9.A.47 The Tight Adherence (Pilus) Biogenesis Apparatus (TABA) Family

Prokaryotic secretion relies on proteins that are widely conserved, including NTPases and secretins, and on proteins that are system specific. The Tad secretion system in Aggregatibacter actinomycetemcomitans is dedicated to the assembly and export of Flp pili, which are needed for tight adherence. Consistent with predictions that RcpA forms the multimeric outer membrane secretion channel (secretin; TC# 1.B.22) of the Flp pilus biogenesis apparatus, Clock et al. (2007) observed that the RcpA multimers are stable in the presence of detergent and found that RcpA and its closely related homologs form a novel and distinct subfamily within the secretin superfamily. RcpA-encoding genes were linked to Aggregatibacter rcpB and rcpC. All 5 proteins were envelope-associated, and TadC localized exclusively to the inner membrane. The RcpA secretin was necessary for wild-type abundances of RcpB and RcpC, and TadC was required for normal levels of all three Rcp proteins. TadC abundance defects were observed in rcpA and rcpC mutants. TadD production was essential for wild-type RcpA and RcpB abundances, and RcpA did not multimerize or localize to the outer membrane without the expression of TadD. Thus, membrane proteins TadC and TadD may influence the assembly, transport, and/or function of individual outer membrane Rcp proteins (Clock et al., 2007). Rose et al. (2008) observed a striking correlation between the natural order of subunits in P-pili and their ability to undergo donor-strand exchange in vitro.



This family belongs to the .

 

References:

Bernardo, S.M. and S.A. Lee. (2010). Candida albicans SUR7 contributes to secretion, biofilm formation, and macrophage killing. BMC Microbiol 10: 133.

Bottacini, F., D. van Sinderen, and M. Ventura. (2017). Omics of bifidobacteria: research and insights into their health-promoting activities. Biochem. J. 474: 4137-4152.

Clock, S.A., P.J. Planet, B.A. Perez, and D.H. Figurski. (2008). Outer membrane components of the Tad (tight adherence) secreton of Aggregatibacter actinomycetemcomitans. J. Bacteriol. 190: 980-990.

Rose, R.J., D. Verger, T. Daviter, H. Remaut, E. Paci, G. Waksman, A.E. Ashcroft, and S.E. Radford. (2008). Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry. Proc. Natl. Acad. Sci. USA 105: 12873-12878.

Young, M.E., T.S. Karpova, B. Br├╝gger, D.M. Moschenross, G.K. Wang, R. Schneiter, F.T. Wieland, and J.A. Cooper. (2002). The Sur7p family defines novel cortical domains in Saccharomyces cerevisiae, affects sphingolipid metabolism, and is involved in sporulation. Mol. Cell Biol. 22: 927-934.

Examples:

TC#NameOrganismal TypeExample
9.A.47.1.1

The tight adherence (pilus) biogenesis apparatus, TadCD-RcpABC.  RcpA is a secretin (TC# 1.B.22) (Clock et al. 2008).

Bacteria

Flp pilus biogenesis apparatus, TadCD-RcpABC of Aggregatibacter actinomycetemcomitans:
TadC (OM) (288aas) (Q9S4A8)
TadD (lipoprotein) (253aas) (Q9S4A7)
RcpA (secretin) (460aas) (Q8GD00)
RcpB (secretion apparatus) (167aas) (Q9X6J2)
RcpC (secretion apparatus) (274aas) (Q8GD01)

 
Examples:

TC#NameOrganismal TypeExample
9.A.47.2.1

The TadABC putative protein secretion system.
TadA: 469 aas, 0 TMSs
TadB: 297aas, 5 TMSs
TadC: 306 aas, 4-6 TMSs

Planctomycetes

TadABC of Rhodopirellula baltica
TadA (Q7UHP7)
TadB (Q7UHP6)
TadC (Q7UHP5)

 
9.A.47.2.2

TadABC complex; the Flp pilus assembly complex, consisting of one ATPase component, TadA or CpaF, and two membrane components, TadB (218 aas and 3 - 5 TMSs) and TadC (200 aas and 2 N- and C-terminal TMSs) (Bottacini et al. 2017).

TadABC of Bifidobacterium longum

 
Examples:

TC#NameOrganismal TypeExample