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ecce/ proteins of the inner membrane/ chemotaxis&motility
Flagella Biosynthesis Proteins,
Proteins Involved in Flagellar Rotation
Transducer/Receptor Proteins for Chemotaxis



Flagella Biosynthesis Proteins

Flagella biosynthesis protein FlhA (flhA )
functionrequired for the rod structure of the flagellar apparatus
may constitute the export apparatus of flagellin together with FliI and FliH
interaction 
regulation 
topologytransmembrane domains: 7 (potential), SP has 8

TMHMM gives 21-43 47-64 76-98 113-135 209-231 251-273 285-307
SP gives 24-44 46-66 71-91 95-115 121-141 209-229 247-267 296-316

msnlaamlrl panlkstqwq ILAGPILILL ILSMMVLPLP AFIldlLFTF
NIALSIMVLL VAMFtqrtle faafpTILLF TTLLRLALNV ASTRIILMeg
htgaaaagkv veAFGHFLVG GNFAIGIVVF VILVIinfmv itkgagriae
vgarfvldgm pgkqmaidad lnagligede akkrrsevtq eadfygsmdg 200
askfvrgdAI AGILIMVINI VGGLLVGVLQ Hgmsmghaae sytlltigdg
LVAQIPALVI STAAGVIVTR VSTdqdvgeq mvnqLFSNPS VMLLSAAVLG
LLGLVPGmpn lvfllftagl lglawwirgr eqkapaepkp vkmaenntvv
eatwndvqle dslgmevgyr lipmvdfqqd gellgrirsi rkkfaqemgf 400
lppvvhirdn mdlqparyri lmkgveigsg daypgrwlai npgtaagtlp
geatvdpafg lnaiwiesal keqaqiqgyt vveastvvat hlnhlisqha
aelfgrqeaq qlldrvaqem pkltedlvpg vvtlttlhkv lqnlldekvp
irdmrtilet laehapiqsd pheltavvrv algraitqqw fpgkdevhvi 600
gldtplerll lqalqggggl epgladrlla qtqealsrqe mlgappvllv
nhalrpllsr flrrslpqlv vlsnlelsdn rhirmtatig gk

MW74842 Da; 692 aa


Flagella biosynthesis protein Flh B (flhB )
functionrequired for the rod structure of the flagellar apparatus
may constitute the export apparatus of flagellin together with FliI and FliH
interaction 
regulation 
topologytransmembrane domains: 4 (potential), SP has 5

TMHMM gives 34-53 92-114 145-167 188-210
SP gives 32-52 74-94 95-115 145-165 190-210

msdesddkte aptphrleka reegqiprsr eltSLLILLV GVSVIWFGGV
SLArrlsgml saglhfdhsi indpnlilgq iillireaml aLLPLISGVV
LVALISPVML GGLVfsgksl qpkfsklnpl pgikrmfsaq tgaeLLKAIL
KTILVGSVTG FFLWHHWpqm mrlmaespit amgnamdLVG LCALLVVLGV 200
IPMVGFDVFF qifshlkklr msrqdirdef kqsegdphvk grirqmqraa
arrrmmadvp kadvivnnpt hysvalqyde nkmsapkvva kgaglvalri
reigaennvp tleapplara lyrhaeigqq ipgqlyaava evlawvwqlk
rwrlaggqrp vqpthlpvpe aldfinekpt he

MW42237 Da; 382 aa


Flagella biosynthesis protein FliP (fliP )
functionplays a role in the flagellum-specific transport system
interaction 
regulation 
topologytransmembrane domains: 5 (potential)

TMHMM gives 7-26 46-68 88-105 185-207 214-236
SP gives 4-24 45-65 88-108 185-205 209-229

mrrllsVAPV LLWLITPLAF AQLPGItsqp lpgggqswsl pvqtlVFITS
LTFIPAILLM MTSFTRIIiv fgllrnalgt psappnqVLL GLALFLTFFI
MSPVIdkiyv dayqpfseek ismqealekg aqplrefmlr qtreadlglf
arlantgplq gpeavpmril lpayvtselk tafqIGFTIF IPFLIIDLVI 200
ASVLMALgmm mvpPATIALP FKLMLFVLVD GWQLLVgsla qsfys

MW26928 Da; 245 aa


Flagella biosynthesis protein FliQ (fliQ )
functionrequired for the assembly of the rivet at the earliest stage of flagellar biosynthesis
interaction 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 20-42 52-74
SP gives 16-40 55-75

mtpesvmmmg teamkvalaL AAPLLLVALV TGLIISILQA ATqinemtls
fIPKIIAVFI AIIIAGPWML NLLLdyvrtl ftnlpyiig

MW9632 Da; 89 aa


Flagella biosynthesis protein FliR (fliR )
functionrole in flagella biosynthesis
interaction 
regulation 
topologytransmembrane domains: 6 (potential), SP has 8

TMHMM gives 15-34 41-58 73-95 132-154 179-201 214-236
SP gives 13-33 45-65 66-86 90-110 131-151 184-204 213-233 235-255

mlqvtseqwl swlnLYFWPL LRVLALISTA PILSersvpk RVKLGLAMMI
TFAIAPSLpa ndvpvfsffa lwLAVQQILI GIALGFTMQF AFAAVrtage
iiglqmglsf atfvdpashl nmpvlarimd mLALLLFLTF NGHLWLISLL
VDTFhtlpig geplnsnafl altkagslIF LNGLMLALPL ITLLLTLNLA 200
Lgllnrmapq lsiFVIGFPL TLTVGISLMA ALMPLIapfc ehlfseifnl
ladiiselpl i

MW28542 Da; 261 aa


Flagella Rotation

Chemotaxis MotA protein (motA )
functionrequired for the rotation of the motor, probabale transmembrane proton channel
interaction 
regulation 
topologytransmembrane domains: 4 (potential)

TMHMM gives 7-29 34-51 171-190 205-227
SP gives 2-21 34-51 171-191 201-222

mlillgYLVV LGTVFGGYLM TGGSLGALYq paeLVIIAGA GIGSFIVGNN
Gkaikgtlka lpllfrrsky tkamymdlla llyrlmaksr qmgmfslerd
ienpreseif asyprilads vmldfivdyl rliisghmnt feiealmdee
ietheseaev panslalvgd SLPAFGIVAA VMGVVHALGS adrpaaelga 200
liahAMVGTF LGILLAYGFI SPLATVLrqk saetskmmqc vkvtllsnln
gyappiavef grktlysser psfieleehv ravknpqqqt tteea

MW32011 Da; 295 aa


Chemotaxis MotB protein (motB )
functionrequired for the rotation of the flagellar motor, might be a linker that fastens the TorQUE generating machinery to the cell wall
interaction 
regulation 
topologytransmembrane domains: 1 (potential)

TMHMM gives 21-43
SP gives 28-49

mknqahpiiv vkrrkakshg aahgsWKIAY ADFMTAMMAF FLVMWLIsis
spkeliqiae yfrtplatav tggdrisnse spipgggddy tqsqgevnkq
pnieelkkrm eqsrlrklrg dldqliesdp klralrphlk idlvqeglri
qiidsqnrpm frtgsadvep ymrdilraia pvlngipnri slsghtddfp 200
yasgekgysn welsadrana srrelmvggl dsgkvlrvvg maatmrlsdr
gpddavnrri sllvlnkqae qailhenaes qnepvsalek pevapqvsvp
tmpsaepr

MW34186 Da; 308 aa


Chemotaxis Receptors/Transducers

Aerotaxis receptor (aer )
functionsignal transducer for aerotaxis, responses to accumulation of cells around air bubbles
interaction 
regulation 
topologytransmembrane domains: 1 (potential), SP has 2

TMHMM gives 172-194
SP gives 167-186 191-209

msshpyvtqq ntpladdttl msttdlqsyi thandtfvqv sgytlqelqg
qphnmvrhpd mpkaafadmw ftlkkgepws givknrrkng dhywvranav
pmvregkisg ymsirtratd eeiaaveply kalnagrtsk rihkglvvrk
gwlgklpslp lrwrargvmt lMFILLAAML WFVAAPVVTY ILCAlvvlla 200
sacfewqivr pienvahqal kvatgernsv ehlnrsdelg ltlravgqlg
lmcrwlindv ssqvssvrng setlakgtde lnehtqqtvd nvqqtvatmn
qmaasvkqns atasaadkls itasnaavqg geamttvikt mddiadstqr
igtitslind iafqtnilal naaveaarag eqgkgfavva gevrhlasrs 400
anaandirkl idasadkvqs gsqqvhaagr tmedivaqvk nvtqliaqis
hstleqadgl ssltravdel nlitqknael veesaqvsam vkhrasrled
avtvlh

MW55065 Da; 506 aa


Methyl accepting chemotaxisprotein IV (tap )
functionmediates taxis towards dipeptides via an interaction with the periplasmic dipeptide binding protein
interaction 
regulationmethyl groups are added by CheR and remover by CheB
topologytransmembrane domains: 2 (potential)

TMHMM gives 10-32 187-209
SP gives 7-33 187-212

mfnriristT LFLILILCGI LQIGSNGMSF WAfrddlqrl nqveqsnqqr aalaqtravm lqastalnka gtltalsypa ddiktlmtta rasltqsttl fksfmamtag nehvrglqke teksfarwhn dlehqatwle snqlsdflta pvqgsqnafd vnfeawqlei nhvleaasaq sqrnyqISAL VFISMIIVAA 200 IYISSALWWt rkmivqplai igshfdsiaa gnlarpiavy grneitaifa slktmqqalr gtvsdvrkgs qemhigiaei vagnndlssr teqqaaslaq taasmeqlta tvgqnadnar qaselaknaa ttaqaggvqv stmthtmqei atssqkigdi isvidgiafq tnilalnaav eaarageqgr gfavvagevr 400 nlasrsaqaa keikgliees vnrvqqgskl vnnaaatmid ivssvtrvnd imgeiasase eqqrgieqva qavsqmdqvt qqnaslveea avateqlanq adhlssrvav ftleehevar hesvqlqiap vvs

MW57511 Da; 533 aa


Methyl accepting chemotaxisprotein II (tar )
functionreceptor for the attractant L-aspartate and related amino acids, also mediates taxis towards the attractant maltose via an interaction with ther periplasmic maltose-binding protein, mediates taxis away from repellents cobalt and nickel
interaction 
regulationmethyl groups are added by CheR and remover by CheB
topology3-d structure/PDB
transmembrane domains: 2

TMHMM gives 7-29 190-212
SP gives 7-33 191-215

minrirVVTL LVMVLGVFAL LQLISGSLFf sslhhsqksf vvsnqlreqq geltstwdlm lqtrinlsrs avrmmmdssn qqsnakvell dsarktlaqa athykkfksm aplpemvats rnidekykny ytaltelidy ldygntgayf aqptqgmqna mgeafaqyal sseklyrdiv tdnaddyrfA QWQLAVIALV 200 VVLILLVAWY GIrrmlltpl akiiahirei aggnlantlt idgrsemgdl aqsvshmqrs ltdtvthvre gsdaiyagtr eiaagntdls srteqqasal eetaasmeql tatvkqnadn arqasqlaqs asdtaqhggk vvdgvvktmh eiadsskkia diisvidgia fqtnilalna aveaarageq grgfavvage 400 vrnlasrsaq aakeikalie dsvsrvdtgs vlvesagetm nnivnavtrv tdimgeiasa sdeqsrgidq valavsemdr vtqqnaslvq esaaaaaale eqasrltqav safrlaaspl tnkpqtpsrp aseqppaqpr lriaeqdpnw etf

MW59943 Da; 533 aa


Methyl accepting chemotaxisprotein III (trg )
functionmediates taxis to the sugars ribose and galactose via an interaction with their periplasmic binding proteins
interaction 
regulationmethyl groups are added by CheR and remover by CheB
topologytransmembrane domains: 2 (potential), SP has 1

TMHMM gives 20-42 199-221
SP gives 202-222

mnttpsqrlg flhhirlvpL FACILGGILV LFALSSALAG YFlwqadrdq rdvtaeieir tglanssdfl rsarinmiqa gaasriaeme amkrniaqae seikqsqqgy rayqnrpvkt padealdtel nqrfqayitg mqpmlkyakn gmfeaiinhe seqirpldna ytdilnkavk irstranqla elahqrtrLG 200 GMFMIGAFVL ALVMTLITFM Vlrrivirpl qhaaqrieki asgdltmnde pagrneigrl srhlqqmqhs lgmtvgtvrq gaeeiyrgts eisagnadls srteeqaaai eqtaasmeql tatvkqnadn ahhasklaqe asikasdggq tvsgvvktmg aistsskkis eitavinsia fqtnilalna aveaarageq 400 grgfavvase vrtlasrsaq aakeieglis esvrlidlgs devatagktm stivdavasv thimqeiaaa sdeqsrgitq vsqaisemdk vtqqnaslve easaaavsle eqaarlteav dvfrlhkhsv saeprgagep vsfatv

MW58898 Da; 546 aa


Methyl-accepting chemotaxis protein I (tsr )
functionreceptor for the attractant L-serine and related amino acids also responsible for a chemotaxis of a wide range nof repellents, including leucine, indole and weak acids
interaction 
regulationmethyl groups are added by CheR and remover by CheB
topologytransmembrane domains: 2 (potential)

TMHMM gives 7-29 192-214
SP gives 7-30 191-210

mlkrikIVTS LLLVLAVFGL LQLTSGGLFf nalkndkenf tvlqtirqqq stlngswval lqtrntlnra girymmdqnn igsgstvael mesasislkq aeknwadyea lprdprqsta aaaeikrnyd iyhnalaeli qllgagkine ffdqptqgyq dgfekqyvay meqndrlhdi avsdnnasys qAMWILVGVM 200 IVVLAVIFAV WFGIkaslva pmnrlidsir hiaggdlvkp ievdgsnemg qlaeslrhmq gelmrtvgdv rnganaiysg aseiatgnnd lssrteqqaa sleetaasme qltatvkqna enarqashla lsasetaqrg gkvvdnvvqt mrdistssqk iadiisvidg iafqtnilal naaveaarag eqgrgfavva 400 gevrnlaqrs aqaareiksl iedsvgkvdv gstlvesage tmaeivsavt rvtdimgeia sasdeqsrgi dqvglavaem drvtqqnaal veesaaaaaa leeqasrlte avavfriqqq qretsavvkt vtpaaprkma vadseenwet f

MW59443 Da; 551 aa