- Genbank accession
- BAW85692.1 [GenBank]
- Protein name
- tail spike protein
- RBP type
-
TFTSPTSPTSPTSP
- Seq2Symm
-
C3 confidence 0,998
Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).C3 0,998 C1 0,048 D3 0,002 - Protein sequence
-
MTNSLIQPKGSVSKETNIQSIARITGSKIEEVKYLEDGLDIAGLKFVYDSSTETIWKLNGNETGMVDSWNIVDESTIIIVTNISSYQINILEQIILSNDDAAGKIGTSNGLSVQKNLDNISNNITLDTGGVLKDALKFITPEMFVINNEKYIHGTTLDAVPYLQAAIDYGKTNNLPVVLSQRYPCITFPQTYELPRDDGTVYPGWITAGTDQNIDPEPIYTMRAAIRLYNDSVIIGTNMQTTGIRGNWSKTSGPYDLNGTIGVFISGDSGKDGYVRYHMHDLNISGFMIGRLCEGISAFSTEDNLQISSCGITGIFQGEDAVERGFIKLWYNIAGDVFGGQWLTRNYAYASTYLPPYPASDIYRAGWNDSSFTEKYHYYGDTSLNFTHTAYSSLDNFFNTYFFKTANSITTANGGRLSNNKQTGVWPLGEYKGITGRAKTVYSRYGREILNCNILEAKIMWSPRTPFYHTSQSGSWVGNSKIGNVILERVGIINYAAGNTTGNRFNVDNVDPWDPSQNFFPAMVCRGNIGCMDVTRSGHVQQSVSNEINPIVTGGQIHRQYRRSDDTSSYSMLTLQEFKNSWVSKYVFNSSYAFVQPLVFTSSNAQFKYDYGTFTPVLQIAGSYITLTEATGIYHRFGDIIRIHIRLRNSNLTINTAGPFRISGLPFISSSIQTGYTKGSVFTPQATGVTLIPLVTPSTDVLTILKDSAGTSFSHPAGTFDFSFHADFDYVISFNS
- Physico‐chemical
properties -
protein length: 736 AA molecular weight: 81533,27150 Da isoelectric point: 5,69984 aromaticity: 0,11957 hydropathy: -0,23030
Domains
Domain architecture
BAW85692.1
1
736 aa
ATT 1–93 ·
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
BAW85692.1
1
736 aa
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 158 | 158 | 0,9823 |
| Central domain | 159 | 549 | 392 | 0,9791 |
| C-terminal | 550 | 736 | 186 | 0,9668 |
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
BAW85692.1
[NCBI]
Genbank nucleotide accession
LC121098.1
[NCBI]
CDS location
range 1 -> 2211
strand +
strand +
CDS
ATGACAAATAGTTTAATACAACCGAAAGGTTCAGTTTCTAAAGAAACTAATATACAAAGCATAGCAAGAATTACTGGGTCAAAAATTGAGGAAGTAAAATATTTAGAAGATGGACTAGATATTGCTGGTTTAAAATTTGTATATGATTCCAGTACTGAAACAATTTGGAAACTTAATGGGAATGAAACAGGGATGGTTGATTCTTGGAATATTGTAGATGAATCAACTATTATTATAGTAACTAATATATCATCATATCAAATTAATATTTTAGAACAAATTATTCTTTCTAATGATGATGCTGCTGGTAAAATTGGAACTAGTAACGGGTTATCAGTACAAAAAAATTTGGATAATATTTCAAATAATATAACACTTGATACTGGTGGAGTATTAAAAGATGCATTAAAATTTATAACTCCAGAAATGTTTGTCATTAATAATGAAAAATATATACATGGAACTACATTAGATGCAGTTCCTTATTTACAAGCGGCAATTGATTATGGAAAAACTAATAATTTACCAGTTGTATTGTCACAAAGATATCCATGTATAACATTTCCACAAACTTATGAATTACCAAGAGATGACGGTACTGTTTATCCGGGATGGATAACTGCCGGAACTGATCAAAATATAGATCCAGAACCAATTTATACAATGAGGGCAGCAATTAGACTATACAACGATTCTGTTATAATTGGAACAAATATGCAAACTACTGGTATTCGTGGTAATTGGAGCAAAACTAGTGGGCCATATGATTTAAATGGAACAATTGGTGTTTTTATTTCTGGTGATTCTGGAAAAGATGGTTATGTAAGATATCATATGCATGATTTAAATATATCAGGATTTATGATTGGTAGATTATGTGAAGGAATTAGTGCATTTTCAACTGAGGATAATTTACAAATTTCAAGTTGTGGAATAACCGGGATATTTCAAGGTGAAGACGCAGTTGAAAGAGGATTTATTAAATTATGGTATAATATAGCAGGTGATGTATTTGGTGGGCAATGGCTAACAAGAAACTATGCTTATGCATCAACTTATTTACCACCATATCCTGCATCAGACATTTATAGAGCAGGATGGAATGATTCTAGTTTCACTGAAAAATATCACTATTATGGTGATACAAGTCTTAATTTCACGCATACTGCATATTCTTCACTGGATAATTTTTTTAATACATATTTTTTTAAAACTGCTAATTCCATAACAACCGCAAATGGTGGTAGATTATCAAATAATAAACAAACTGGTGTATGGCCGTTGGGTGAATATAAAGGAATAACAGGTCGTGCCAAAACTGTATATTCAAGATATGGTCGTGAAATATTAAATTGTAATATTTTAGAAGCCAAAATAATGTGGTCTCCGAGAACTCCATTTTATCATACATCACAATCAGGTTCATGGGTAGGTAATAGTAAAATAGGAAATGTAATTTTAGAAAGAGTTGGTATAATCAATTATGCTGCCGGTAATACAACCGGTAATCGTTTTAATGTAGATAACGTAGACCCTTGGGATCCTTCACAAAATTTCTTCCCAGCAATGGTATGTAGAGGTAATATTGGTTGTATGGATGTTACTAGATCTGGACATGTTCAACAATCAGTCTCAAATGAAATAAACCCAATTGTTACTGGTGGTCAAATACATAGACAATATAGAAGATCAGATGATACTAGTAGTTATTCAATGTTAACCCTTCAGGAGTTTAAAAATAGTTGGGTAAGCAAATACGTTTTCAATAGTTCATATGCATTTGTTCAACCGTTGGTATTCACTTCATCAAATGCACAATTTAAATATGATTATGGAACATTTACTCCTGTACTTCAAATTGCAGGAAGTTATATAACTCTAACGGAAGCAACTGGTATATATCACAGATTCGGTGATATAATCAGAATACATATAAGATTGAGAAATAGTAATTTGACTATTAATACGGCTGGACCATTTAGAATATCTGGTTTACCATTTATTTCAAGCTCAATTCAAACTGGATATACAAAAGGTAGTGTGTTTACTCCACAGGCAACTGGTGTGACATTAATACCATTAGTTACTCCAAGTACTGATGTATTAACAATTTTAAAAGATAGTGCAGGAACCTCATTTTCACATCCAGCAGGAACTTTTGATTTTTCTTTCCACGCTGATTTTGATTATGTAATATCATTCAATAGCTAA
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 |
DepoCatalog
BAW85692
|
depolymerase_activity RBP | S1-2 (tail spike protein) | PMID 10.1101/2025.09.09.675204 |
| Validated by sequence identity |
UniProt
A0A0A8JA02
|
ECO:0000269:FUNCTION:28077636 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 KN4-type polysaccharides of Klebsiella pneumoniae capsule (PubMed:28077636) | PMID 28077636 |
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 |
|---|---|---|---|---|
| Klebsiella Phage PhiK64-1 Encodes Multiple Depolymerases for Multiple Host Capsular Types | Pan,Y.J., Lin,T.L., Chen,C.C., Tsai,Y.T., Cheng,Y.H., Chen,Y.Y., Hsieh,P.F., Lin,Y.T. and Wang,J.T. | 2017 | 28077636 | GenBank |