Gene/

Protein

(new name)

Gene/

protein

(old/other name)

Uniprot code

Other codes

aa/MW

pI

Modifications

Secretion mechanism

Effect of deletion

mutation on

secretion

Effect on

pedestal

formation /

virulence

Known

Interactions/

method/

ref

Homologues

Domains

Known function

New functional prediction

rorf1

B7UMC9_ECO27

286/

31/993

?

+

+/+

EspD

YjiK

SdiA-regulated domain (NHLrepeats)

SdiA-regulated?

espG1

B7UMC8_ECO27

398/

43,919

5.21

T3S

+

+/+

VirA Translocated effector

Disassemble microtubules to induce RhoGTPase-mediated cytokeletal rearrangements that promote bacterial attachment, entry, or movement within the cytoplasm

Ler

Orf1

B7UMC6_ECO27

E2348_3969, O52122_ECOLI

129/

15,134

  5.91

No

No expression

  -/-

HNS, StpA                      Positive regulator

NS, StpA

Might form heterodimers with H

escE

orf2

B7UMC5_ECO27

72/

?

Orf29

Interacts with C terminus of SepL

YscE, PscE, SsaE,

CV2595,

YPO0259

T3S

Functionally important conserved residues can be identified by scrutiny of homologues

cesAB

Orf3/

L0052

B7UMC4_ECO27

E2348_3966

107/

No

±EspA, EspB

-/-

EspA, EspB

NleF   effector (B7UR63_ECO27)

Chaperone for EspA and EspB

orf4

L0051

B7UMC3_ECO27

E2348_3965

199/

No

-

-/-,

YPO0264, CV2589, STM1410

(Q8ZPP3_SALTY),

Q0WK43_YERPE

T3S

Functionally important conserved residues can be identified by scrutiny of homologues

escL

orf5/

L0050

B7UMC2_ECO27

E2348_3964

231/

No

-

-/-

EspA/Co-purification [Ku 2009]

YscL, FliH

T3S

Binds to and regulates activity of ATPase EscN

escR

B7UMC1_ECO27

217/

Sec?

-

-/-

EscR, EscS, EscU, SepZ EspD

YscR, FliP

PF00813

T3S

escS

B7UMC0_ECO27

89/

Sec?

-

-/- EscR,

EspD

YscS, FliQ

PF01313

T3S

escT

B7UMB9_ECO27

258/

Sec?

-

-/-

YscT, FliR

PF01311

T3S

Physically associated in the basal body with EscU in a 1:1 ratio; C-terminus is cytoplasmic [158]

escU

B7UMB8_ECO27

345/

Sec?

-

-/-

EscR, EscI, EspD

YscU, FlhB

PF00771

T3S

Physically associated in the basal body with EscT in a 1:1 ratio [158]; cleaved at NPTH motif [159];regulates substrate specificity of secretion system[160].

etgA

rorf3

B7UMB7_ECO27

152/ 17,104

Sec

±

±/±

EscI

lytic   transglycosylase IagB, IpgF

Lytic transglycosylase needed to open gap in peptidoglycan for assembly of secretion system [58]; potential drug target

grIR

Global regulator of LEE repressor

B7UMB6_ECO27

123/

13,944

No

+

+/++

GrlR/GrlA

Bongori regulator

Negative regulator

Will work in concert with GrlA

grIA  

Global regulator of LEE activator

B7UM_ECO27

137/ 16,052

No

No expression

-/-

GrlR

Bongori regulator, CaiF

Positive regulator

Will work in concert with GrlR

cesD

B7UM_ECO27

151/ 17,503

No

-/EspD

±/-

Other TPR chaperones

Chaperone for EspD TPR chaperone [115]

escC

Secretin

B7UMB3_ECO27

512/

56.27

8.61

Sec?

- -/-

EscD YscC, MxiD, InvG

T3S

Interacts with peptidoglycan [161], Dsbdependent domain missing

sepD

B7UMB2_ECO27

151/

No

-/Translocators

-/-

SepL

None

Switches translocator/effector secretion

Works in concert with SepL

escJ

Assembly platform

B7UMB1_ECO27

190/

Palmitoylated at C19(by analogy to PrgK Yip 2005 -Fig. S2)

Sec-Lipoprotein

-

-/-

YscJ,PrgK, FliF

PF01514

T3S

EscD and EscJ form ring-like structure in inner membrane [66, 162, 163]

escI

Rorf8-rod

B7UMB0_ECO27

142

T3S?

-

-/-

EscU, rORF3

PrgJ, MxiI, YscI

T3S

Forms inner rod within base of needle complex[65, 68-70].

sepZ

espZ

B7UMA9_ECO27

98/

9.39

4.73

T3S

+

+/±

EscR

None

Translocated effector

Mpc

Orf12

- multiple point controller

B7UMA08_ECO27

117/

No

-

-/-

Interacts with Ler-suppresses LEE expression [Tsai 2006]

SsaM

T3S

Might play a role in switching translocator/effector secretion

escN

B7UMA6_ECO27

O52140_ECOLX

446/

48.858

No

-

-/-

CesT, Tir [50]

YscN

T3S

ATPAse Forms hexameric complex

orf15

B7UMA5_ECO27

E2348 _ 3947

125/

14.66

9.94

No

-

-/-

None

T3S

orf16

B7UMA4_ECO27

E2348_ 3946

138/

16.58

9.47

No

±/Translocators

±/±

None

PF00771

Secretion of translocators

FliK/YscP analogue?

escV

B7UMA7_ECO27

675/

Sec?

-

-/-

LcrD, FlhA

T3S

C-terminal cytoplasmic domain might play a role in gene regulation [164, 165].

sepQ

escQ-C-ring like

B7UMA3_ECO27

305/

34.96

4.51

No

-

-/-

YscQ, FliN

COG1887

T3S

Forms ring within basal body [56]; interacts with EscL [54]

espH

B7UMA2_ECO27

168/

T3S

+

+/++

Translocated effector

cesF

B7UMA1_ECO27

120/

No

±/EspF?

+/+

Chaperone for EspF

map

B7UMA0_ECO27

203/

22.569

  9.08

T3S

+

+/++

CesT

Translocated effector

tir

B7UM99_ECO27

550/

56.50

4.68

@Y454 Phosphoryaltion in the host by Fyn [Phillips 2004]

@S 436 & S437 by PKA [Allen-Vercoe 2006]

@Phosphorylation affects oligomerization [Hawrani   2003]

T3S

+

-/-

CesT Tir

Translocated

effector; Phosphorylated

cesT

CEST_

ECO27

P21244

156/

No

±/Tir

-/-

Map, EspF, Tir, CesT

Many

Chaperone for Tir/Map

Possible regulatory role, by analogy with ExsC?

eae

intimin

EAE_ ECO27

939/

102.40

9.00

Self/

Auto

transporter?

+

-/-

Adhesin (intimin)

escD

B7UM96_ECO27

406/

45.27

6.62

?

-

-/-

YscD, PrgH

YscD: cytoplasmic FHA and BON domains

T3S

EscD and EscJ form ring-like structure in inner membrane [66, 162, 163]; BON domains mediate binding to phospholipids; FHA domain mediates protein-protein interactions and signalling

sepL

B7UM95_ECO27

351/

39.98

4.51

No

-/Translocators

-/-

SepD

YopN, TyeA

Switches translocator/effector secretion

single protein mediating effects of YopN and TyeA; internal interaction between YopN- and TyeA-like moieties; also a translocated effector?

espA

B7UM94_ECO27

O33976_ECOLX

206/

20.534

4.17

T3S

+

-/-

CesAB

Flagellin (B7USU2_ECO27)

Translocator

Half-flagellin model (see text); dimerizes before polymerizes; lacks D0 and D3 domains

espD

B7UM93_ECO27

O88127_ECOLI

/39.47

4.88

T3S

+

-/-

EspD, EscRSU,CesD, rORF1, SepZ

YopB etc

Translocator

espB

EaeB

EAEB_ECO27

P71213_ECOLX

314/

33.14

4.97

T3S

+

-/-

CesAB

YopD etc

Translocator- Binds to myosins that interact with actin filaments and mediate essential processes (e.g.microvillus formation ,phagocytosis). Inhibits the interaction of myosins with actin [Iizumi 2007]

cesD2

B7UM91_ECO27

135

No

±/EspD?

+/±

LcrR

Chaperone for EspD

LcrR will bind YopB

escF

Needle

B7UM90_ECO27

73/8.13

4.03

T3S

-

-/-

YscF

Major needle component

orf29

CesA2

/L0017

B7UM89_ECO27

O85623_ECOLX

92/

10.31

5.81

No

-

-/-

EscE(Orf2), EspA

YPO0261, SsaH, CV2586

DUF1039

T3S?. EspA chaperone? [Su 2008]

Functionally important conserved residues can be identified by scrutiny of homologues, Needle component like SsaH? Is that why it binds EspA?

espF

B7UM88_ECO27

206/ 20,978

T3S

+

+/+

Translocated effector

Effector name

Other name

Uniprot code

aa/MW

pI

Modifications

Secretion

Mechanism

Pathogenicity

island

Biochemical

properties

Target in Host cell

  Function in host cell

EspG2

 Orf3

B7UH72_ECO27

390/

42,730

  5.76

  IE5

EspJ

B7ULW8_ECO27

217/

24583

  9.67

  PP2

"

EspL

B7UI20_ECO27

549/

62,188

  6.33

  IE6

"

NleA

/EspI

B7UR60_ECO27

440/

47,478

  5.27

  PP6

"/targets Golgi aparratus/Binds PDZ domain-containing proteins

Lee etal., 2008

NleB1

B7UNX3_ECO27

326/

38,056

  5.96

  IE6

"

NleB2

B7UI21_ECO27

329/ 37,627

  5.52

  PP4

NleC

B7UNX4_ECO27

330/

37,226

  4.67

  PP4

"

NleD

B7UNX6_ECO27

232/

25,951

  5.78

 PP4

"

224/

26,057

NleE2

B7UP11_ECO27

168/

19,723

  5.62

  IE2

"

NleF

B7UR63_ECO27

189/

21,388

  4.94

  PP6

"

NleG/

NleI

B7UNX2_ECO27

192/

20,331

  5.34

  PP4

"

NleH1

B7ULW4_ECO27

293/

32,482

  5.34

PP2 

"

NleH2

B7UR62_ECO27

303/

33,683

  5.54

  PP6

Name

Other name

Uniprot code

aa/

MW

pI

Modifications

Secretion

Mechanism

Pathogenicity

island

Biochemical

properties

    Function in host cell

  Refs

EspC

Autotransporter/

Serine protease

548/

56,301

468/

48,496

Efa1/

LifA

Lympho

statin

Multi-domain protein:

Glucosyl transferase/

YopT-like protease/

adhesin?

 Klapproth,2000

Babbin 2009

Efa1/

LifA-

like

Lympho

statin

Glucosy ltransferase/

YopT-like protease/

adhesin?

 Klapproth,2000

Babbin 2009

Stevens 2004