Genbank accession
APZ82768.1 [GenBank]
Protein name
Kpv74_56 (putative tail fiber protein)
RBP type
TSP
Evidence DepoScope
Probability 1,00
TSP
Evidence RBPdetect
Probability 0,91
TSP
Evidence RBPdetect2
Probability 0,99
TSP
Evidence DepoCatalog
Probability 1,00
Seq2Symm
C3 confidence 1,000
C3 1,000
C1 0,002
D2 0,000
Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).
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

View on InterPro
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

Tail Spike Domain Segmentation

Segmented into three structural domains: N-terminal, central, and C-terminal.

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 +
CDS
ATGGCACTAGTAGATTTAGTGAGGGCTGGGGGATATTCTATTGAGTACCCGCAATTCTCCAGTATGGCTAAGCTAAAAGAGTTCCCACACTCTGAGGACGGGAAACTTGTTAGGTTGTTGTCTTGGCATGAAGGGGTTGGTTTAGGTGGTGGGCTGTTTAAGGTCAGCACTAGCAGCACCGCTACAGGTAACGACGGTACTGTAGTAGTAGCTAGTAATGGGGTGCGGCTGCTTCGAGTAGTAAACGGACCTATCTGGGCGGATATGTTTGGTGCACTACCGAATTCAGACATAGACAGTATGCCAGCAGTAGCTGCGGCTTATGCGTACGCTGCTTCTGTGAATACGGACCTGTATATAGGGGTGGCGACTTACAAATTCAAGGGGAGCACCCCAATTAATATAGACCCATCCAGGGCCGGTATTATTGGTTATCAAGGTAAGGTGCGCATTGACTGCTCCGAGTTTACTGGCTCGATTGTGTTTTCTATAAACAGCAGCTATAGCTACACCCCCGCAGCCTACTACAACAACCTTAGTCCGGCCCTGCAGGGGCTGTACGTGTTGGGTGCTAAAACGTCCGGTGTAGACGGTCTACTGGTTGGTAGGGAAACAGTGGGGGCGGACAAGAGCTATAACGGGCAGACAGAGATTCGTGAGTGCACGTTCGATAAGTTCGACCGCAACATCCGAATGGGGCACAACTCTTGGCGCTTTGTGTTCTACAAAGTAAACAGCCTAAACGCTCTCAGTCCTAACGGGATACTGTACGTACCGGCTGGGCTGGATGACTCTGGGGAGATTCTGTCGTTCTACCACTGCCAGTTCTTTGACGGTGCAGGTAGTAATATCCGATTATCTTGCTCCTCGTATACTATGGTATTTAATACTTGCTCGTTCCTGAACATCACGTTCTTTGTGGATTCGGCGAGTAGTGCGACAGTAACTTGCAATGGGTGCAACTTCGAGAACCCGGGAAGTGCTAGTACCCGTAGATACGTTGACATTAGTGCTGGGCACACTAACGTATTCAACATTATTGGGGGCAGTATAGTCACAAACAGCAACCCTGGACAGACCCAGGCGCTACTGTATGTCTCTACCAACAATCTCCTGAACCTTGTAGGTGTAACTGTCCCTTACGGCGGGCACTATCAGCAGGAGCAGGAGCTCGGCTATCACGCATTCATTGGTGGGGCCGGTACAGTAACAGCCTCTGGGGTTATGCTGCAGCTGCGGAACGGGGCAGGTACGTGTCCTTTGCACTCTAGTCTTAGCACGTTCAGTAACTGGGATTTTGGTTATGGGAACCTGAATGCTTGGACGGTAGATAAGGGGGCTGGTACATCCTCCGTGGTAGAGTACTTGGCTAACGCTGGACCTAAAGGTACAGGGGGAGCTATGCGAGTTGCTCCTGTAAGTGTCGGTACTAACGTATCGCAAGTACAGGCAGTAACCAACCCCGGCATGTTCAGTATGTCCTGCATGGTGAACATTGCGACGACCTCCGGTAACGCAGGGCAGATATCTATTGGGTTCTTGGATGCTGCCGGTAACAGTATACCTGGCGGGGTATCAGCTAACCTGGGCACCACTACGGGTTGGAAGGTAATCGGCAAGAACACCCTGCGTGGCAAAGTCCCAATCGGTGCTAAGCAGATTCGTGTGAACGTTCAGACCGTGGCTGGTGCAGACGTTAAGTACGCGTACTTGCTGTGCAATGTGGTCAAGTAA

Genome Context

Tertiary structure

APZ82768.1
1 / 2
Structure ID
Source
Method
Resolution
Oligomeric state

Experimental validation

Validated by sequence identity

The 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