Genbank accession
YP_009785900.1 [GenBank]
Protein name
Dpo43 (hypothetical protein)
RBP type
TF
Evidence Phold
Probability 1,00
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 0,998
C3 0,998
C1 0,396
T 0,001
Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).
Protein sequence
MLNNLNQPKGSTIGVLKDGRTIQQAIDGLENPVHYVKDVSITPSALLAVAVEAARLGRTVEFGPGHYTNQGQPFEVDFPLNLDVPVGTFLDFPIIIRGKTVKTVRSVATNLTAAQCPAGTTVIAGDFSAFPVGSVVGVKLGDNTNGSASYNNEAGWDFTTVAAASNTSITLSTGLRWAFDKPEVFTPEYAVRYSGQLSRSSYFIPGDYTSGLNVGDIIRVENIDGTDGVHGNKEYFEMLKVSSIDSSGITVETRLRYTHVNPWIVKTGLVKGSSVTGGGRLKRLEVRGVDTPKVNNVDVDRLIVGLCYNIDVGEITSRGVGEPSSVNFTFCFGRGFLYNVRASGSVSTTDNSALKLMSCPGLIINNCSPHNSTSTGSQGDYGFYVDAYYSPYWCWNDGMSINGIVTETPRSAVTRALWLFGLRGCSVSNLSGAQVFLQGCAKSVFSNIVTPDNLLELRDLSGCIVSGMANNALVLGCWNSTFDLTLFGIGSGSNLNIALRAGAGVTHPETGVPTTLGKNNTFNVKSFSQSSLAVTLSIAQQERPIFGAGCVDVDSANKSVALGSNVIVPTMLPLALTKGIDSGSGWVGGRTKGGIWFDGNYRDAAVRWNGQYVWVADNGSLKAAPTKPDSDSPSNGVVIGP
Physico‐chemical
properties
protein length:641 AA
molecular weight: 67884,62180 Da
isoelectric point:6,12988
aromaticity:0,08580
hydropathy:-0,01045

Tail Spike Domain Segmentation

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

YP_009785900.1
1 641 aa
Domain Start End Length (AA) Confidence
N-terminal 1 73 73 0,6812
Central domain 74 578 506 0,9835
C-terminal 579 641 62 0,9346
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

Host No host information

Coding sequence (CDS)

Genbank protein accession
YP_009785900.1 [NCBI]
Genbank nucleotide accession
NC_047761 [NCBI]
CDS location
range 35950 -> 37875
strand +
CDS
ATGTTAAACAACCTGAACCAGCCGAAAGGCTCAACCATTGGTGTGCTCAAGGATGGGCGCACTATCCAACAGGCAATTGATGGCTTGGAGAACCCGGTGCATTACGTCAAAGATGTGAGCATCACGCCATCGGCACTACTGGCAGTAGCAGTAGAGGCTGCACGACTTGGCCGTACTGTGGAGTTTGGGCCGGGGCACTACACGAACCAAGGTCAACCATTCGAGGTGGACTTCCCGCTTAATCTGGATGTTCCAGTAGGAACCTTTCTGGACTTCCCTATCATCATACGAGGTAAGACCGTGAAGACGGTCAGGAGTGTGGCCACGAACCTCACTGCCGCCCAGTGCCCTGCTGGTACAACAGTCATCGCCGGGGACTTCTCAGCGTTCCCTGTTGGTTCCGTTGTGGGTGTAAAACTTGGGGATAATACCAACGGCTCAGCAAGTTATAACAACGAGGCTGGCTGGGATTTCACTACAGTTGCGGCTGCGTCCAACACCTCAATCACCCTCAGCACAGGGCTACGGTGGGCTTTCGATAAACCGGAAGTGTTTACCCCGGAGTATGCGGTACGATACTCAGGACAGCTGAGTCGGTCATCTTACTTCATACCGGGAGATTACACTTCCGGGCTGAATGTTGGAGATATCATCCGTGTTGAGAACATTGACGGTACTGATGGGGTCCACGGCAACAAGGAATACTTCGAGATGCTTAAGGTATCAAGTATAGATTCCTCAGGTATAACAGTTGAGACGCGCCTTCGGTATACTCATGTGAACCCTTGGATTGTAAAGACAGGGCTGGTCAAAGGCTCTTCGGTAACCGGGGGAGGCCGATTGAAGCGTTTAGAAGTACGCGGTGTCGACACGCCAAAGGTTAACAATGTAGATGTGGACCGCTTAATTGTCGGCCTGTGCTACAACATCGACGTTGGGGAGATAACCTCTCGTGGCGTTGGTGAGCCTTCCTCGGTGAACTTCACGTTCTGCTTCGGTCGTGGCTTCCTGTACAACGTAAGGGCCTCTGGGTCAGTGTCCACAACGGATAACTCAGCGTTAAAGCTGATGAGCTGTCCCGGCCTAATCATTAACAACTGTTCACCTCACAACTCTACATCCACTGGTTCTCAAGGTGACTACGGGTTCTACGTTGACGCTTATTACTCTCCGTACTGGTGCTGGAACGACGGCATGTCTATCAATGGGATTGTCACTGAGACACCTAGGTCGGCTGTGACACGTGCGTTGTGGCTGTTTGGTCTGAGAGGCTGTTCTGTTAGTAACCTGTCCGGTGCCCAAGTGTTCCTACAGGGCTGCGCTAAGTCGGTGTTCTCCAACATCGTCACCCCGGACAATCTACTTGAACTACGTGACCTGTCTGGTTGCATTGTATCCGGCATGGCAAATAACGCGCTGGTACTCGGCTGTTGGAACTCGACGTTCGACCTTACGCTATTTGGTATTGGCTCTGGGTCAAACCTTAACATAGCGTTACGGGCCGGGGCTGGCGTTACCCACCCGGAGACTGGTGTGCCCACTACCCTCGGTAAGAACAACACGTTCAACGTTAAGAGTTTTAGCCAATCGTCGCTTGCTGTCACCCTAAGTATCGCCCAGCAAGAGCGGCCAATCTTCGGTGCTGGCTGTGTTGACGTCGATTCTGCGAACAAGTCAGTCGCTCTCGGTAGTAACGTTATCGTTCCGACCATGCTCCCTCTAGCGTTAACCAAAGGTATCGACTCCGGCTCTGGCTGGGTTGGTGGCAGGACTAAGGGTGGTATCTGGTTCGATGGTAACTACCGCGATGCGGCGGTGCGCTGGAACGGTCAGTACGTATGGGTGGCTGACAATGGTTCACTCAAGGCAGCACCTACTAAACCGGATTCTGACTCGCCTTCTAATGGTGTGGTTATTGGTCCATAA

Genome Context

Tertiary structure

YP_009785900.1
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 GO
GO:0098996
GO:IDA RBP symbiont entry into host cell via disruption of host cell glycocalyx ECO:0000314
Validated by sequence identity UniProt
A0A0U3C9T3
ECO:0000269:FUNCTION:32117192 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 some K47-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor (PubMed:32117192) PMID 32117192
Validated by sequence identity UniProt
A0A0U3C9T3
protein_existence:evidence_at_protein_level 1: Evidence at protein level —
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
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