Compact archived record and sequence evidence for P41067
Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids.
-
The F-type outer-membrane core complex is built from an outer ring of TraK and TraV C-terminal domains and a central cone made entirely of TraB beta-barrels, establishing TraB as a structural subunit of the complex.
"The OMCCF consists of a 13-fold symmetrical outer ring complex (ORC) built from 26 copies of TraK and TraV C-terminal domains, and a 17-fold symmetrical central cone (CC) composed of 17 copies of TraB β-barrels."
-
TraB's domains are functionally load-bearing for the secretion system, not incidental to it.
"define the importance of TraK, TraV and TraB domains to T4SSF function"
Analysis of the sequence and gene products of the transfer region of the F sex factor.
-
The F transfer region is the reference conjugation system, and its genes cover pilus synthesis, mating-pair stabilization, surface exclusion, DNA nicking and transfer, and regulation. TraB belongs to the pilus-synthesis group.
"These are involved in the synthesis of pili, extracellular filaments which establish contact between donor and recipient cells; mating-pair stabilization; prevention of mating between similar donor cells in a process termed surface exclusions; DNA nicking and transfer during conjugation; and the regulation of expression of these functions."
Biochemical dissection of the ATPase TraB, the VirB4 homologue of the Escherichia coli pKM101 conjugation machinery.
-
The protein characterized in this paper is the VirB4 homologue of the pKM101 conjugation system, not the F-plasmid TraB that carries accession P41067.
"a VirB4 homologue from the pKM101 conjugation"
-
Even for the pKM101 protein, ATP hydrolysis depended on how the protein was prepared: the membrane-derived form did not hydrolyse ATP and only the soluble hexamer did.
"TraB can form hexamers capable of hydrolyzing ATP."
OpenScientist hypothesis report for traB ATP hydrolysis activity