Post on 05-Jul-2020
Phaco DAPI GFP FM4-64 Overlay Model
P. li
mno
phila
f
E. c
oli
d
c
e
g
h
P. li
mno
phila
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Inte
nsity
FM4-64 GFP DAPI
P. limnophilaE. coli
Ctr 30% sucrose0
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Nuc
leoi
d si
ze [%
]
Ctr 30% sucrose0
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osol
size
[%]
Ctr 30% sucrose0
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osol
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[%]
P = 0.0001P = 0.0001
P = 0.0001
Ctr 30% sucrose0
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Nuc
leoi
d si
ze [%
] P = 0.0009
i j lk
Fields of view
Cel
ls [%
]
invaginations no invaginationsa bP.
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ila
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nsity
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01 2 3 4 5 6 7 8 9 10
SupplementaryFigure1:PlasmolyticstressincreasesthecytoplasmicinvaginationsofP.
limnophila
(a+b) Representative section of one field of view with Fm4-64 (red) stained cells. In (b) the
rationbetweenmorphotype1(noinvaginations)andmorphotype2(invaginations)isgivenfor
1838cellsamong10randomlychosenfieldsofview.Scalebar:10µm.
(c-f)Artificialinvaginationofthecytoplasmicmembranebyplasmolysis.GFP(green)expressing
E.coli(c+d)andP.limnophila(e+f)cellswereuntreated(c+e)orosmoticallystressedwith30%
sucrose(d+f).E.colicellsformcharacteristicperiplasmicbays(d,Phaco).Both,nucleoid(blue)
andcytoplasm(green)ofE.colicellsareshrunkwhilethemembranesignal(red)resemblesthe
stainingpatternofmorphotype2P.limnophilacells(eandFigure2c+d).Suchnaturaloccurring
cytoplasmicmembrane invaginationsofP. limnophilamorphotype2 cells (e andFigure2c+d)
increased by osmotic stress and became visible in phase contrast (f, Phaco). The cytoplasm
shrunk further (f, GFP) and a black dot became visible in membrane staining experiments (f,
FM4-64).Scalebars:1µm.
(g+h)OverlayofWF,Phaco,Fm4-64(red),GFP(green)andDAPI(blue)signalsofuntreated(g)
andtreated(h)P.limnophilacells.Theoverviewdemonstratesthatin(e)and(f)selectedcells
were representative. Corresponding fluorescence intensity profiles of untreated- (g) and
osmoticallystressedcells(h)revealedonecytosolicGFPmaximaoftheuntreatedcontrolwhile
aseparationofthecytosolicGFPsignalintotwodistinctintensitymaximawasobservedamong
treatedcells(h).Scalebars:5µm.
(i-l)Quantification revealeda significantdecreaseofboth, sizeof thenucleoidand sizeof the
cytosol in E. coli (i+j) and P. limnophila (k+l), if treated with 30% sucrose compared to the
respectively untreated control. (T-test: P=0.0001, P=0.0001, P=0.0009 and P=0.0001
respectively,errorbars:mintomaxof10measuredcellsamong2individualexperiments).
Gem
mat
a ob
scur
iglo
bus
Rho
dopi
rellu
la b
altic
a
Phaco DAPI FM4-64 Overlay Model Overlay Nile Red DAPI
WF SR-SIM
e
d
g
f
Pla
ncto
piru
s lim
noph
ila
h i
0 1 2 30
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4000
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Size [µm]
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nsity
a
SR-SIMWF
0 1 2 30
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Size [µm]
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nsity
DAPI GFPNile RedGFPFM4-64 DAPI
b c
Pla
ncto
piru
s lim
noph
ila
GAT
TA-S
IM 1
20b
Supplementary Figure 2: The innermost planctomycetal membrane is the cytoplasmic
membrane
(a-c) Control of super resolution structured illumination (SR-SIM) performance under
experimentalconditions. (a+b)Representative fluorescence intensity lineprofilesofFM4-64/
Nile Red (red) and DAPI (blue) stained, GFP (green) expressingP. limnophila cells imaged in
wide field- (a:WF)andSR-SIM(b).Thewidthofouter-and innermembranepeaks(red)was
442+/-68nmforWF-and225+/-44nmforSR-SIMexperiments(20randomlychosencells).
Thus,SR-SIMroughlydoubledtheresolutioncomparedtoWF.(c)Overviewofarepresentative
SR-SIMimageshowingmultipleDNAorigamis,eachwithtwoAlexaFluor488dyes in120nm
distance.Signalsofboth fluorophoresoverlap(c:magnification,whitearrowheads), indicating
thattheresolutionis>120nm.Scalebars:5µmand0.1µmrespectively.
(d-g)G. obscuriglobus (d+e) andR. baltica (f+g) cells analysed in WF and structured SR-SIM.
Phase contrast (Phaco) microscopy revealed intracellular structures. In both species, the blue
nucleoid (DAPI) is highly condensed and the red cytoplasmicmembrane (FM4-64 /NileRed)
exhibitmultiple invaginationsas illustratedinthemodel.SR-SIManalysesresolvedmembrane
invaginationsthatappearasreddotsorlinesinWFmicrographs.Scalebars:1µm.
(h+i) A representative freeze fractured, plunge-frozen P. limnophila cell (h) with enlarged
periplasm, caused by multiple invaginations of the cytoplasmic membrane (selected from 50
cells among 3 independent experiments). (i) False colours correspond to colours used in the
modelsabove(d-g).Scalebars:0.5µm.
a b c
d e f
g h i
j k l
SupplementaryFigure3:Cryo-electrontomographyofPlanctopiruslimnophilacells
(a-f)Exampleofacellwithoutinvaginationsofthecytoplasmicmembrane.Representativeslices
of a tomogram of a FIB-thinned cell (thickness of remaining cell volume 260 nm; inter-slice
distances are17, 21, 17, 21 and17nm). (g-l) Cellwith "tubular"- or "disk"-like invaginations
apparently "enclosing" part of the cytoplasm (second image from top left). Slices are from a
tomogramofaFIB-thinnedcell(thicknessofremainingcellvolume360nm;inter-slicedistances
are41,38,41,38and38nm).Scalebars:250nm.
Phaco DAPI FM4-64 OverlayDiOC6(3)R
hodo
pire
llula
bal
tica
Pla
ncto
piru
s lim
noph
ilaG
emm
ata
obsc
urig
lobu
s
b
a
d
c
f
e
P. limnophila R. baltica G. obscuriglobus
Intensity DiOC6(3)
Inte
nsity
FM
4-64
hg i0,909 +/- 0,0490,932 +/- 0,0280,922 +/- 0,0970,984 +/- 0,018
0,911 +/- 0,0340,928 +/- 0,0280,985 +/- 0,0250,970 +/- 0,021
0,811 +/- 0,0300,843 +/- 0,0250,929 +/- 0,0310,998 +/- 0,002
SupplementaryFigure4:Membranepotentialattheinnermostmembrane
(a-f)Theplanctomycetalspecies,P.limnophila(a+b),R.baltica(c+d)andG.obscuriglobus(e+f)
were stained with DAPI (DNA, blue), FM4-64 (membrane, red) and DiOC6(3) (energized
membrane, green). The overlays show a distinct red signal around the outer rim of all three
species. This indicates that the outermost membrane is not energized. The innermost
membranesappearyellowintheoverlays,whichprovidesevidencethattheyareenergizedand
correspondtothecommonbacterialcytoplasmicmembrane.Scalebars:2µm.
(g-i)IntensityblotsofFM4-64versusDiOC6(3)signalsrevealatypicallinearcorrelationwhich
is slightly blurry for G. obscuriglobus cells (i). Calculation of Pearsons’s correlation (white),
Mander’soverlap(green)andco-localisationcoefficientsc1(blue)andc2(red)furthersupport
co-localisation of FM4-64 and DiOC6(3) signals among all analysed species. For (g+h) 50
individualcellswerecompared.For(i)10fieldsofviewwereused,duetoaggregateformation
ofG.obscuriglobus.
WF
Immunogold overview
Outer rim 0.4 µm
Inner partOuter rim Inner part
0
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nsity
/ A
rea
[%]
Immunogold
Bgr OM IM Unspc.0
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ion
/ 3.5
µm
2 [%
]
a b
Outer membrane Inner membrane Background Unspecific in cell
****
********
c
d
SupplementaryFigure5:QuantitativeATPaselocalisationanalysisinG.obscuriglobus
(a+b)Thewidefieldimmunofluorescencequantificationwasachievedbydividingcellsintotwo
parts(a).Theouterrimcomprisedadiameterof0.4µmandthuscoverstheentirerangewhere
signals associated with the outer membrane (OM) could be expected. In contrast, only
invaginationsofthecytoplasmicmembrane(CM)cancauseATPasesignalsfromtheinnerpart
ofthecell.(b)Comparisonoftheintensityperareabetweentheinnerandouterpartof50cells
in5fieldsofview.39.21%ofthesignalsrelatetotheouterrimand60.79%tothecellcentre.T-
test:P=0.0001,errorbarsindicate95%confidenceinterval.Scalebar:0.5µm.
(c) Analysis of immunogold ATPase labelling of 10 micrographs from three independent
experiments.Mean-valuesareshownanderrorbarscorrespondtothe95%confidenceinterval.
T-testsrevealedsignificantdifferencesbetweenlocalizationattheinnermembranecomparedto
background(p=0.0001),totheoutermembrane(p=0.0001)andtounspecificsignalsinsidethe
cells(p=0.0001).
(d)Representativemicrographof immunogold labelledATPase localization inG.obscuriglobus
cells.Goldparticles(blackdots)areassignedtofourdifferentlocalizationsasshowninFig.4c.
Diameter of coloured circles indicatesuncertainty of localizationdue to the size of antibodies
andgoldparticle(22.5nm∅).Scalebar:0.5µm.
Type I Type IIType III Type Va Type Vb Type Vc Type IV Type VI
TolC
HlyD
HlyB
YscW
YscFYscOPX
YscJ
YscVURTS
YscQL YscNGspE GspO
GspFLM
GspGHIJK
GspC
GspS
GspDYscC
TatABCESecDEFGY
YajCYidC
SecAFtsY
VirB4 VirD4
VirB11
VirB6VirB8VirB10
VirB1
VirB3VirB5
VirB7VirB9
VirB2Hcp
VgrG
Lip
IcmFDotU
PpkAClpV
Fha1
PppASecB ffh
YscF
YscO YscP YscX
YscC
YscJ YscR YscS
YscT YscU YscV
YscQ YscL
Type III
YscW
YscN
HlyB
Type I
GspS
GspC
GspH GspI GspJ
GspL GspM
GspO
Type II
VacA ShlB
ShlA YadB/C
YadA
Type V
SecE SecG
SecM
SecB
Sec-Secretion pathway
TatB TatE
Twin arginine targeting (Tat)
VirB1
VirB2
VirB7
VirB6
VirB4
VirB3
VirB9
VirB8
VirB11
VirB5
VirB10
VirD4
Type IV
VgrG
Hcp
Lip
IcmF DotU
Type VI
Planctopirus limnophila Gemmata obscuriglobus Rhodopirellula baltica
Planctopirus limnophila Proteome verification
TolC
HlyD
GspD
GspF GspG
GspK
GspE
ClpV
PpkA Fha1 PppA
SecD/F
YajC YidC
SecA
FtsY
ffh
TatA TatC
OM
PP
IM
CP
SecY
a
b
Supplementary Figure 6: Planctomycetes lack most proteins of canonical secretion
systems
(a) Schematic drawing of bacterial secretion systems I to VI, according to the KEGG database
bacterialsecretionsystemsection.
(b) Proteins that correspond to the individual secretion system are indicated in boxes.
HomologousproteinsencodedinthegenomesofP.limnophila(pink),G.obscuriglobus(green)or
R.baltica(grey)areindicatedinrepresentativecolours.IncaseofP.limnophilamostpredicted
proteinswereconfirmedinproteomicexperiments(shadedpinkandSupplementaryTable2).
While all Planctomycetes possess a slightly modified Sec secretion pathway, only few
homologous proteins of the other secretion systems are present. Noteworthy, R. baltica
harboursalmostallgenesforatypeVIsecretionsystem.
DAPI Nile Red OverlayGFP
SR-SIM
WF
Ove
rlay
Epi
fluor
esce
nce
cba fe
GFP + CCCP GFP GFP + CCCP GFP
3D re
cons
truct
ion
Epi
fluor
esce
nce
Gem
mat
a ob
scur
iglo
bus
i
h
0 %
50 %
100 %d
0 %
50 %
100 %g
Gemmata obscuriglobus Planctopirus limnophila
SupplementaryFigure7:G.obscuriglobustakesupGFPintotheperiplasm
(a-d)G.obscuriglobuscellswerefedwithGFP(green)andanalysedwithwidefieldmicroscopy
(WF).CellspoisonedwithCCCPshowednosignal(a),whilesomeuntreatedcells tookupGFP
(b).Magnifiedcellsrevealedregionsofintensefluorescence,indicatinglocallyconcentratedGFP
(c). For quantification, among 6 fields of view 1281 cells were counted. 10.2% of the cells
internalizedGFP(d).Errorbarsindicatestandarddeviation.Scalebars:1µm.
(e-f) P. limnophila cells do not show GFP uptake in similar experiments. For quantification
among6 fieldsofview1294cellswerecountedwhilenotasingleone internalizedGFP(f+g).
Scalebars:10µm.
(h+i)G.obscuriglobuscellswerefedwithGFPwhilemembraneswerestainedwithNileRedand
the nucleoid with DAPI (blue). Super-resolution structured illumination microscopy (SR-SIM)
revealed an associationof theGFP signalwith the lipid staining (h).The red signal illustrates
complexinvaginationsofthecytoplasmicmembranewhiletheGFPsignalcorrespondstopartof
theenlargedperiplasmicspace in theoverlayandthethree-dimensionalreconstruction(iand
SupplementaryMovie2).Scalebars:1µm.
SR-Tesseler: Voronoi tessellation and Clusterprediction
ba
c
Alexa 647 labelled Dextran on 0.01% Polylysine
Overlay DIC & dSTORM dSTORM
SR-Tesseler: Voronoi tessellation and Clusterprediction
ed
f
dSTORMOverlay DIC & dSTORM
Gemmata obscuriglobus with Alexa 647 labelled Dextran
SR-Tesseler: Voronoi tessellation and Clusterprediction
hg
ic
dSTORMOverlay DIC & dSTORM
Planctopirus limnophila with Alexa 647 labelled Dextran
SupplementaryFigure8:DetaileddSTORMdextranuptakeanalysis.
(a-c) As negative control Alexa Fluor 647 labelled dextran was imaged with differential
interference contrast (a, DIC) and Super-resolution direct stochastic optical reconstruction
microscopic (b, dSTORM). No clusters >40 nm were detected with SR-Tesseler applying a
minimumof20detections.
(d-f)Detailedanalysisof thedSTORMdextran feedingexperimentswithG. obscuriglobus cells
(see Fig. 5e for details). The overlay of a dSTORM and a DIC image demonstrates that red
dextransignalslocalizewithinthecells(d+e).Clusters>40nmwerecalculatedwithSR-Tesseler
applying a minimum of minimum 20 detections and results are visualized in green (f). Scale
bars:10µm.
(g-i)DetailedanalysisofthedSTORMdextranfeedingexperimentswithP.limnophilacells(see
SupplementaryFig.9eforoverview).TheoverlayofdSTORMandDICimagesdemonstratesthat
thereddextransignalslocalizewithinthecells(g+h).Clusters>40nmwerecalculatedwithSR-
Tesselerapplyingaminimumofminimum20detectionsandresultsarevisualizedingreen(i).
Scalebars:10µm.
Ove
rvie
wCtr Dextran +CCCP Dextran -CCCP DextranDextran Detail
WF dSTORM
DAPI Nile Red Dextran Overlay
SR-SIM
b
Epi
fluor
esce
nce a c
3D re
cons
truct
ion
g
f
Epi
fluor
esce
nce
no uptakedextran uptake 0 %
50 %
100 %d e
SupplementaryFigure9:P.limnophilatakesupdextranintotheperiplasm
(a-d)P. limnophila cells, except thoseof thenegative control (Ctr),were fedwith fluorescein-
labelled 40 kDa dextran (green). (a+b) Poisoned cells showed no signal (+CCCP), while other
cells (-CCCP) took up dextran. Scale bars: 10 µm. (c) Magnified cells revealed foci of intense
fluorescence, indicating locally concentrated dextran. Scale bar: 1 µm. (d) For quantification,
among24fieldsofview15,557cellswerecountedand22.17%ofthecellsinternalizeddextran.
Errorbarsindicatestandarddeviation.
(e)Super-resolutiondirectstochasticopticalreconstructionmicroscopic(dSTORM)analysisof
P.limnophilacellsfedwithAlexa647-labelled10kDadextran.Incontrasttodiffractionlimited
micrographs (c), no distinct foci are visible, but the red fluorescence signal shows an almost
homogeneousdistributionofdextraninaconfinedcompartmentofthecell(seeSupplementary
Fig.8g-Ifordetails).Scalebar:1µm.
(f+g) P. limnophila cells were fed with fluorescein-labelled 40 kDa dextran (green), while
membraneswere stainedwithNileRed and the nucleoidewithDAPI (blue). Super-resolution
structuredilluminationmicroscopy(SR-SIM)revealedthatthegreendextransignalislocalized
ininvaginationsoftheinnermembrane(red)thatenlargetheperiplasmicspaceasshowninthe
overlay image and in the three-dimensional reconstruction (g and Supplementary Movie 4).
Scalebar:1µm.
1100
200
300
400
500
600
700
800
900
1000
1100
1200
1300
1400
NU
P120
S. ce
revi
siae
ZP
_02732338.1
G. obsc
uriglo
bus
D5S
XW
5P
. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_1972
D5S
U03
P. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_1153
D5S
VK
0P
. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_1436
D5S
WP
7P
. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_1564
D5S
QU
5P
. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_2734
D5S
R45
P. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_0666
D5S
U68
P. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_3308
D5S
XI6
P. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_1723
D5S
MG
2P
. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_0029
D5S
VH
1P
. lim
nophila
Ord
ere
d L
ocu
s N
am
es:
Plim
_1407
alp
ha
he
lix
be
ta s
tran
d
tran
sme
mb
ran
e h
elix
α-he
lixβ-
stra
ndtra
nsm
embr
ane
helix
Supplementary Figure 10: Putative membrane coat-like proteins of Planctopirus
limnophila
P.limnophilahomologstotheMC-likeproteinZP_02732338.1ofG.obscuriglobuswereidentified
bysequenceanalysesandsecondarystructureprediction.Theblackhorizontal linesrepresent
the sequence of each protein. The predicted α-helices (magenta) and β-strands (cyan) are
indicatedbybarsaboveeachline.Theheightofthebarsisproportionaltotheconfidenceofthe
prediction (Psipred). Predicted transmembrane helices are shown in green boxes below the
sequences(TMMH).Theestimatedlevelofglobularityisindicatedbyalinebelowthesequence
(pred), the higher the line, the more globular. Plim_1972 is the most similar P. limnophila
homologtoZP_02732338.1intermsofsequencecomparisonandstructureprediction.
P. limnophilaWT
P. limnophilaΔ Plim 1972
Dex
tran
10 k
Da
Ove
rlay
ca
3 kb
1 kb
3.628 kb
Plim_1972
1 kb
KanR
Flank PCR
Kan PCR
Flank PCR Kan PCR
M WT Δ1972 - WT Δ1972 - M M WT Δ1972
Anti-Plim_1972
130 kDa100 kDa
b
d e
0
20
40
60
80
f
P: 0.21
Δ Plim_1972WT
Dex
tran
upta
ke p
er c
ell [
%]
SupplementaryFigure11:UptakeofdextraninPlanctopiruslimnophiladoesnotrequire
theMC-likeproteinPlim_1972
(a)ThePlim_1972geneofP.limnophilawasreplacedbyakanamycinresistancecassette(Kan).
ThecontrolPCRs for themutantvalidationconsistedof twodifferentprimersets. InWTcells
the flankingprimersetshallamplifya3.628kb fragmentwhile theKan-primersetshouldnot
resultinanyproduct.IntheDPlim_1972mutant,theflankingprimersetshouldresultina1.1kb
fragmentwhiletheKan-primersetshouldamplifya1kbregionofthemutant’sgenome.
(b) PCR products for P. limnophila WT cells and the DPlim_1972 mutant correspond to the
predictedfragmentlength(a),indicatingintegrityofthemutants’genotype.
(c)WesternblotanalysisofP.limnophilaWTandtheΔPlim_1972mutant.Theantibodyagainst
Plim_1972 detects a protein band around 120 kDa in WT cells while the ΔPlim_1972 mutant
shows no respective band. Employing the protein molecular weight calculator
(www.sciencegateway.org)amassof120.82kDawasestimatedforPlim_1972whichfitstothe
sizeofthedetectedbandforWTcells.
(d-f)P.limnophilaWT(d)andΔPlim_1972mutants(e)werefedwithfluorescence-labelled10
kDa dextran. Wide field epifluorescence and epifluorescence / phase contrast overlays
demonstratethatbothWTandmutantcellstakeupdextran(red).Nosignificantdifferencesin
the uptake among three independent experiments could be detected while 15,556 WT and
19,502 mutant cells were analysed (f, T-test: P=0.21, error bars indicate standard deviation).
Thus,theproteinPlim_1972isnotrequiredfordextranuptake.
SupplementaryTable1:ImmunogoldlocalisationofATPases
Goldparticleswerecountedin10fieldsofview(fov)bythreedifferentresearchers(R#1-R#3).
Localisation was differentiated between background, outer membrane, inner membrane and
unspecific within a cell. Thereby a localization uncertainty of 22.5 nm ∅ caused by antibody
labellingwasacknowledged.
fov
Background OuterMembrane InnerMembrane UnspecificincellR#1 R#2 R#3 R#1 R#2 R#3 R#1 R#2 R#3 R#1 R#2 R#3
1 5 15 12 32 20 17 29 44 57 35 24 132 10 10 18 37 30 24 21 49 53 32 21 223 4 18 17 36 32 25 33 55 59 23 22 194 6 24 18 34 25 30 23 54 67 26 19 185 5 15 21 44 44 15 23 52 67 28 17 206 6 12 10 42 20 13 26 45 52 23 21 247 7 9 16 34 20 22 31 41 49 37 11 148 5 7 13 30 21 18 26 40 50 36 23 239 6 16 21 34 34 24 22 58 63 33 8 16
10 4 15 22 26 26 27 13 30 47 41 9 16
SupplementaryTable2:P.limnophilaproteomeanalysis
List of typical Gram-negative proteins identified by our proteomic approach compared to oursecretion pathway prediction (SECPATH, Supplementary Fig. 6) and to the computationalanalysisbySpethetal.20121.LocalizationpredictionwasachievedwithPSORTB3.0.
ACCESSION NUMBER ANNOTATION
LOCALISATION
WITH PSORTB 3.0
SECPATH SPETH ET AL., 20121
ADG68672.1 Putative TolC Outer membrane + +
ADG69500.1 GspD Outer membrane + +
ADG66639.1 Type II/III ss homologue Outer membrane +
ADG67415.1 Beta barrel transporter Outer membrane +
ADG68191.1 BamA Outer membrane +
ADG68627.1 Beta barrel transporter Outer membrane +
ADG69297.1 TolC homologue Outer membrane +
ADG69651.1 CpaC Outer membrane +
ADG65956.1 LptD Outer membrane
ADG66250.1 Putative fimbrial subunit Outer membrane
ADG66422.1 Hypothetical protein Outer membrane
ADG66532.1 Hypothetical protein Outer membrane
ADG67744.1 OMPT Outer membrane
ADG68522.1 Carboxylase Outer membrane
ADG68596.1 Cytochrome C Outer membrane
ADG67045.1 Hypothetical protein Outer membrane
ADG67290.1 Hypothetical protein Outer membrane
ADG67378.1 Glycanotransferase Outer membrane
ADG69934.1 Hypothetical protein Outer membrane
ADG67060.1 Sulfatase Outer membrane
ADG67760.1 BamB Outer membrane
ADG69252.1 OMPA Outer membrane
ADG69913.1 Porin Outer membrane
ADG69212.1 Esterase Outer membrane
ADG66736.1 Porin Cytoplasm +
ADG69997.1 GspE/PilB Cytoplasm +
ADG67874.1 ClpV/VasG/ClpB Cytoplasm +
ADG68194.1 SecA Cytoplasm +
ADG69980.1 FtsY Cytoplasm +
ADG66008.1 GspF/PilC/PulF Cytoplasmic membrane +
ADG69480.1 PpkA Cytoplasmic membrane +
ADG67183.1 SecD/F Cytoplasmic membrane +
ADG66345.1 SecY Cytoplasmic membrane +
ADG67540.1 YidC Cytoplasmic membrane +
ADG68547.1 TatA Cytoplasmic membrane +
ADG68503.1 TatC Cytoplasmic membrane +
ADG66306.1 Cell adhesion Extracellular +
ADG67429.1 HlyD Periplasm +
ADG69451.1 GspK/ PulK Periplasm +
ADG66488.1 Putative Secretin Unknown
ADG70027.1 Fha1 Unknown +
ADG67044.1 TolC homologue Unknown
ADG67856.1 OMP Unknown +
SupplementaryReferences
1. Speth DR, van Teeseling MC, Jetten MS. Genomic analysis indicates the presence of an asymmetric bilayer outer membrane in planctomycetes and verrucomicrobia. Frontiers in microbiology 3, 304 (2012).