STEPdb: Sub-cellular Topologies of E.coli Polypeptides.

Table: Homologous proteins of type three secretion system (T3SS) within pathogens and the flagellum  Export to Excel  

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Homologous proteins of type three secretion system (T3SS) within pathogens and the flagellum


Structural sub assembly of injectisome
Subunit function/role
Common name
EPEC
Accession (Uniprot)
P. aeruginosa T3SS
Yersinia T3SS
Shigella flexneri
Salmonella sp. SPI 1
Salmonella enterica SPI 2
Chlamydia pneumoniae
Bordetella
P. syringae
R. solanacearum
Xanthomonas spp.
B. pseudomallei T3SS3
Flagellum
Translocators
Translocon pore protein
SctE1
EspD
B7UM93
PopB15
YopB
IpaB
SipB
SseC
CopB1/26, 7
BopB12
HrpK14
PopF1/PopF2
HrpK14
BipB13
 
Translocators
Translocon pore protein
SctB1
EspB
Q05129
PopD15
YopD
IpaC
SipC
SseD
CopD1/27
BopD12
 
XopA14
XopA14
BipC13
 
Translocators
Tip/filament protein
SctA1
EspA
B7UM94
PcrV15
LcrV
IpaD
SipD
SseD
CT584 or LcrV6, 7
Bsp228
 
 
 
BipD13
FliC3
Needle
Needle component
SctF1
EscF
B7UM90
PscF15
YscF
MxiH
PrgI
SsaG
CdsF6, 7
BscF11
HrpA
HrpY
HrpE14
BsaL13
 
OM ring
Secretin
SctC1
EscC
B7UMB3
PscC15
YscC
MxiD
InvG
SsaC
CdsC6, 7
BscC11
HrcC14
HrcC14
HrcC14
BsaO13
FlgI/FlgH * 2
 
Pilotin
 
 
 
ExsB15
VirG
MxiM
InvH
 
 
BscW11
 
 
 
 
 
OM-IM connector
Inner rod
SctI1
EscI
B7UMB0
PscI15
YscI
MxiI
PrgJ
SsaI
 
BscI11
HrpB
HrpJ
HrpB214
BsaK13
FlgB/FlgC/FlgF/FlgG4
Accessory enzyme
Muramidase
 
EtgA
B7UMB7
 
YsaH13
IpgF13
IagB13
IagB13
 
 
HrpH
 
 
BapC13
 
IM ring
Lipoprotein ring component
SctJ1
EscJ
B7UMB1
PscJ15
YscJ
MxiJ
PrgK
SsaJ
CdsJ7
BscJ11
HrcJ14
HrcJ14
HrcJ14
BsaJ13
FliF2
IM ring
Major IM ring component
SctD1
EscD
B7UM96
PscD15
YscD
MxiG
PrgH
SsaD
CdsD6, 7
BscD11
HrpQ
HrcD14 HrpW
HrcD14
BsaM13
FliG5
Export apparatus or Translocase
Translocase channel
SctR1
EscR
B7UMC1
PscR15
YscR
Spa24
InvL/SpaP
SsaR
CdsR7
BscR11
HrcR14
HrcR14
HrcR14
BsaW13
FliP2
Export apparatus or Translocase
Translocase channel
SctS1
EscS
B7UMC0
PscS15
YscS
Spa9
SpaQ
SsaS
CdsS7
BscS11
HrcS14
HrcS14
HrcS14
BsaX13
FliQ2
Export apparatus or Translocase
Translocase channel
SctT1
EscT
B7UMB9
PscT15
YscT
Spa29
InvN/SpaR
SsaT
CdsT7
BscT11
HrcT14
HrcT14
HrcT14
BsaY13
FliR2
Export apparatus or Translocase
Minor component, external to channel
SctU1
EscU
B7UMB8
PscU15
YscU
Spa40
SpaS
SsaU
CdsU7
BscU11
HrcU14
HrcU14
HrcU14
BsaZ13
FlhB2
Export apparatus or Translocase
Major component, external to channel
SctV1
EscV
B7UMA7
PcrD15
YscV (LcrD)
MxiA
InvA
SsaV
CdsV7
BscV11
HrcV
HrcV
HcrV14
BsaQ13
FlhA2
ATPase complex
External stator** connecting ATPase and Cytoplasmic ring
SctL1
EscL
B7UMC2
PscL15
YscL
MxiN
OrgB13
SsaK
CdsL6, 7
BscL11
HrcE
HrpF
HrcL14
OrgB13
FliH2
ATPase complex
Hexameric ring-structure ATPase
SctN1
EscN
B7UMA6
PscN15
YscN
Spa47
InvC/SpaL
SsaN
CdsN6, 7
BscN11
HrcN14
HrcN14
HrcN14
BsaS13
FliI2
ATPase complex
Central stalk**, inserting in ATPase ring
SctO1
EscO
B7UMA5
PscO15
YscO
Spa13
InvI
SsaO
CdsO6, 7
 
HrpO
HrpD
HrpB714
HrpD or BsaU13
FliJ5
Cytoplasmic ring
Component of 6 Pod assembly
SctQ1
SepQ
B7UMA3
PscQ15
YscQ
Spa33
SpaO
SsaQ
CdsQ6, 7
BscQ11
HrcQA+B14
HrcQ
HrcQA+B 14
BsaV13
FliN/FliM2
Cytoplasmic ring
Connector of Pods with SctD
SctK1
EscK
B7UMC3
PscK15
YscK
MxiK
OrgA13
 
 
 
HrpD
 
 
OrgA13
 
Gatekeeper
Gatekeeper/Affinity switch
SctW1
SepL
B7UM95
PopN15
YopN +TyeA
MxiC
InvE
SsaL
CopN6, 7
BopN12
HrpJ
HpaA14
HpaA14
BsaP13
 
Gatekeeper
Subunit 1 of SctW chaperone heterodimer
 
SepD
B7UMB2
 
 
 
 
SpiC16
 
 
 
 
 
 
 
Gatekeeper
Subunit 2 of SctW chaperone heterodimer
 
CesL
B7UMA8
 
 
 
 
 
 
 
 
 
 
 
 
Assembly regulators
Molecular ruler regulating needle/filament length
SctP1
EscP
B7UMA4
PscP15
YscP
Spa32
InvJ
SsaP
CdsP7
BscK11
HrpP
HpaP
HpaC14
BsaU13
FliK2
Chaperones
For early substrates (needle component)
 
EscG
B7UM89
PscG15
YscG15
 
 
 
 
 
 
 
 
 
 
Chaperones
For early substrates
 
EscE
B7UMC5
PscE15
YscE15
 
 
 
 
 
 
 
 
 
 
Chaperones
For middle substrates (filament component)
 
CesAB
B7UMC4
 
 
 
 
 
 
Btc229
 
 
 
 
 
Chaperones
For middle substrates (translocators)
 
CesD
B7UMB4
PcrH15
SycD15
IpgC15
SicA17
 
 
Scc2/Scc310
 
 
 
BicA13
 
Chaperones
For middle substrates (translocators)
 
CesD2
B7UM91
 
 
 
 
 
 
 
 
 
 
 
 
Chaperones
For late substrates (effectors)
 
CesF
B7UMA1
 
 
 
 
 
 
 
 
 
 
 
 
Chaperones
For late substrates (effectors)
 
CesT
P21244
 
SycE20
 
SigE18
 
 
 
 
 
 
 
 
Chaperones
For late substrates (effectors)
 
 
 
 
YsaK20
Spa1520
InvB20, 13
 
 
 
 
 
 
InvB20, 13
 
Chaperones
For flagellar substrate (FlgK)
 
 
 
 
 
 
 
 
 
 
 
 
 
 
FlgN
Chaperones
For flagellar substrate (FliC)
 
 
 
 
 
 
 
 
 
 
 
 
 
 
FliS
Chaperones
For flagellar substrate (FliD)
 
 
 
 
 
 
 
 
 
 
 
 
 
 
FliT
Transcription regulators
Global Regulator
 
Ler
B7UMC6
 
 
 
 
 
 
 
 
 
 
 
 
Records 1 to 36 of 36     
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Remarks:
* FlgI/FlgH proteins are not homologous to SctC proteins, but fulfill the same function.
** Nomenclature based on the homology of the F0F1-ATPases, γ subunit (central stalk) and b and δ subunits (external stator) as described in:
- (Nam et al., 2014)
Nam, K., Pu, J., and Karplus, M. (2014). Trapping the ATP binding state leads to a detailed understanding of the F1-ATPase mechanism. Proc Natl Acad Sci U S A 111, 17851-17856. PMID: 25453082
- (Pallen et al., 2006)
Pallen, M.J., Bailey, C.M., and Beatson, S.A. (2006). Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoF1 and vacuolar ATPases. Protein Sci 15, 935-941. PMID: 16522800





References for the homologues table:


1 (Diepold and Wagner, 2014)
Diepold, A., and Wagner, S. (2014). Assembly of the bacterial type III secretion machinery. FEMS Microbiol Rev 38, 802-822. PMID: 24484471
2 (Cornelis, 2006)
Cornelis, G.R. (2006). The type III secretion injectisome. Nat Rev Microbiol 4, 811-825. PMID: 17041629
3 (Ince et al., 2015)
CInce D, Sutterwala FS, Yahr TL.Secretion of Flagellar Proteins by the Pseudomonas aeruginosa Type III Secretion-Injectisome System. Journal of Bacteriology (2015);197(12):2003-2011. doi:10.1128/JB.00030-15. PMID: 25845843
4 (Buttner, 2012)
Buttner, D. (2012). Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria. Microbiol Mol Biol Rev 76, 262-310. PMID: 22688814
5 (Minamino, 2014b)
Minamino, T. (2014). Protein export through the bacterial flagellar type III export pathway. Biochim Biophys Acta 1843, 1642-1648. PMID: 24064315
6 (Betts-Hampikian and Fields, 2010)
Betts-Hampikian, H.J., and Fields, K.A. (2010). The Chlamydial Type III Secretion Mechanism: Revealing Cracks in a Tough Nut. Front Microbiol 1, 114. PMC: PMC3125583
7 (Beeckman and Vanrompay, 2010)
Beeckman, D.S., and Vanrompay, D.C. (2010). Bacterial Secretion Systems with an Emphasis on the chlamydial Type III secretion system. Curr Issues Mol Biol 12, 17-41 PMID: 19605938"
8 (Medhekar et al., 2009)
Medhekar, B., Shrivastava, R., Mattoo, S., Gingery, M., and Miller, J.F. (2009). Bordetella Bsp22 forms a filamentous type III secretion system tip complex and is immunoprotective in vitro and in vivo. Mol Microbiol 71, 492-504. PMID: 19040642
9 (Kurushima et al., 2012)
Kurushima, J., Kuwae, A., and Abe, A. (2012). Btc22 chaperone is required for secretion and stability of the type III secreted protein Bsp22 in Bordetella bronchiseptica. FEMS Microbiol Lett 331, 144-151. PMID: 22458424
10 (Fields et al., 2005)
Fields, K.A., Fischer, E.R., Mead, D.J., and Hackstadt, T. (2005). Analysis of putative Chlamydia trachomatis chaperones Scc2 and Scc3 and their use in the identification of type III secretion substrates. J Bacteriol 187, 6466- 6478. PMC: PMC1236624
11 (Park et al., 2015)
Park, J., Zhang, Y., Chen, C., Dudley, E.G., and Harvill, E.T. (2015). Diversity of secretion systems associated with virulence characteristics of the classical bordetellae. Microbiology 161, 2328-2340. PMID: PMC5410106
12 (Yuk et al., 2000)
Yuk, M.H., Harvill, E.T., Cotter, P.A., and Miller, J.F. (2000). Modulation of host immune responses, induction of apoptosis and inhibition of NF-kappaB activation by the Bordetella type III secretion system. Mol Microbiol 35, 991-1004. PMID: 10712682
13 (Sun and Gan, 2010)
Sun, G.W., and Gan, Y.H. (2010). Unraveling type III secretion systems in the highly versatile Burkholderia pseudomallei. Trends Microbiol 18, 561-568. PMID: 20951592
14 (Gazi et al., 2012)
Gazi, A.D., Sarris, P.F., Fadouloglou, V.E., Charova, S.N., Mathioudakis, N., Panopoulos, N.J., and Kokkinidis, M. (2012). Phylogenetic analysis of a gene cluster encoding an additional, rhizobial-like type III secretion system that is narrowly distributed among Pseudomonas syringae strains. BMC Microbiol 12, 188. PMID: 22937899
15 (Izore et al., 2011)
Izore, T., Job, V., and Dessen, A. (2011). Biogenesis, regulation, and targeting of the type III secretion system. Structure 19, 603-612. PMID: 21565695
16 (Younis et al., 2010)
Younis, R., Bingle, L.E., Rollauer, S., Munera, D., Busby, S.J., Johnson, S., Deane, J.E., Lea, S.M., Frankel, G., and Pallen, M.J. (2010). SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N- terminal secretion signal. J Bacteriol 192, 6093-6098. PMID: 20833800
17 (Tucker and Galan, 2000)
Tucker, S.C., and Galan, J.E. (2000). Complex function for SicA, a Salmonella enterica serovar typhimurium type III secretion-associated chaperone. J Bacteriol 182, 2262-2268. PMC: PMC111276
18 (Luo et al., 2001)
Luo, Y., Bertero, M.G., Frey, E.A., Pfuetzner, R.A., Wenk, M.R., Creagh, L., Marcus, S.L., Lim, D., Sicheri, F., Kay, C., et al. (2001). Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Nat Struct Biol 8, 1031-1036. PMID: 11685226
19 (Shaw et al., 2005)
Shaw, R.K., Smollett, K., Cleary, J., Garmendia, J., Straatman-Iwanowska, A., Frankel, G., and Knutton, S. (2005). Enteropathogenic Escherichia coli type III effectors EspG and EspG2 disrupt the microtubule network of intestinal epithelial cells. Infect Immun 73, 4385-4390. PMID: 15972534
20 (van Eerde et al., 2004)
van Eerde, A., Hamiaux, C., Perez, J., Parsot, C., and Dijkstra, B.W. (2004). Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity. EMBO reports 5, 477-483. PMC: PMC1299055
21 (Minamino, 2014a)
Minamino, T. (2014b). Protein export through the bacterial flagellar type III export pathway. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1843, 1642-1648. PMID: 24064315

 

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