632 |
Tertiary structure
No tertiary structures available.