- UniProt accession
- A0A219YHG0 [UniProt]
- Protein name
- Depolymerase 1, capsule K8-specific
- RBP type
-
TFTSPTSPTSPTSP
- Seq2Symm
-
C3 confidence 0,999
Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).C3 0,999 C1 0,004 C6 0,000 - Protein sequence
-
MDQDIKTVIQYPVGATEFDIPFDYLSRKFVRVSLVADDNRRLLSNITEYRYVSKTRVKLLVETTGFDRVEIRRFTSASERIVDFSDGSVLRAADLNVSQIQSAHIAEEARDAALMAMPEDDAGNLDARNRKIVRLAPGEAGTDAINKNQLDETLGEAGGILSDFEDVRDEIIQYISKFTDDTGAVRGVSYVYNNGRALGGETGFHIDITPPPLGVPYLSINGSKQYRGYHFTYDPITGNVQGLATPLEKDDFVVATTTESVTPIEDLYASTQGASMIGTLSGSTVEERIAEVEQSVLDSIDGIRVDSFIGMTDSGAIDAAIAEALRVNSYVKFSPRVYTVDRPVILPSKTVLVGTQGLTKIVASASWNGPVVMSKDAPAGDYLTINVPSAMVYGVYIFGIIIESGWKGTTDDSRYHTECLRIYGAGTILKGVRVGKCRGDGANLGGRGLTAIDYGAPSLYSDVRADLIGKNGITIGGSSDNHTQNIVVRNAGLLEHDVYYCIGIGPGGGTRGNEYHTWHSGDAQITPLYQNRPKYGLYLAGWDTYITNGHFEGAASAQIANFGGRNQVTNVRAYSTWDQDKCTVLVAGPAFKFVGNIGAPMNNVPANRCHAFQLGTADIQVNQVEITAQVNGQKFVNYVNAGGSNSIAVRGTLGIAGASGIGTLVTGTVPDDNELTIIAEPYKGKRLGLNLILTGDKGLTCRDVNSTGQISGVNALLTGKVMLTGLSSDIPTTPGTVYVDSNGNLKVKL
- Physico‐chemical
properties -
protein length: 749 AA molecular weight: 80190,07140 Da isoelectric point: 5,18027 aromaticity: 0,07610 hydropathy: -0,13632
Domains
Domain architecture
A0A219YHG0
1
749 aa
ATT 3–127 · STR 310–655 ·
ATT Attachment Domain
STR Structural Domain
RBD Receptor-Binding Domain
CBM Carbohydrate-Binding Module
LEC Lectin-like Domain
ENZ Enzymatic Domain
CHP Intramolecular Chaperone
LNK Linker/Spacer Domain
TAS Tail-Associated Structural
TTP Tail Tubular Protein
UNK Uncharacterized Domain
Unmapped
Proteins with similar domain architecture
Tail Spike Domain Segmentation
Segmented into three structural domains: N-terminal, central, and C-terminal.
Domain layout
A0A219YHG0
1
749 aa
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 313 | 313 | 0,9975 |
| Central domain | 314 | 706 | 394 | 0,9882 |
| C-terminal | 707 | 749 | 42 | 0,8948 |
N-terminal
Central domain
C-terminal
View these domains on the 3D structure via the Color by → Tail spike option in the Tertiary structure section below.
Taxonomy
Coding sequence (CDS)
No CDS data available.
Genome Context
Gene Ontology
| Description | Category | Evidence (source) | |
|---|---|---|---|
| GO:0098015 | virus tail | Cellular Component | IEA:UniProtKB-KW (UniProt) |
| GO:0098671 | adhesion receptor-mediated virion attachment to host cell | Biological Process | IEA:UniProtKB-KW (UniProt) |
| GO:0098994 | symbiont entry into host cell via disruption of host cell envelope | Biological Process | IEA:UniProtKB-KW (UniProt) |
| GO:0098996 | symbiont entry into host cell via disruption of host cell glycocalyx | Biological Process | IEA:UniProtKB-KW (UniProt) |
Tertiary structure
Structure ID
Source
Method
Resolution
Oligomeric state
Experimental validation
Experimentally validatedA wet-lab result is recorded for this protein, or for its sequence: a solved structure, an experimental GO annotation, a UniProt ECO:0000269 assertion, or a GenBank /experiment= qualifier.
| Tier | Source | Assay | Claim | Reference |
|---|---|---|---|---|
| Experimentally validated |
UniProt
A0A219YHG0
|
ECO:0000269:FUNCTION:28676686 RBP | Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K8-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor (PubMed:28676686) | PMID 28676686 |
Rows marked “Validated by sequence identity” come from a different entry carrying the same sequence — the experiment was not performed on this protein.