UniProt accession
A0ABZ0S344 [UniProt]
Protein name
Membrane protein
RBP type
TSP
Evidence DepoScope
Probability 1,00
Protein sequence
MAYGIWTQPVGPGPATPAPLFIDSGSTFPQFKNSIRGSFNFNGAGRSFPISGWDGSGQIVIVPTGSLCWQWEVPPNLVPDVYCVNDIYVENNSSFRVTLNQNPGSNPLFDCGFNVYQIWPRADRNYGITFSNTADYFSISDSGVVGQCIWAWQGTINNSLQIPNIGGFNMTNAVVFANWSDGGVGLSYTSDDRIIRVYQNRPYVNGNTNEGGSVFVRIAVFCNGAGVPEHNGGLNIYSPGTTQCVFSTNRTPFTVDTFIGSGGGNTGMSYPMIPLTSGIGAIKGQGSGWRYQQMRSHTMSGSSIGTGYGRYLFQWDQNYDLGADTVVNLSVPVMNAAKVFAGL
Physico‐chemical
properties
protein length:343 AA
molecular weight: 36998,80640 Da
isoelectric point:5,28417
aromaticity:0,13120
hydropathy:-0,13499

Domains

Domains [InterPro]
DC_1434
ATT
1–40
IPR045604
STR
22–315
A0ABZ0S344
1 343
Architecture
ATT
STR
ATT 1-40 | STR 41-315 |
Legend: ATT STR RBD CBM LEC ENZ CHP LNK TAS TTP UNK Unmapped

Tail Spike Domain Segmentation

Tail Spike Domain Segmentation

This protein has been segmented into three structural domains: N-terminal, central domain, and C-terminal.

Domain Layout
N-terminal
Central
C-terminal
A0ABZ0S344
1 343
Domain Start End Length (AA) Confidence
N-terminal 1 92 92 0,0027
Central domain 93 291 200 0,0219
C-terminal 292 343 51 0,9967
Legend: N-terminal Central domain C-terminal
3D Structure with Domain Coloring

The structure is colored according to the domain segmentation: N-terminal (blue), Central (green), C-terminal (pink).

Domain Coloring
N-terminal
1-92
Central
93-291
C-terminal
292-343

Taxonomy

  Name Taxonomy ID Lineage
Phage Escherichia phage vB-EcoP-XT18
[NCBI]
3093889 Uroviricota > Caudoviricetes > Mktvariviridae > Kuravirus > Kuravirus XT18
Host Escherichia coli
[NCBI]
562 cellular organisms > Bacteria > Pseudomonadati > Pseudomonadota > Gammaproteobacteria > Enterobacterales

Coding sequence (CDS)

Coding sequence (CDS)

No CDS data available.

Genome Context

Genome Context

Tertiary structure

PDB ID
68b0ed45ba4d0c503602a42714d51d701eef4aaa42820e1da60c3605f45f397a
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,8220
Oligomeric State monomer
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50