- Genbank accession
- APZ82768.1 [GenBank]
- Protein name
- Kpv74_56 (putative tail fiber protein)
- RBP type
-
TSPTSPTSPTSP
- Seq2Symm
-
C3 confidence 1,000
Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).C3 1,000 C1 0,002 D2 0,000 - Protein sequence
-
MALVDLVRAGGYSIEYPQFSSMAKLKEFPHSEDGKLVRLLSWHEGVGLGGGLFKVSTSSTATGNDGTVVVASNGVRLLRVVNGPIWADMFGALPNSDIDSMPAVAAAYAYAASVNTDLYIGVATYKFKGSTPINIDPSRAGIIGYQGKVRIDCSEFTGSIVFSINSSYSYTPAAYYNNLSPALQGLYVLGAKTSGVDGLLVGRETVGADKSYNGQTEIRECTFDKFDRNIRMGHNSWRFVFYKVNSLNALSPNGILYVPAGLDDSGEILSFYHCQFFDGAGSNIRLSCSSYTMVFNTCSFLNITFFVDSASSATVTCNGCNFENPGSASTRRYVDISAGHTNVFNIIGGSIVTNSNPGQTQALLYVSTNNLLNLVGVTVPYGGHYQQEQELGYHAFIGGAGTVTASGVMLQLRNGAGTCPLHSSLSTFSNWDFGYGNLNAWTVDKGAGTSSVVEYLANAGPKGTGGAMRVAPVSVGTNVSQVQAVTNPGMFSMSCMVNIATTSGNAGQISIGFLDAAGNSIPGGVSANLGTTTGWKVIGKNTLRGKVPIGAKQIRVNVQTVAGADVKYAYLLCNVVK
- Physico‐chemical
properties -
protein length: 577 AA molecular weight: 60741,75760 Da isoelectric point: 7,94181 aromaticity: 0,09879 hydropathy: 0,07279
Domains
Domain architecture
APZ82768.1
1
577 aa
RBD 18–81 ·
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
APZ82768.1
1
577 aa
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 98 | 98 | 0,9874 |
| Central domain | 99 | 417 | 320 | 0,9876 |
| C-terminal | 418 | 577 | 159 | 0,9911 |
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)
Genbank protein accession
APZ82768.1
[NCBI]
Genbank nucleotide accession
KY385423
[NCBI]
CDS location
range 42255 -> 43988
strand +
strand +
CDS
ATGGCACTAGTAGATTTAGTGAGGGCTGGGGGATATTCTATTGAGTACCCGCAATTCTCCAGTATGGCTAAGCTAAAAGAGTTCCCACACTCTGAGGACGGGAAACTTGTTAGGTTGTTGTCTTGGCATGAAGGGGTTGGTTTAGGTGGTGGGCTGTTTAAGGTCAGCACTAGCAGCACCGCTACAGGTAACGACGGTACTGTAGTAGTAGCTAGTAATGGGGTGCGGCTGCTTCGAGTAGTAAACGGACCTATCTGGGCGGATATGTTTGGTGCACTACCGAATTCAGACATAGACAGTATGCCAGCAGTAGCTGCGGCTTATGCGTACGCTGCTTCTGTGAATACGGACCTGTATATAGGGGTGGCGACTTACAAATTCAAGGGGAGCACCCCAATTAATATAGACCCATCCAGGGCCGGTATTATTGGTTATCAAGGTAAGGTGCGCATTGACTGCTCCGAGTTTACTGGCTCGATTGTGTTTTCTATAAACAGCAGCTATAGCTACACCCCCGCAGCCTACTACAACAACCTTAGTCCGGCCCTGCAGGGGCTGTACGTGTTGGGTGCTAAAACGTCCGGTGTAGACGGTCTACTGGTTGGTAGGGAAACAGTGGGGGCGGACAAGAGCTATAACGGGCAGACAGAGATTCGTGAGTGCACGTTCGATAAGTTCGACCGCAACATCCGAATGGGGCACAACTCTTGGCGCTTTGTGTTCTACAAAGTAAACAGCCTAAACGCTCTCAGTCCTAACGGGATACTGTACGTACCGGCTGGGCTGGATGACTCTGGGGAGATTCTGTCGTTCTACCACTGCCAGTTCTTTGACGGTGCAGGTAGTAATATCCGATTATCTTGCTCCTCGTATACTATGGTATTTAATACTTGCTCGTTCCTGAACATCACGTTCTTTGTGGATTCGGCGAGTAGTGCGACAGTAACTTGCAATGGGTGCAACTTCGAGAACCCGGGAAGTGCTAGTACCCGTAGATACGTTGACATTAGTGCTGGGCACACTAACGTATTCAACATTATTGGGGGCAGTATAGTCACAAACAGCAACCCTGGACAGACCCAGGCGCTACTGTATGTCTCTACCAACAATCTCCTGAACCTTGTAGGTGTAACTGTCCCTTACGGCGGGCACTATCAGCAGGAGCAGGAGCTCGGCTATCACGCATTCATTGGTGGGGCCGGTACAGTAACAGCCTCTGGGGTTATGCTGCAGCTGCGGAACGGGGCAGGTACGTGTCCTTTGCACTCTAGTCTTAGCACGTTCAGTAACTGGGATTTTGGTTATGGGAACCTGAATGCTTGGACGGTAGATAAGGGGGCTGGTACATCCTCCGTGGTAGAGTACTTGGCTAACGCTGGACCTAAAGGTACAGGGGGAGCTATGCGAGTTGCTCCTGTAAGTGTCGGTACTAACGTATCGCAAGTACAGGCAGTAACCAACCCCGGCATGTTCAGTATGTCCTGCATGGTGAACATTGCGACGACCTCCGGTAACGCAGGGCAGATATCTATTGGGTTCTTGGATGCTGCCGGTAACAGTATACCTGGCGGGGTATCAGCTAACCTGGGCACCACTACGGGTTGGAAGGTAATCGGCAAGAACACCCTGCGTGGCAAAGTCCCAATCGGTGCTAAGCAGATTCGTGTGAACGTTCAGACCGTGGCTGGTGCAGACGTTAAGTACGCGTACTTGCTGTGCAATGTGGTCAAGTAA
Genome Context
Tertiary structure
Structure ID
Source
Method
Resolution
Oligomeric state
Experimental validation
Validated by sequence identityThe evidence was produced on a different entry with an identical sequence. Strong, but the experiment was not done on this protein.
| Tier | Source | Assay | Claim | Reference |
|---|---|---|---|---|
| Validated by sequence identity |
UniProt
A0A1P8VW90
|
ECO:0000269:FUNCTION:28988127 RBP | Functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K2-type polysaccharides of Klebsiella pneumoniae capsule (PubMed:28988127) | PMID 28988127 |
| Literature-linked |
bioRxiv
https://doi.org/10.1101/2025.09.09.675204
|
literature_xref | DepoCatalog: Mapping the Diversity of 105 Recombinant Klebsiella Phage Depolymerases Across Sequence, Structure, and Substrate Specificity | PMID https://doi.org/10.1101/2025.09.09.675204 |
Rows marked “Validated by sequence identity” come from a different entry carrying the same sequence — the experiment was not performed on this protein.
Literature
| Title | Authors | Date | PMID | Source |
|---|---|---|---|---|
| Complete genome sequence of Klebsiella pneumoniae bacteriophage vB_KpnP_KpV74 | Komisarova,E.V., Krasilnikova,V.M., Kislichkina,A.A. and Volozhantsev,N.V. | 2017-09-14 | — | GenBank |
| DepoCatalog: Mapping the Diversity of 105 Recombinant Klebsiella Phage Depolymerases Across Sequence, Structure, and Substrate Specificity | DepoCatalog: Mapping the Diversity of 105 Recombinant Klebsiella Phage Depolymerases Across Sequence, Structure, and Substrate Specificity | — | https://doi.org/10.1101/2025.09.09.675204 | bioRxiv |