T4SS ID	812
Strain	Escherichia coli plasmid R388 (NC_028464)
Replicon	plasmid R388 [Browse all T4SS(s) in this replicon]
Accession	NC_028464
Location	1020..15650
Name	Trw
Function	Conjugation
Classification	Type IVA; Type P
Experimental investigation has been performed on this T4SS.

Information of structure: T4SS3−10 complex , TrwB with ADP and Mg2+, VirD4 bound to a Type IV secretion system, TrwBΔN70, TrwC bound with oriT ssDNA, TrwB in complex with the non-hydrolisable ATP-analogue ADPNP, The outer membrane complex , TrwBdeltaN70, TrwB

T4SS components

Component	TrwB	TrwD	TrwE	TrwF	TrwG	TrwH	TrwI	TrwJ	TrwK
Number	1	1	1	1	1	1	1	1	1
Component	TrwL	TrwM	TrwN
Number	1	1	1

The information of T4SS components from NC_028464
#	Locus tag (Gene)	Coordinates [+/-], size (bp)	Protein GI	Product	Component
1	- (korB)	1..288 [-], 288	971848294	putative transcriptional repressor
2	-	425..1018 [+], 594	971848295	hypothetical protein
3	- (trwN)	1020..1616 [+], 597	971848296	TrwN protein	TrwN
4	- (korA)	1841..2137 [+], 297	971848297	putative transcriptional repressor
5	- (trwL)	2070..2408 [+], 339	971848298	TrwL protein	TrwL
6	- (trwM)	2421..2735 [+], 315	971848299	TrwM protein	TrwM
7	- (trwK)	2738..5209 [+], 2472	971848300	TrwK protein	TrwK
8	- (trwJ)	5206..5886 [+], 681	971848301	TrwJ protein	TrwJ
9	- (eex)	5883..6113 [+], 231	971848302	entry exclusion protein
10	- (trwI)	6127..7155 [+], 1029	971848303	TrwI protein	TrwI
11	- (trwH)	7269..7412 [+], 144	971848304	TrwH protein	TrwH
12	- (trwG)	7409..8104 [+], 696	971848305	TrwG protein	TrwG
13	- (trwF)	8115..8915 [+], 801	971848306	TrwF protein	TrwF
14	- (trwE)	8915..10102 [+], 1188	971848307	TrwE protein	TrwE
15	- (trwD)	10068..11144 [+], 1077	971848308	TrwD protein	TrwD
16	- (trwC)	11227..14127 [-], 2901	971848309	TrwC protein
17	- (trwB)	14127..15650 [-], 1524	971848310	TrwB protein	TrwB
18	- (trwA)	15652..16017 [-], 366	971848311	TrwA protein
19	-	16471..16896 [+], 426	971848312	hypothetical protein
20	-	16893..17588 [+], 696	971848313	hypothetical protein
21	-	17602..17988 [+], 387	971848314	hypothetical protein
22	-	18142..18393 [-], 252	971848315	hypothetical prootein
23	-	18541..19194 [-], 654	971848316	hypothetical protein
24	-	19210..19554 [-], 345	971848317	hypothetical protein
25	-	20139..20207 [-], 69	971848318	hypothetical protein
26	-	20247..20570 [-], 324	971848319	hypothetical protein

 This T4SS contains information of accessory protein.

Genes in the 5-Kb flanking regions if available, or non-essential genes in the T4SS gene cluster if any.

Download FASTA format files

Proteins        Genes

The information on structure of this T4ss

#	Name	Image	Resource	Detail	Reference
1	T4SS3−10 complex		EMDB(2567)	T4SS3−10 complex from the E. coli R388 plasmid	(1) PubMed: 24670658
2	The outer membrane complex		PDB (3JQO )	Crystal structure of the outer membrane complex	(2) PubMed: 19946264
3	TrwB		PDB (1GL6)	Plasmid coupling protein	(3) PubMed: 11214325
4	TrwBdeltaN70		PDB (1E9R)	Bacterial conjugative coupling protein TrwBdeltaN70. Trigonal form in complex with sulphate.	(4) PubMed: 11214325
5	TrwB in complex with the non-hydrolisable ATP-analogue ADPNP		PDB (1GL7)	Plasmid coupling protein TrwB in complex with the non-hydrolisable ATP-analogue ADPNP	(5) PubMed: 11214325
6	TrwB with ADP and Mg2+		PDB (1GKI)	Plasmid coupling protein TrwB in complex with ADP and Mg2+.	(6) PubMed: 11214325
7	TrwBΔN70		PDB (1E9S )	Bacterial conjugative coupling protein TrwBdeltaN70. Unbound monoclinic form.	(7) PubMed: 11214325
8	TrwC bound with oriT ssDNA		PDB (1OMH)	Crystal structure of the transesterase domain of R388 relaxase TrwC bound with 25mer oriT single-stranded (ss)DNA	(8) PubMed: 14625590
9	VirD4 bound to a Type IV secretion system		EMDB(3585)	Structure of the VirD4 bound to a Type IV secretion system.	(9) PubMed: 28923826

(1) Low HH et al. (2014). Structure of a type IV secretion system. Nature. 508(7497):550-553. [PudMed:24670658]

(2) Chandran V; Fronzes R; Duquerroy S; Cronin N; Navaza J; Waksman G (2009). Structure of the outer membrane complex of a type IV secretion system. Nature. 462(7276):1011-5. [PudMed:19946264]

(3) Gomis-Rüth FX et al. (2001). The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase. Nature. 409(6820):637-41.. [PudMed:11214325]

(4) Gomis-Rüth FX et al. (2001). The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase. Nature. 409(6820):637-41.. [PudMed:11214325]

(5) Gomis-Rüth FX et al. (2001). The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase. Nature. 409(6820):637-41.. [PudMed:11214325]

(6) Gomis-Rüth FX et al. (2001). The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase. Nature. 409(6820):637-41.. [PudMed:11214325]

(7) Gomis-Rüth FX et al. (2001). The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase. Nature. 409(6820):637-41.. [PudMed:11214325]

(8) Guasch A et al. (2003). Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC. Nat Struct Biol. 10(12):1002-10. [PudMed:14625590]

(9) Redzej A et al. (2017). Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery. EMBO J. 36(20):3080-3095. [PudMed:28923826]

The information on requirements for T4SS substrate-channel docking

Certain T4SS substrates require secretion chaperones for translocation. These chaperones often possess physical properties (small size of 15 kDa, acidic pI, and amphipathic helices) resembling those of chaperones associated with the type III secretion systems, a family of macromolecular translocation systems ancestrally related to bacterial flagella.

#	Accessory protein(GI)	motif(s)	Substrate(s)	Function	Reference
1	TrwA (971848311)	ND (interacts with TrwB T4CP)	TrwC	TrwA is RHH DNA binding tetramer protein which stimulates T4CP ATP hydrolysis. TrwA protein enhances the effects of DNA on TrwB ATPase activity.	(1) PubMed: 17599913

Tips:
1.Substrate(s): For the conjugation systems, the listed proteins are relaxases that bind a cognate T4CP and are delivered to recipient cells. For the effector translocator systems, the listed proteins are effectors that play a role in the infection processes of the bacterial pathogen.
2.motif(s):The motifs listed are required for substrate translocation. In some cases, the protein or its C-terminal fragment (CT) is sufficient to mediate translocation to target cells, as shown by fusion to a reporter protein such as Cre recombinase or adenylate cyclase. Amino acids (aa) at positions listed relative to the C-terminal fragment (subscript) are required for translocation, as shown by mutational analysis. ND, not determined. Parentheses indicate that the interaction between a protein substrate and a cognate T4CP has been experimentally shown.
3.Accessory protein: Accessory factors required for T4SS channel docking or translocation. The proposed function in mediating substrate-T4SS channel docking is shown in parentheses.PubMed:19946141

(1) Tato I et al. (2007). The ATPase activity of the DNA transporter TrwB is modulated by protein TrwA: implications for a common assembly mechanism of DNA translocating motors. J Biol Chem. 282(35):25569-76. [PudMed:17599913]

(1) Grohmann E et al. (2018). Type IV secretion in Gram-negative and Gram-positive bacteria.. Mol Microbiol. 107(4):455-471.. [PudMed:29235173]

(2) Christie PJ (2016). The Mosaic Type IV Secretion Systems. EcoSal Plus. 7(1). [PudMed:27735785]

(3) Chandran Darbari V et al. (2015). Structural Biology of Bacterial Type IV Secretion Systems. Annu Rev Biochem. 84:603-29. [PudMed:26034891]

(4) Ilangovan A et al. (2015). Structural biology of the Gram-negative bacterial conjugation systems. Trends Microbiol. 23(5):301-10. [PudMed:25825348]

This literature contains experimental investigation