| Claim/annotation element | Evidence summary | Key quantitative data | Primary source (authors, year) | DOI URL | Citation id |
|---|---|---|---|---|---|
| Identity / correct target | UniProt P10929 matches bacteriophage T4 gene product 11 (gp11), a structural baseplate wedge protein that forms the interface between the baseplate and short tail fibers; literature explicitly refers to gp11 of bacteriophage T4 rather than an unrelated “gene 11”. | Gene product 11; 218–219 aa polypeptide | Leiman et al., 2000 | https://doi.org/10.1006/jmbi.2000.3989 | (pqac-00000002, pqac-00000005) |
| Localization | gp11 localizes to the T4 baseplate wedge/pin region, at the bottom angles/corners of the baseplate, where it serves as the short-tail-fiber connecting protein. | 18 copies per virion; wedge-pin / baseplate localization | Mesyanzhinov et al., 2004 | https://doi.org/10.1007/pl00021751 | (pqac-00000004, pqac-00000011) |
| Oligomeric state | Purified gp11 is trimeric in solution and in the virion is organized as 3 subunits per wedge; crystal structure confirms a trimeric assembly. | Trimer; sedimentation 4.2S; ~78 × 78 × 72 Å overall size | Leiman et al., 2000; Arisaka, 2012 | https://doi.org/10.1006/jmbi.2000.3989 ; https://doi.org/10.5772/35125 | (pqac-00000016, pqac-00000018) |
| Copy number / stoichiometry | Baseplate has six wedges, each containing a gp11 trimer; thus gp11 occurs as 18 copies per virion/tail. | 18 copies total = 6 wedges × 3 gp11 | Arisaka et al., 2016 | https://doi.org/10.1007/s12551-016-0230-x | (pqac-00000012, pqac-00000013) |
| Interaction partners | gp11 interacts with gp10 during wedge initiation/assembly and associates with gp12 short tail fibers; the dome-shaped baseplate is stabilized by binding of (gp9)3 and (gp11)3(gp12)3. | gp10-gp11 wedge-initiation complex; (gp11)3(gp12)3 module | Vishnevskiy et al., 2005; Arisaka et al., 2016 | https://doi.org/10.1007/s10541-005-0232-y ; https://doi.org/10.1007/s12551-016-0230-x | (pqac-00000003, pqac-00000013) |
| Role in adsorption | gp11 connects short tail fibers to the baseplate and is required for efficient irreversible adsorption/host attachment; gp11-deficient particles have poor adsorption and low infectivity, and recombinant gp11 can restore infectivity to deficient particles. | Functional complementation reported; loss of gp11 impairs adsorption/infectivity | Kurochkina et al., 2001; Leiman et al., 2000 | https://doi.org/10.1023/a:1002831212462 ; https://doi.org/10.1006/jmbi.2000.3989 | (pqac-00000006, pqac-00000002) |
| Role in infection trigger / signaling | gp11 helps transmit the receptor-recognition signal from long tail fibers/baseplate to short tail fibers during the baseplate hexagon-to-star transition that precedes sheath contraction and DNA injection. | Acts in trigger pathway rather than catalysis; linked to baseplate conformational change | Vishnevskiy et al., 2005; Leiman et al., 2000 | https://doi.org/10.1007/s10541-005-0232-y ; https://doi.org/10.1006/jmbi.2000.3989 | (pqac-00000003, pqac-00000008, pqac-00000009) |
| Structural domains | Each monomer comprises an N-terminal domain, middle “finger” domain, and C-terminal domain; N-terminus forms a short parallel coiled coil, while C-termini form a 3-fold β-annulus important for trimer architecture. | N-terminal domain residues ~12–64; finger ~80–188; C-terminal domain ~65–79 and 189–219 | Leiman et al., 2000 | https://doi.org/10.1006/jmbi.2000.3989 | (pqac-00000018, pqac-00000009) |
| Structural dimensions / model detail | Crystal structure resolved most of the polypeptide and showed a compact trimer with internal ordered water network in the β-annulus region. | Model residues Ser12–Ala219; at least 18 ordered waters; central constriction ~2.8 Å van der Waals radius | Leiman et al., 2000 | https://doi.org/10.1006/jmbi.2000.3989 | (pqac-00000018) |
| Broader assembly context | gp11 is one of seven proteins assembling sequentially into each T4 baseplate wedge and can bind gp10 at essentially any stage of wedge assembly, making it an early and flexible adaptor in morphogenesis. | 7 wedge proteins: gp11, gp10, gp7, gp8, gp6, gp53, gp25 | Arisaka & Kanamaru, 2013; Yap et al., 2010 | https://doi.org/10.1007/s12551-013-0114-2 ; https://doi.org/10.1002/mabi.201000042 | (pqac-00000003, pqac-00000016) |


*Table: This table summarizes core functional-annotation evidence for bacteriophage T4 gp11 (UniProt P10929), including its verified identity, localization, interactions, structural organization, and role in adsorption and infection triggering. It is useful as a compact evidence map linking specific annotation claims to primary sources and quantitative details.*