Structural highlights
Function
PILA4_THET2 Plays an essential role in the assembly of two types of T4P pili: a wide and a narrow that participate in natural transformation and twitching motility (PubMed:32376942). Major component of the wide pilus that is essential for natural transformation working as a DNA translocator structure that spans the inner and outer membranes (PubMed:12839734, PubMed:16857013, PubMed:19396940, PubMed:32376942). In addition, participates in the assembly of the narrow pilus composed of the PilA5 subunit that is required for twitching motility (PubMed:32376942).[1] [2] [3] [4]
References
- ↑ Friedrich A, Rumszauer J, Henne A, Averhoff B. Pilin-like proteins in the extremely thermophilic bacterium Thermus thermophilus HB27: implication in competence for natural transformation and links to type IV pilus biogenesis. Appl Environ Microbiol. 2003 Jul;69(7):3695-700. PMID:12839734 doi:10.1128/AEM.69.7.3695-3700.2003
- ↑ Rumszauer J, Schwarzenlander C, Averhoff B. Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27. FEBS J. 2006 Jul;273(14):3261-72. PMID:16857013 doi:10.1111/j.1742-4658.2006.05335.x
- ↑ Schwarzenlander C, Haase W, Averhoff B. The role of single subunits of the DNA transport machinery of Thermus thermophilus HB27 in DNA binding and transport. Environ Microbiol. 2009 Apr;11(4):801-8. PMID:19396940 doi:10.1111/j.1462-2920.2008.01801.x
- ↑ Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM. Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium. Nat Commun. 2020 May 6;11(1):2231. doi: 10.1038/s41467-020-15650-w. PMID:32376942 doi:http://dx.doi.org/10.1038/s41467-020-15650-w