- Genbank accession
- BAW85696.1 [GenBank]
- Protein name
- S2-2 (tail fiber protein)
- RBP type
-
TSPTSPTFTFTSPTSP
- Seq2Symm
-
C3 confidence 1,000
Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).C3 1,000 C1 0,020 C2 0,000 - Protein sequence
-
MGNFIQPKGSTSTEIAREILSKTYSINYSEIDFIKQNLSVNGLKLLIDPNTQYIWGTISSLETGTISSWSIDSTGEIMTVLTTNGTLTLRKISVSTSTTTANSIYNFMTSDDIYNIKNVVGIEINVDYALQKAINSGLMSIYYPPSKGIYVHSNVCTLPSGFNMYGQSRKPYTVSNDASFNNCGTVIRLASGSPGIFVLSGRHTFDNIVFDGRNNTVGSMNATSQVSGCRFEKCGFYRWGIGLGRTSGYVATVYARGCNFSGNNTAMQDWIDSRAVDCTINAQVSRGIAMRTGANNNAWVGCRVEWNGTDGFYFYQSVGNVITGELIDRNGYAGITVADGASVSVTTCSIQRNGRISSNTNNGANILINDSGIILLNGNRFTSGVDDGGTGVLTPDYDIICAGGTGKILIASGNSFSGGNLGYMKEVTIANKVITGNYGLPDIVNTGTYQKSSGLVKMGNTSTGTLPPAASNGTLTLSLSRPAMTQYMIPQKIVLEISARDTIGGRAEYFTVPLLCSWESTVPVINMISSKLDTYPDNVWGPSTNTPTGVQVSVSTTSDGSTITINLVSMDTRNRQIQAYIRGA
- Physico‐chemical
properties -
protein length: 584 AA molecular weight: 62475,47190 Da isoelectric point: 7,92789 aromaticity: 0,08390 hydropathy: -0,09229
Domains
Domain architecture
BAW85696.1
1
584 aa
ATT 2–100 · STR 127–475 ·
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
BAW85696.1
1
584 aa
| Domain | Start | End | Length (AA) | Confidence |
|---|---|---|---|---|
| N-terminal | 1 | 126 | 126 | 0,9616 |
| Central domain | 127 | 451 | 326 | 0,9907 |
| C-terminal | 452 | 584 | 132 | 0,9698 |
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
BAW85696.1
[NCBI]
Genbank nucleotide accession
LC121102.1
[NCBI]
CDS location
range 1 -> 1755
strand +
strand +
CDS
ATGGGAAATTTTATACAACCTAAAGGTTCAACTTCTACTGAAATCGCTAGAGAAATTTTATCTAAAACTTATTCAATAAATTATTCTGAAATAGATTTTATAAAACAAAATCTTTCAGTTAATGGTTTAAAACTTCTTATTGATCCAAATACTCAATATATATGGGGAACTATTTCAAGTTTAGAAACTGGAACAATTTCATCATGGAGTATAGATAGTACTGGCGAAATTATGACTGTATTAACTACTAATGGCACTTTAACATTAAGAAAAATTTCTGTTTCTACTTCAACAACAACCGCAAATTCTATATATAATTTTATGACATCTGATGATATTTACAACATAAAAAATGTAGTTGGGATTGAAATTAATGTTGATTATGCTTTACAAAAAGCAATAAATTCTGGATTAATGTCAATTTATTATCCACCATCTAAAGGTATATATGTACATAGTAATGTATGTACATTACCATCAGGATTCAATATGTATGGTCAAAGTAGAAAACCATACACTGTTTCGAATGATGCATCATTTAATAATTGCGGTACTGTTATTAGATTAGCATCTGGTTCGCCTGGTATTTTTGTTCTTTCAGGGAGACATACTTTCGACAATATTGTATTTGATGGTAGAAACAACACAGTGGGTTCTATGAATGCTACATCACAAGTTTCTGGGTGTAGATTCGAAAAATGTGGATTTTATAGATGGGGTATTGGTTTAGGAAGAACTAGTGGGTATGTAGCAACCGTTTATGCTCGTGGTTGTAATTTTAGTGGTAATAATACAGCAATGCAAGACTGGATTGACTCTCGTGCAGTCGATTGTACAATAAATGCACAAGTCTCTCGTGGCATTGCGATGCGAACAGGAGCTAATAATAATGCATGGGTTGGGTGCCGAGTAGAATGGAATGGAACCGATGGTTTTTATTTTTATCAATCAGTAGGTAATGTAATTACTGGGGAATTGATTGACCGTAACGGATATGCAGGAATTACTGTTGCCGATGGTGCAAGTGTATCAGTTACAACCTGCTCAATACAACGAAACGGAAGAATATCCTCTAATACAAATAATGGGGCTAATATATTAATTAATGATTCTGGGATAATTTTATTAAATGGTAATAGATTTACTTCTGGTGTAGATGACGGTGGTACTGGTGTATTAACACCAGATTATGATATTATATGTGCTGGTGGTACTGGAAAAATCCTTATTGCTTCAGGAAATTCGTTTTCGGGTGGAAACTTAGGCTATATGAAAGAAGTAACTATAGCTAATAAAGTAATAACCGGAAACTATGGTTTACCTGATATAGTTAATACAGGGACATATCAAAAATCATCTGGTTTGGTTAAAATGGGGAATACATCTACTGGAACATTACCGCCAGCAGCATCAAATGGAACATTAACATTATCATTAAGCAGACCAGCAATGACACAATATATGATTCCACAAAAAATAGTTCTTGAGATATCAGCAAGAGATACTATAGGTGGAAGAGCTGAATATTTTACAGTACCTCTATTGTGTTCATGGGAAAGCACCGTACCCGTAATTAATATGATATCATCGAAATTAGATACATATCCAGACAATGTATGGGGTCCAAGTACAAATACACCTACTGGGGTTCAAGTATCTGTTAGTACAACATCTGATGGTTCTACTATTACTATCAACTTAGTATCTATGGATACAAGAAATAGACAAATACAAGCTTATATTAGAGGTGCATAA
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 |
GO
GO:0098996
|
GO:IDA RBP | symbiont entry into host cell via disruption of host cell glycocalyx | ECO:0000314 |
| Validated by sequence identity |
UniProt
A0A0A8J9V7
|
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 K25-type polysaccharides of Klebsiella pneumoniae capsule (PubMed:28077636) | PMID 28077636 |
| 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 |