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ecce/ proteins of the inner membrane/ enzymes II


-Oxidoreductases acting on NADH or NADPH with quinon or similar compound as acceptor

-Oxidoreductases acting on diphenols and related compounds with oxygen as acceptor

-Phosphotransferases with a nitrogenous group as acceptor (sensor proteins of two-component regulatory systems)

-Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides


Oxidoreductases Acting on NADH or NADPH with Quinon or Similar Compound as Acceptor

NADH dehydrogenase I chain A (nuoA )
functiontransfer of electrons from NADH to the respiratory chain
composed of 14 different subunits: NuoA, H, J, K, L, M, N constitute the membrane sector of the complex
interactionelectron acceptor is believed to be ubiquinone
cofactors 
regulation 
topologytransmembrane domains: 3 (potential)

TMHMM gives 15-37 68-90 100-122
SP gives 16-36 68-88 98-118

msmststevi ahhwAFAIFL IVAIGLCCLM LVGGWFLggr ararsknvpf
esgidsvgsa rlrlsakFYL VAMFFVIFDV EALYLFAWST siresgwvgF
VEAAIFIFVL LAGLVYLVRI GAldwtpars rrermnpetn sianrqr

MW16457 Da; 147 aa


NADH dehydrogenase I chain H (nuoH )
functiontransfer of electrons from NADH to the respiratory chain
composed of 14 different subunits: NuoA, H, J, K, L, M, N constitute the membrane sector of the complex
interactionelectron acceptor is believed to be ubiquinone
cofactors 
regulation 
topologytransmembrane domains: 8 (potential)

TMHMM gives 10-32 81-103 113-135 155-174 184-206 235-257 267-289 302-324
SP gives 11-31 81-101 114-134 154-174 186-206 237-257 265-285 304-324
mswispeliE ILLTILKAVV ILLVVVTCGA FMsfgerrll glfqnrygpn
rvgwggslql vadmikmffk edwipkfsdr VIFTLAPMIA FTSLLLAFAI
VPVspgwvva dlNIGILFFL MMAGLAVYAV LFAGWssnnk ysllgamras
aqtlSYEVFL GLSLMGVVAQ AGSFnmtdiv nsqAHVWNVI PQFFGFITFA 200
IAGVAVchrh pfdqpeaeqe ladgyhieys gmkfGLFFVG EYIGIVTISA
LMVTLFFggw qgpllpPFIW FALKTAFFMM MFILIRASLp rprydqvmsf
gWKICLPLTL INLLVTAAVI LWQAq

MW36219 Da; 325 aa


NADH dehydrogenase I chain J (nuoJ )
functiontransfer of electrons from NADH to the respiratory chain
composed of 14 different subunits: NuoA, H, J, K, L, M, N constitute the membrane sector of the complex
interactionelectron acceptor is believed to be ubiquinone
cofactors 
regulation 
topologytransmembrane domains: 5 (potential)

TMHMM gives 4-22 29-51 56-78 91-113 133-155
SP gives 1-21 28-48 54-74 92-112 138-158

mefAFYICGL IAILATLRVI THtnpvhaLL YLIISLLAIS GVFFSLGAYF
AgaleIIVYA GAIMVLFVFV VMMLNLGGse ieqerqwlkp QVWIGPAILS
AIMLVVIVYA ILGvndqgid gtpisakavg itLFGPYVLA VELASMLLLA
GLVVAfhvgr eeragevlsn rkddsakrkt eeha

MW19874 Da; 184 aa


NADH dehydrogenase I chain K (nuoK )
functiontransfer of electrons from NADH to the respiratory chain
composed of 14 different subunits: NuoA, H, J, K, L, M, N constitute the membrane sector of the complex
interactionelectron acceptor is believed to be ubiquinone
cofactors 
regulation 
topologytransmembrane domains: 3 (potential), SP has 2

TMHMM gives 4-23 28-50 60-82
SP gives 4-24 60-80

mipLQHGLIL AAILFVLGLT GLVirrnLLF MLIGLEIMIN ASALAFVVAG
sywgqtdgqV MYILAISLAA AEASIGLALL LQlhrrrqnl nidsvsemrg

MW10845 Da; 100 aa


NADH dehydrogenase I chain L (nuoL )
functiontransfer of electrons from NADH to the respiratory chain
composed of 14 different subunits: NuoA, H, J, K, L, M, N constitute the membrane sector of the complex
interactionelectron acceptor is believed to be ubiquinone
cofactors 
regulation 
topologytransmembrane domains: 16 (potential), SP has 14

TMHMM gives 4-21 28-50 84-106 113-132 136-158 171-193 213-235 248-267 277-299 306-328 332-354 375-397 412-434 455-477 492-514 590-612
SP gives 7-23 32-52 75-99 116-133 211-228 249-267 282-300 307-325 339-356 374-397 414-437 455-472 495-514 590-607

mnmLALTIIL PLIGFVLLAF SrgrwseNVS AIVGVGSVGL AALVTAFIGV
dffangeqty sqplwtwmsv gdfnigfnlv ldgLSLTMLS VVTGVGFLIH
MYASWYmrge egYSRFFAYT NLFIASMVVL VLadnLLLMY LGWEGVGLCS
YLLIGFYYtd pkngaaamka FVVTRVGDVF LAFALFILYN ELGtlnfrem 200
velapahfad gnNMLMWATL MLLGGAVGKS AQLPLqtwla damagptPVS
ALIHAATMVT AGVYLIArth glflmtPEVL HLVGIVGAVT LLLAGFAALv
qtdikRVLAY STMSQIGYMF LALGVQAWda aIFHLMTHAF FKALLFLASG
SVILachheq nifkmgglrk siplVYLCFL VGGAALSALP LVTAGFFskd 400
eilagamang hINLMVAGLV GAFMTSLYTF RMIFivfhgk eqihahavkg
vthsLPLIVL LILSTFVGAL IVPPLQGvlp qttelahgsm lTLEITSGVV
AVVGILLAAW LWLGkrtlvt siansapgrl lgtwwynawg fdwlydkvfv
kpflgiawll krdplnsmmn ipavlsrfag kglllsengY LRWYVASMSI 600
GAVVVLALLM VLr

MW66438 Da; 613 aa


NADH dehydrogenase I chain M (nuoM )
functiontransfer of electrons from NADH to the respiratory chain
composed of 14 different subunits: NuoA, H, J, K, L, M, N constitute the membrane sector of the complex
interactionelectron acceptor is believed to be ubiquinone
cofactors 
regulation 
topologytransmembrane domains: 14 (potential)

TMHMM gives 4-18 30-49 81-103 115-134 139-161 174-196 222-244 251-273 288-307 314-336 341-363 384-406 416-438 459-481
SP gives 1-21 30-50 83-103 122-142 174-194 222-242 259-279 286-306 314-334 340-360 383-403 404-424 426-446 465-485

mllPWLILIP FIGGFLCWqt erfgvkvprW IALITMGLTL ALSLQLWLQg
gysltqsagi pqwqsefdmp wiprfgisih LAIDGLSLLM VVLTGLLGVL
AVLcswkeie kyqgFFHLNL MWILGGVIGV FLAIdmflFF FFWEMMLVPM
YFLIALWGHK Asdgktrita atkFFIYTQA SGLVMLIAIL ALVFVHynat 200
gvwtfnyeel lntpmssgve yLLMLGFFIA FAVKMPVVPL HGWLpdahsq
APTAGSVDLA GILLKTAAYG LLRfslplfp nasaefaPIA MWLGVIGIFY
GAWMAFAqtd ikrLIAYTSV SHMGFVLIAI YTGSQLayqg AVIQMIAHGL
SAAGLFILCG QLYerihtrd mrmmgglwsk mkwLPALSLF FAVATLGMPG 400
TGNFVGefmi lfgsfQVVPV ITVISTFGLV FASVYSLAml hrayfgkaks
qiasqelpGM SLRELFMILL LVVLLVLLGF Ypqpildtsh saigniqqwf
vnsvtttrp

MW56524 Da; 509 aa


NADH dehydrogenase I chain N (nuoN )
functiontransfer of electrons from NADH to the respiratory chain
composed of 14 different subunits: NuoA, H, J, K, L, M, N constitute the membrane sector of the complex
interactionelectron acceptor is believed to be ubiquinone
cofactors 
regulation 
topologytransmembrane domains: 12 (potential)

TMHMM gives 15-37 44-61 65-87 99-121 141-163 176-198 208-230 237-259 269-291 311-333 348-370 390-412
SP gives 11-31 45-65 67-87 99-119 143-163 175-195 211-231 237-257 266-286 313-333 336-356 395-415

mdvtplmrvd gfamLYTGLV LLASLATCTF AYPWLEGynd nkdEFYLLVL
IAALGGILLA NanhLASLFL GIELISLPLF GLVGYAFrqk rsleasikYT
ILSAAASSFL LFGMALVYAQ Sgdlsfvalg knlgdgmlne PLLLAGFGLM
IVGLGFKLSL VPFhlwtpdv yqgapAPVST FLATASKIAI FGVVMRLFly 200
apvgdseAIR VVLAIIAFAS IIFGNLMALS qtnikrLLGY SSISHLGYLL
VALIALQTGe msmeavgvYL AGYLFSSLGA FGVVSLMSSP Yrgpdadslf
syrglfwhrp ILAAVMTVMM LSLAGIPMTL GFIgkfyvla vgvqahlWWL
VGAVVVGSAI GLYYYLRVAV slylhapeqp grdapsnwqY SAGGIVVLIS 400
ALLVLVLGVW PQplisivrl amplm

MW45650 Da; 425 aa



Oxidoreductases Acting on Diphenols and Related Compounds with Oxygen as Acceptor

Cytochrome bdII oxidase subunit II (appB )
functionterminal step in respiratory chain
interactionheterodimer of subunits I and
cofactors 
regulationinduction: stationary phase, triggered by phosphate starvation or shift from aerobic to anaerobic conditions
topologytransmembrane domains: 8 (potential)

TMHMM gives 7-24 78-100 121-143 166-188 209-231 263-285 292-314 334-356
SP gives 9-28 80-99 123-142 165-184 206-225 262-281 292-311 336-355

mfdyetLRFI WWLLIGVILV VFMIsdgfdm gigcllplva rndderrivi
nsvgahwegn qvwlilagga lfaawprVYA AAFSGFYVAM ILVLCSLFFR
plafdyrgki adarwrkmwd AGLVIGSLVP PVVFGIAFGN LLLgvpfaft
pqlrveylgs fwqllTPFPL LCGLLSLGMV ILQGGVWLql ktvgvihlrs 200
qlatkraaLL VMLCFLLAGY WLWVGIDGFV Llaqdangps nplmklvavl
pgawmnnfve spVLWIFPLL GFFCPLLTVM AIYRGrpgwg fLMASLMQFG
VIFTAGITLF PFVMpssvsp issltlwdst ssqLTLSIML VIVLIFLPIV
LLYTLWsyyk mwgrmttetl rrnenely

MW42423 Da; 378 aa


Cytochrome bdII oxidase subunit I (appC )
functionterminal step in respiratory chain
interaction 
cofactors 
regulationinduction: stationary phase, triggered by phosphate starvation or shift from aerobic to anaerobic conditions, n-terminal is blocked
topologyheterodimer of subunits I and II
transmembrane domains: 9 (potential), SP has 7

TMHMM gives 20-42 54-76 96-118 125-147 186-208 215-237 387-409 421-443 466-488
SP gives 23-42 95-114 130-149 188-207 220-239 393-412 471-490

mwdvidlsrw qfaltalyhF LFVPLTLGLI FLLAIMETIY VVtgktiyrd
mtrFWGKLFG INFALGVATG LTMEFQfgtn wsfysnyvgd ifgapLAMEA
LMAFFLESTF VGLFFFGWqr lnkyQHLLVT WLVAFGSNLS ALWILNAngw
mqyptgahfd idtlrmemts fselvfnpvs qvkfvHTVMA GYVTGAMFIM 200
AISAWYLLrg rernVALRSF AIGSVFGTLA IIGTLQLgds sayevaqvqp
vklaamegew qtepapapfh vvawpeqdqe rnafalkipa llgilathsl
dkpvpglknl maetyprlqr grmawllmqe isqgnrephv lqafrglegd
lgygmllsry apdmnhvtaa qyqaamrgai pqvapvFWSF RIMVGCGSLL 400
LLVMLIALVq tlrgkidqhr WVLKMALWSL PLPWIAIEAG WFMtefgrqp
waiqdilpty sahsaLTTGQ LAFSLIMIVG LYTLFLIAev ylmqkyarlg
psamqseqpt qqqg

MW57920 Da; 514 aa


Cytochrome d ubiquinol oxidase subunit I (cydA )
functionterminal steps in respiratory chain, complex predominates at low aeration
interactionheterodimer of subunits I and II
cofactorscontains protoheme IX center B595 and one iron-chlorine
regulation 
topology
transmembrane domains: 9 (potential), SP has 7

TMHMM gives 20-42 54-76 96-118 130-152 184-206 219-238 387-409 421-443 471-493
SP gives 23-42 95-114 130-149 188-207 220-239 393-412 471-490

mldivelsrl qfaltamyhF LFVPLTLGMA FLLAIMETVY VLsgkqiykd
mtkFWGKLFG INFALGVATG LTMEFQfgtn wsyyshyvgd ifgapLAIEG
LMAFFLESTF VGLFFFGWdr lgkvqhmcvT WLVALGSNLS ALWILVANGW
MQnpiasdfn fetmrmemvs fselvlnpva qvkFVHTVAS GYVTGAMFIL 200
GISAWYmlkg rdfafakrSF AIAASFGMAA VLSVIVLGde sgyemgdvqk
tklaaieaew etqpapaaft lfgipdqeee tnkfaiqipy algiiatrsv
dtpviglkel mvqheerirn gmkayslleq lrsgstdqav rdqfnsmkkd
lgyglllkry tpnvadatea qiqqatkdsi prvaplYFAF RIMVACGFLL 400
LAIIALSFWs virnrigekk WLLRAALYGI PLPWIAVEAG WFVaeygrqp
waigevlpta vanssltagd LIFSMVLICG LYTLFLVAEL FLMfkfarlg
psslktgryh feqsstttqp ar

MW57920 Da; 522 aa


Cytochrome d ubiquinol oxidase subunit II (cydb )
functionterminal steps in respiratory chain, complex predominates at low aeration
interactionheterodimer of subunits I and II
cofactorscontains protoheme IX center b595 and one iron-chlorine
regulation 
topologytransmembrane domains: 8 (potential)

TMHMM gives 7-24 77-99 123-145 160-182 203-225 262-281 293-315 335-357
SP gives 9-28 80-99 123-142 165-184 206-225 263-282 293-312 337-356

midyevLRFI WWLLVGVLLI GFAVtdgfdm gvgmltrflg rndterrimi
nsiaphwdgn qvwlitagga lfaawpMVYA AAFSGFYVAM ILVLASLFFr
pvgfdyrski eetrwrnmwd wgIFIGSFVP PLVIGVAFGN LLQGVpfnvd
eylrlyytgN FFQLLNPFGL LAGVVSVGMI ITqgatylqm rtvgelhlrt 200
raTAQVAALV TLVCFALAGV WVMYGidgyv vkstmdhyaa snplnkevvr
eagawlvnfn nTPILWAIPA LGVVLPLLTI Ltarmdkaaw afVFSSLTLA
CIILTAGIAM FPFVMpsstm mnasltmwda tssqLTLNVM TWVAVVLVPI
ILLYTAWcyw kmfgritked iernthsly

MW42453 Da; 379 aa


Ubiquinol oxydase polypeptide II precursor (cyoA )
functioncomplex is part of respiratory chain that predominates, when cells are grown at high aeration
interaction 
cofactors 
regulation 
topology3-d structure
transmembrane domains: 3 (potential), SP has 2

TMHMM gives 12-30 45-67 88-110
SP gives 51-68 93-111

mrlrkynksl gWLSLFAGTV LLSGCNSALL dpkgqigleq rsliLTAFGL
MLIVVIPAIL MAVGFAWkyr asnkdakysp nwshsnkVEA VVWTVPILII
IFLAVLTWKT thalepskpl ahdekpitie vvsmdwkwff iypeqgiatv
neiafpantp vyfkvtsnsv mnsffiprlg sqiyamagmq trlhlianep 200
gtydgisasy sgpgfsgmkf kaiatpdraa fdqwvakakq spntmsdmaa
feklaapsey nqveyfsnvk pdlfadvink fmahgksmdm tqpegehsah
egmegmdmsh aesah

MW34911 Da; 315 aa


Ubiquinol oxydase polypeptide I (cyoB )
functioncomplex is part of respiratory chain that predominates, when cells are grown at high aeration.
Shows proton pump activity across the membrane in addition to electron transfer. Catalyses terminal step in respiratory chain
interaction 
cofactorscontains two protoheme IX (heme b55 and b562) and copper B
regulation 
topologytransmembrane domains: 14 (potential), SP has 15

TMHMM gives 15-37 57-79 105-127 140-162 191-213 233-255 275-297 310-332 347-369 382-404 414-436 457-479 494-516 590-612
SP gives 17-35 58-76 102-121 144-162 195-213 232-250 277-296 320-339 348-366 382-401 410-429 458-476 495-513 588-606 614-632

mfgklsldav pfhePIVMVT IAGIILGGLA LVGLITYfgk wtylwkewlt
svdhkrLGIM YIIVAIVMLL RGFADAIMMr sqqalasage agflpphhyd
qiftAHGVIM IFFVAMPFVI GLMNLVVplq igardvafpF LNNLSFWFTV
VGVILVNVSL GVgefaqtgw laypplsgie yspgvgvdyw IWSLQLSGIG 200
TTLTGINFFV TILkmrapgm tmfkmpvftw asLCANVLII ASFPILTVTV
ALLTLdrylg thfftndmgg nmmmYINLIW AWGHPEVYIL ILPVFGVfse
iaatfsrkrL FGYTSLVWAT VCITVLSFIV WLhhfftmga ganvnaFFGI
TTMIIAIPTG VKIFNWLFTm yqgrivfhsa mLWTIGFIVT FSVGGMTGVL 400
LAVPgadfvl hnsLFLIAHF HNVIIGGVVF GCFAGMtyww pkafgfklne
twgkraFWFW IIGFFVAFMP LYALGFMGMt rrlsqqidpq fhtMLMIAAS
GAVLIALGIL CLVIQMyvsi rdrdqnrdlt gdpwggrtle watsspppfy
nfavvphvhe rdafwemkek geaykkpdhy eeihmpknsG AGIVIAAFST 600
IFGFAMIWHI WWlaivgfag miitwivksf dedvdyyvpv aeieklenqh
fdeitkaglk ngn

MW74368 Da; 663 aa


Cytochrome o ubiquinol oxydase subunit III (cyoC )
functioncomplex is part of respiratory chain that predominates, when cells are grown at high aeration
interaction 
cofactorscontains two protoheme IX (heme b55 and b562) and copper B
regulation 
topologytransmembrane domains: 5 (potential)

TMHMM gives 27-49 69-91 98-118 138-160 181-203
SP gives 32-50 67-85 102-120 143-161 185-203

matdtlthat ahahehghhd aggtkiFGFW IYLMSDCILF SILFATYAVl
vngtaggptg kdifelpfVL VETFLLLFSS ITYGMAAIAM YknnksqVIS
WLALTWLFGA GFIGMEIYef hhlivngmgp drsgflsAFF ALVGTHGLHV
TSGLIWMAVL mvqiarrglt stnrtrimcl SLFWHFLDVV WICVFTVVYL 200
MGAm

MW22622 Da; 204 aa


Cytochrome o ubiquinol oxydase operon protein CyoD (cyoD )
functioncomplex is part of respiratory chain that predominates, when cells are grown at high aeration
interaction 
cofactorscontains two protoheme IX (heme b55 and b562) and copper B
regulation 
topologytransmembrane domains: 3 (potential)

TMHMM gives 21-40 44-66 78-100
SP gives 18-36 46-64 81-99

mshstdhsga shgsvktymt GFILSIILTV IPFWMVMTGA aspAVILGTI
LAMAVVQVLV HLVCFLhmnt ksdegwnMTA FVFTVLIIAI LVVGSIWIMW
nlnynmmmh

MW12029 Da; 109 aa


Cytochrome o ubiquinol oxydase operon protein CyoE (cyoE )
functioncomplex is part of respiratory chain that predominates, when cells are grown at high aeration
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential), TMHMM has 9

TMHMM gives 12-34 38-60 81-103 108-127 134-156 161-183 209-231 235-252 264-286
SP gives 10-28 38-56 79-97 108-126 198-216 229-247 269-287

mmfkqylqvt kpgIIFGNLI SVIGGFLLAS KGSIdypLFI YTLVGVSLVV
ASGCVFNNYI drdidrkmer tknrvlvkgl ISPAVSLVYA TLLGIAGFML
LWFganpLAC WLGVMGFVVY VGVYSLYmkr hsvygtligs lsgaappvig
ycavtgefds gaaillaifs lwqmphsyai aifrfkdyqa anipvlpvvk 200
gisvaknhIT LYIIAFAVAT LMLSLGGYAG YkylVVAAAV SVWWLGMALR
GYkvaddriw arkLFGFSII AITALSVMMS VDFMVPdsht llaavw

MW32248 Da; 296 aa


Phosphotransferases with a Nitrogenous Group as Acceptor (Sensor Proteins of Two-Component Regulatory Systems)

Aerobic respiration control sensor protein AcrB (arcB )
functionanaerobic repression of arc modulon
interactionactivates AcrA by phosphorylation
cofactors 
regulation 
topology3d structurePDB


transmembrane domains: 2 (potential)

TMHMM gives 20-42 55-77
SP gives 23-50 58-77

mkqirllaqy yvdlmmklgL VRFSMLLALA LVVLAIVVQM AVtmvlhgqv
esidVIRSIF FGLLITPWAV YFLSVVVeql eesrqrlsrl vqkleemrer
dlslnvqlkd niaqlnqeia vrekaeaelq etfgqlkiei kereetqiql
eqqssflrsf ldaspdlvfy rnedkefsgc nramelltgk sekqlvhlkp 200
advyspeaaa kvietdekvf rhnvsltyeq wldypdgrka cfeirkvpyy
drvgkrhglm gfgrditerk ryqdaleras rdkttfisti shelrtplng
ivglsrilld teltaeqeky lktihvsavt lgnifndiid mdkmerrkvq
ldnqpvdfts fladlenlsa lqaqqkglrf nleptlplph qvitdgtrlr 400
qilwnlisna vkftqqgqvt vrvrydegdm lhfevedsgi gipqdeldki
famyyqvkds hggkpatgtgig lavsrrlakn mggditvtse qgkgstftlt
ihapsvaeev ddafdeddmp lpalnvllve dielnvivar svleklgnsv
dvamtgkaal emfkpgeydl vlldiqlpdm tgldisrelt krypredlpp 602
lvaltanvlk dkqeylnagm ddvlskplsv paltamikkf wdtqddeest
vtteenskse alldipmleq ylelvgpkli tdglavfekm mpgyvsvles
nltaqdkkgi veeghkikga agsvglrhlq qlgqqiqspd lpawednvge
wieemkeewr hdvevlkawv akatkk

MW87982 Da; 778 aa


Sensor protein AtoS (atoS )
function 
interactionactivates AtoC by phosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential), SP has 3

TMHMM gives 15-37 192-211
SP gives 16-36 190-210 584-604
mhymkwiypr rlrnQMILMA ILMVIVPTLT IGYIVETegr savlsekekk
lsavvnllnq algdrydlyi dlpreerira lnaelapite nithafpgig
agyynkmlda iityapsaly qnnvgvtiaa dhpgrevmrt ntplvysgrq
vrgdilnsml pierngeilg yiwanelted irrqawkmdv rIIIVLTAGL 200
LISLLLIVLF Srrlsanidi itdglstlaq niptrlpqlp gemgqisqsv
nnlaqalret rtlndliien aadgviaidr qgdvttmnpa aevitgyqrh
elvgqpysml fdntqfyspv ldtlehgteh valeisfpgr drtielsvtt
srihnthgem igalvifsdl tarketqrrm aqaerlatlg elmagvahev 400
rnpltairgy vqilrqqtsd pihqeylsvv lkeidsinkv iqqllefsrp
rhsqwqqvsl nalveetlvl vqtagvqarv dfiseldnel spinadrell
kqvllnilin avqaisargk iriqtwqysd sqqaisiedn gcgidlslqk
kifdpffttk asgtglglal sqriinahqg dirvaslpgy gatftlilpi 600
npqgnqtv

MW67789 Da; 608 aa


Sensor Protein BaeS (baeS )
function 
interactionmay activate BaeR by phosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 13-35 168-190
SP gives 12-32 168-186
mkfwrpgitg klFLAIFATC IVLLISMHWA VRISFergfi dyikhgneqr
lqllsdalge qyaqhgnwrf lrnndrfvfq ilrsfehdns edkpgpgmpp
hgwrtqfwvv dqnnkvlvgp rapippdgtr rpilvngaev gaviaspver
ltrntdinfd kqqrqtsWLI VALATLLAAL ATFLLARGLL apvkrlvdgt 200
hklaagdftt rvtptsedel gklaqdfnql astleknqqm rrdfmadish
elrtplavlr geleaiqdgv rkftpetvas lqaevgtltk lvddlhqlsm
sdegalayqk apvdliplle vaggafrerf asrglklqfs lpdsitvfgd
rdrlmqlfnn llenslrytd sggslqisag qrdktvrltf adsapgvsdd 400
qlqklferfy rtegsrnras ggsglglaic lniveahngr iiaahspfgg
vsitvelple rdlqrev

MW51991 Da; 467 aa


Sensor protein BarA (barA )
function 
interactioncould activate OmpR by phosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 10-32 177-199
SP gives 10-31 177-196

mtnyslrarM MILILAPTVL IGLLLSIFFV VHryndlqrq ledagasiie
plavsteygm slqnresigq lisvlhrrhs divraisvyd ennrlfvtsn
fhldpssmql gsnvpfprql tvtrdgdimi lrtpiisesy spdespssda
knsqnmlgyi aleldlksvr lqqykeIFIS SVMMLFCIGI ALIFGWRLMr 200
dvtgpirnmv ntvdrirrgq ldsrvegfml geldmlkngi nsmamslaay
heemqhnidq atsdlretle qmeiqnveld lakkraqeaa rikseflanm
shelrtplng vigftrltlk teltptqrdh lntiersann llaiindvld
fskleagkli lesipfplrs tldevvtlla hsshdkglel tlniksdvpd 400
nvigdplrlq qiitnlvgna ikftengnid ilvekralsn tkvqievqir
dtgigiperd qsrlfqafrq adasisrrhg gtglglvitq klvnemggdi
sfhsqpnrgs tfwfhinldl npniiiegps tqclagkrla yvepnsaaaq
ctldilsetp levvysptfs alppahydmm llgiavtfre pltmqherla 600
kavsmtdflm lalpchaqvn aeklkqdgig acllkpltpt rllpaltefc
hhkqntllpv tdesklamtv mavddnpanl kligalledm vqhvelcdsg
hqaverakqm pfdlilmdiq mpdmdgirac elihqlphqq qtpviavtah
amagqkekll gagmsdylak pieeerlhnl llrykpgsgi ssrvvtpevn 800
eivvnpnatl dwqlalrqaa gktdlardml qmlldflpev rnkveeqlvg
enpeglvdli hklhgscgys gvprmknlcq lieqqlrsgt keedlepell
elldemdnva reaskilg

MW102453 Da; 918 aa


Sensor protein BasS (basS )
function 
interactionmay activate BasR by phosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 15-34 66-88
SP gives 14-34 65-88

mhflrrpisl rqrlILTIGA ILLVFELISV FWLWhesteq iqlfeqalrd
nrnndrhimr eireaVASLI VPGVFMVSLT LFICYQAVrr itrplaelqk
eleartadnl tpiaihsatl eieavvsaln dlvsrltstl dnerlftadv
ahelrtplag vrlhlellak thhidvaplv arldqmmesv sqllqlarag 200
qsfssgnyqh vklledvilp sydelstmld qrqqtlllpe saaditvqgd
atllrmllrn lvenahrysp qgsnimiklq eddgavmave degpgidesk
cgelskafvr mdsryggigl glsivsritq lhhgqfflqn rqetsgtraw
vrlkkdqyva nqi

MW41029 Da; 363 aa


Sensor kinase CitA (citA )
functionessential for expression citrate specific fermentation genes
interactionmay activate CitB by phosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 20-42 180-202
SP gives 22-42 183-203

mlqlnenkqf affqrlafpl rIFLLILVFS IFVIAALAQY FTasfedylt
lhvrdmamnq akiiasndsv isavktrdyk rlatianklq rdtdfdyvvi
gdrhsirlyh pnpekigypm qftkqgalek gesyfitgkg smgmamrakt
pifdddgkvi gvvsigylvs kidswraeFL LPMAGVFVVL LGILMLLSWF 200
Laahirrqmm gmepkqiarv vrqqealfss vyegliavdp hgyitainrn
arkmlglssp grqwlgkpiv evvrpadfft eqidekrqdv vanfnglsvi
anreairsgd dllgaiisfr skdeistlna qltqikqyve slrtlrhehl
nwmstlngll qmkeydrvla mvqgesqaqq qlidslreaf adrqvagllf 400
gkvqrarelg lkmiivpgsq lsqlppglds tefaaivgnl ldnafeaslr
sdegnkivel flsdegddvv ievadqgcgv peslrdkife qgvstradep
gehgiglyli asyvtrcggv itledndpcg tlfsiyipkv kpndssinpi
dr

MW61684 Da; 552 aa


Sensor protein CpxA (cpxA )
functioninvolved in unfolded stress response
interactionactivates CpxR by phosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 5-27 165-187
SP gives 9-27 165-187

migsLTARIF AIFWLTLALV LMLVLMLpkl dsrqmtelld seqrqglmie
qhveaeland ppndlmwwrr lfraidkwap pgqrlllvtt egrvigaers
emqiirnfig qadnadhpqk kkygrvelvg pfsvrdgedn yqlylirpas
ssqsdfinll fdrpLLLLIV TMLVSTPLLL WLAWSLAkpa rklknaadev 200
aqgnlrqhpe leagpqefla agasfnqmvt alermmtsqq rllsdishel
rtpltrlqlg tallrrrsge skeleriete aqrldsmind llvmsrnqqk
nalvsetika nqlwsevldn aafeaeqmgk sltvnfppgp wplygnpnal
esalenivrn alryshtkie vgfavdkdgi titvdddgpg vspedreqif 400
rpfyrtdear dresggtglg laivetaiqq hrgwvkaeds plgglrlviw
lplykrs

MW51624 Da; 457 aa


Sensor protein CreC (creC )
functioninvolved in catabolite regulation
interactionphosphorylates CreB in response to environmental signals, is able to phosphorylate PhoB
cofactors 
regulation 
topologytransmembrane domains: 2 (potential), SP has 3

TMHMM gives 5-27 184-206
SP gives 7-27 147-167 184-204

mrigMRLLLG YFLLVAVAAW FVLAIFVkev kpgvrrateg tlidtatlla
elarpdllsg dpthgqlaqa fnqlqhppfr anigginkvr neyhvymtda
qgkvlfdsan kavgqdysrw ndvwltlrgq ygarstlqnp adpessvmyv
aapimdgsrl igvlsvgkpn aamapvikrs errILWASAI LLGIALVIGA 200
GMVWWInrsi arltryadsv tdnkpvplpd lgsselrkla qalesmrvkl
egknyieqyv yalthelksp laairgaaei lregpppevv arftdniltq
narmqalvet llrqarlenr qevvltavdv aalfrrvsea rtvqlaekki
tlhvtptevn vaaepalleq algnlldnai dftpesgcit lsaevdqehv 400
tlkvldtgsg ipdyalsrif erfyslpran gqkssglgla fvsevarlfn
gevtlrnvqe ggvlaslrlh rhft

MW52117 Da; 474 aa


Sensor protein DcuS (dcuS/yjdH )
functionMember of the two-component regulatory system DcuR/DcuS. Expected to activate DcuR by phosphorylation.
Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; dcuC; sdhCDAB).
interaction 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 20-42 183-205
SP gives 21-41 182-202

mrhslpyrml rkrpmklstT VILMVSAVLF SVLLVVHLIY FSqisdmtrd
glankalava rtladspeir qglqkkpqes giqaiaeavr krndllfivv
tdmqslrysh peaqrigqpf kgddilkaln geenvainrg flaqalrvft
piydenhkqi gvvaiglels rvtqqindsr wsIIWSVLFG MLVGLIGTCI 200
LVKVLkkilf glepyeistl feqrqamlqs ikegvvavdd rgevtlinda
aqellnyrks qddeklstls hswsqvvdvs evlrdgtprr deeitikdrl
llintvpvrs ngviigaist frdktevrkl mqrldglvny adalrershe
fmnklhvilg llhlksykql edyilktann yqeeigsllg kikspviagf 400
liskinratd lghtlilnse sqlpdsgsed qvatlittlg nlienaleal
gpepggeisv tlhyrhgwlh cevnddgpgi apdkidhifd kgvstkgser
gvglalvkqq venlggsiav esepgiftqf fvqipwdger snr

MW60550 Da; 543 aa


Osmolarity sensor protein EnvZ (envZ )
functioninvolved in regulation of osmoregulation (ompF, ompC)
interactionphosphorylates OmpR in response to environmental signals
cofactors 
regulation 
topology3d structurePDB

transmembrane domains: 2 (potential)

TMHMM gives 15-37 160-179
SP gives 16-35 162-182

mrrlrfsprs sfarTLLLIV TLLFASLVTT YLVVLNFail pslqqfnkvl
ayevrmlmtd klqledgtql vvppafrrei yrelgislys neaaeeaglr
waqhyeflsh qmaqqlggpt evrvevnkss pvvwlktwls pniwvrvplt
eihqgdfspL FRYTLAIMLL AIGGAWLFIr iqnrplvdle haalqvgkgi 200
ippplreyga sevrsvtraf nhmaagvkql addrtllmag vshdlrtplt
rirlatemms eqdgylaesi nkdieecnai ieqfidylrt gqempmemad
lnavlgevia aesgyereie talypgsiev kmhplsikra vanmvvnaar
ygngwikvss gtepnrawfq veddgpgiap eqrkhlfqpf vrgdsartis 400
gtglglaivq rivdnhngml elgtserggl sirawlpvpv traqgttkeg

MW50334 Da; 450 aa


Putative sensor protein EvgS precursor (evgS )
function 
interactionphosphorylates EvgA in response to environmental signals
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 0
SP gives 379-394 536-552

mkFLPYIFLL CCGLWSTISF Adedyieyrg issnnrvtld plrlsnkelr
wlaskknlvi avhksqtatl lhtdsqqrvr ginadylnll kralnikltl
reyadhqkam dalaegevdi vlshlvtspp lnndiaatkp liitfpalvt
tlhdsmrplt spkpvniarv anyppdevih qsfpkatiis ftnlyqalas 200
vsaghndyfi gsniitssmi sryfthslnv vkyynsprqy nffltrkesv
ilnevlnrfv daltnevrye vsqnwldtgn laflnkplel tehekqwikq
hpnlkvlenp ysppysmtde ngsvrgvmgd ilniitlqtg lnfspitvsh
nihagtqlsp ggwdiipgai ysedrennvl faeafittpy vfvmqkapds 400
eqtlkkgmkv aipyyyelhs qlkemypeve wiqvdnasaa fhkvkegeld
alvatqlnsr ymidhyypne LYHFLIPGVP NASLSFAFpr gepelkdiin
kalnaippse vlrltekwik mpnvtidtwd lyseqfyivt tlsvllvgss
llwgfyllrs vrrrkviqgd lenqisfrka lsdslpnpty vvnwqgnvis 600
hnsafehyft adyyknamlp lensdspfkd vfsnahevta etkenrtiyt
qvfeidngie krcinhwhtl cnlpasdnav yicgwqdite trdlinalev
eknkaikatv aksqflatms heirtpissi mgflellsgs glskeqrvea
islayatgqs llgligeild vdkiesgnyq lqpqwvdipt lvqntchsfg 800
aiaasksial scsstfpehy lvkidpqafk qvlsnllsna lkfttegavk
ittslghidd nhavikmtim dsgsglsqee qqqlfkrysq tsagrqqtgs
glglmickel iknmqgdlsl eshpgigttf titipveisq qvatveakae
qpitlpekls iliaddhptn rlllkrqlnl lgydvdeatd gvqalhkvsm 1000
qhydllitdv nmpnmdgfel trklreqnss lpiwgltana qanerekgls
cgmnlclfkp ltldvlkthl sqlhqvahia pqyrhldiea lknntandlq
lmqeilmtfq hethkdlpaa fqaleagdnr tfhqcihrih gaanilnlqk
linishqlei tpvsddskpe ilqllnsvke hiaeldqeia vfcqknd

MW134742 Da; 1197 aa


Sensor protein HydH (hydH )
functioninvolved in regulation of the labile hydrogenase activity
interactionphosphorylates HydG in response to environmental signals
cofactors 
regulation 
topologytransmembrane domains: 2 (potential), SP has 5

TMHMM gives 10-32 200-222
SP gives 15-35 84-104 202-222 360-380 407-427

mrfmqrskdS LAKWLSAILP VVIVGLVGLF AVtvirdygr aseadrqall
ekgnvliral esgsrvgmgm rmhhvqqqal leemagqpgv lwfavtdaqg
iiilhsdpdk vgralyspde mqklkpeens rwrllgktet tpalevyrlf
qpmsapwrhg mhnmprcngk avpqvdaqqa ifiavdasdl vatqsgekrN 200
TLIILFALAT VLLASVLSFF WYrrylrsrq llqdemkrke klvalghlaa
gvaheirnpl ssikglakyf aerapaggea hqlaqvmake adrlnrvvse
llelvkpthl alqavdlntl inhslqlvsq dansreiqlr ftandtlpei
qadpdrltqv llnlylnaiq aigqhgvisv tasesgagvk isvtdsgkgi 400
aadqldaift pyfttkaegt glglavvhni veqhggtiqv asqegkgstf
tlwlpvnitr kdpqg

MW51031 Da; 465 aa


Sensor protein KdpD (kdpD )
functioninvolved in regulation of the kdp operon
interactionphosphorylates KdpE in respose to environmental signals
cofactors 
regulation 
topologytransmembrane domains: 4 (potential), SP has 5

TMHMM gives 399-421 425-444 449-471 476-498
SP gives 25-45 403-423 424-444 446-466 478-498

mnneplrpdp drlleqtaap hrgklkvffg acagvgktwa mlaeaqrlra
qgldivvgvv ethgrkdtaa mleglavlpl krqayrgrhi sefdldaala
rrpalilmde lahsnapgsr hpkrwqdiee lleagidvft tvnvqhlesl
ndvvsgvtgi qvretvpdpf fdaaddvvlv dlppddlrqr lkegkvyiag 200
qaeraiehff rkgnlialre lalrrtadrv deqmrawrgh pgeekvwhtr
daillcighn tgseklvraa arlasrlgsv whavyvetpa lhrlpekkrr
ailsalrlaq elgaetatls dpaeekavvr yarehnlgki ilgrpasrrw
wrretfadrl ariapdldqv lvaldeppar tinnapdnrs fkdkwrvqIQ 400
GCVVAAALCA VITLIAMQWL MafdAANLVM LYLLGVVVVA LFYGrwpsVV
ATVINVVSFD LFFIAPRGTL AvsdvQYLLT FAVMLTVGLV IGNLTAGVry
qarvaryreq rtrhlyemsk alavgrspqd iaatseqfia stfharsqvl
lpddngklqp lthpqgmtpw ddaiaqwsfd kglpagagtd tlpgvpyqil 600
plksgektyg lvvvepgnlr qlmipeqqrl letftllvan alerltltas
eeqarmaser eqirnallaa lshdlrtplt vlfgqaeilt ldlasegsph
arqaseirqh vlnttrlvnn lldmariqsg gfnlkkewlt leevvgsalq
mlepglsspi nlslpepltl ihvdgplfer vlinllenav kyagaqaeig 800
idahvegenl qldvwdngpg lppgqeqtif dkfargnkes avpgvglgla
icraivdvhg gtitafnrpe ggacfrvtlp qqtapeleef hedm

MW98718 Da; 894 aa


Nitrat/nitrite sensor protein NarQ (narQ )
functionsensor for nitrate/nitrite availability
interactionprobably activates NarL and NarP by phosphorylation and negatively regulates NarL by dephosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 15-37 147-169
SP gives 14-34 147-167

mivkrpvsas laraFFYIVL LSILSTGIAL LTLASSLrda eainiagslr
mqsyrlgydl qsgspqlnah rqlfqqalhs pvltnlnvwy vpeavktrya
hlnanwlemn nrlskgdlpw yqaninnyvn qidlfvlalq hyaerkMLLV
VAISLAGGIG IFTLVFFTLr rirhqvvapl nqlvtasqri ehgqfdsppl 200
dtnlpnelgl laktfnqmss elhklyrsle asveektrdl heakrrlevl
yqcsqalnts qidvhcfrhi lqivrdneaa eylelnvgen wrisegqpnp
elpmqilpvt mqetvygelh wqnshvssse pllnsvssml grglyfnqaq
khfqqlllme eratiarelh dslaqvlsyl riqltllkrs ipednataqs 400
imadfsqaln dayrqlrell ttfrltlqqa dlpsalreml dtlqnqtsak
ltldcrlptl aldaqmqvhl lqiireavln amkhanasei avscvtapdg
nhtvyirdng igigepkepe ghyglnimre raerlggtlt fsqpsgggtl
vsisfrsaeg eesqlm

MW63696 Da; 566 aa


Nitrate/nitrite sensor protein NarX (narX )
functionsensor for nitrate/nitrite availability, transduction of nitrate availability to NarL and of nitrate/nitrite avaliability to NarP
interactionactivates NarL and NarP by phosphorylateion in the presence of nitrate, probably inactivates NarL by dephosphorylation in the absence of nitrate
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 15-37 152-174
SP gives 15-37 152-174

mlkrclsplt lvnqVALIVL LSTAIGLAGM AVSGWLVqgv qgsahainka
gslrmqsyrl laavplsekd kplikemeqt afsaeltraa erdgqlaqlq
glqdywrnel ipalmraqnr etvsadvsqf vagldqlvsg fdrttemrie
tVVLVHRVMA VFMALLLVFT IIWLrarllq pwrqllamas avshrdftqr 200
anisgrnema mlgtalnnms aelaesyavl eqrvqektag lehknqilsf
lwqanrrlhs raplcerlsp vlnglqnltl lrdielrvyd tddeenhqef
tcqpdmtcdd kgcqlcprgv lpvgdrgttl kwrladshtq ygillatlpq
grhlshdqqq lvdtlveqlt atlaldrhqe rqqqlivmee ratiarelhd 400
siaqslscmk mqvsclqmqg dalpessrel lsqirnelna swaqlrellt
tfrlqltepg lrpaleasce eysakfgfpv kldyqlpprl vpshqaihll
qiarealsna lkhsqasevv vtvaqndnqv kltvqdngcg vpenairsnh
ygmiimrdra qslrgdcrvr rresggtevv vtfipektft dvqgdthe

MW67083 Da; 598 aa


Sensor protein PhoQ (phoQ )
functioninvolved in regulation of acid phosphatase
interactionphosphorylates PhoR in response to environmental signals
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 20-42 194-216
SP gives 17-44 189-216

mkkllrlffp lslrvrfllA TAAVVLVLSL AYGMVALIGY SVsfdkttfr
llrgesnlfy tlakwennkl hvelpenidk qsptmtliyd engqllwaqr
dvpwlmkmiq pdwlksngfh eieadvndts lllsgdhsiq qqlqevredd
ddaemthsva vnvypatsrm pkltivvvdt ipvelkssym vwsWFIYVLS 200
ANLLLVIPLL WVAAWWslrp iealakevre leehnrelln pattreltsl
vrnlnrllks ererydkyrt tltdlthslk tplavlqstl rslrsekmsv
sdaepvmleq isrisqqigy ylhrasmrgg tllsrelhpv aplldnltsa
lnkvyqrkgv nisldispei sfvgeqndfv evmgnvldna ckyclefvei 400
sarqtdehly ivveddgpgi plskrevifd rgqrvdtlrp gqgvglavar
eiteqyegki vagesmlgga rmevifgrqh sapkde

MW55299 Da; 486 aa


Phosphate regulon sensor protein PhoR (phoR )
functioninvolved in the phosphate regulon gene expression
interactionphosphorylates PhoB in response to environmental signals
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 12-34
SP gives 10-28 33-51

mlerlswkrL VLELLLCCLP AFILGAFFgy lpWFLLASVT GLLIWHFWNL
Lrlswwlwvd rsmtpppgrg swepllyglh qmqlrnkkrr relgnlikrf
rsgaeslpda vvltteeggi fwcnglaqqi lglrwpedng qnilnllryp
eftqylktrd fsrplnlvln tgrhleirvm pythkqllmv ardvtqmhql 200
egarrnffan vshelrtplt vlqgylemmn eqplegavre kalhtmreqt
qrmeglvkql ltlskieaap thllnekvdv pmmlrvvere aqtlsqkkqt
ftfeidnglk vsgnedqlrs aisnlvynav nhtpegthit vrwqrvphga
efsvedngpg iapehiprlt erfyrvdkar srqtggsglg laivkhavnh 400
hesrlniest vgkgtrfsfv iperliakns d

MW49629 Da; 431 aa


Sensor protein RcsC (rcsC )
functioninvolved in regulation of the expression of colanic acid synthesis
interactionprobabaly phosphorylates RcsB in response to environmental signals
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 20-42 315-334
SP gives 20-41 314-335

mkylasfrtt lkasry
mfrALALVLW LLIAFSSVFY IVNALHqres eirqefnlss dqaqrfiqrt
sdvmkelkyi aenrlsaeng vlsprgretq advpafeplf adsdcsamsn
twrgslesla wfigywrdnf saaydlnrvf ligsdnlcma nfglrdmpve
rdtalkalhe rinkyrnapq ddsgsnlywi segprpgvgy fyaltpvyla 216
nrlqallgve qtirmenffl pgtlpmgvti ldenghtlis ltgpeskikg
dprwmqersw fgytegfrel vlkknlppss lsivysvpvd kvlerirmLI
LNAILLNVLA GAALFTLArm yerrifipae sdalrleehe qfnrkivasa
pvgicilrta dgvnilsnel ahtylnmlth edrqrltqii cgqqvnfvdv 416
ltsnntnlqi sfvhsryrne nvaicvlvdv ssrvkmeesl qemaqaaeqa
sqsksmflat vshelrtply giignldllq tkelpkgvdr lvtamnnsss
lllkiisdil dfskieseql kieprefspr evmnhitany lplvvrkqlg
lycfiepdvp valngdpmrl qqvisnllsn aikftdtgci vlhvradgdy 616
lsirvrdtgv gipakevvrl fdpffqvgtg vqrnfqgtgl glaiceklis
mmdgdisvds epgmgsqftv riplygaqyp qkkgveglsg krcwlavrna
slcqfletsl qrsgivvtty egqeptpedv litdevvskk wqgravvtfc
rrhigiplek apgewvhsva aphelpalla riyliemesd dpanalpstd 816
kavsdnddmm ilvvddhpin rrlladqlgs lgyqcktand gvdalnvlsk
nhidivlsdv nmpnmdgyrl tqrirqlglt lpvigvtana laeekqrcle
sgmdsclskp vtldvikqtl tlyaervrks rds

MW106506 Da; 933 aa


Sensor protein RstB (rstB )
function 
interactionphosphorylates RstA
cofactors 
regulation 
topologytransmembrane domains: 2 (potential), SP has 3

TMHMM gives 5-27 139-156
SP gives 4-24 136-156 385-405

mkklFIQFYL LLFVCFLVMS LLVGLVYkft aeragkqsld dlmnsslylm
rselreipph dwgktlkemd lnlsfdlrve plskyhlddi smhrlrggei
valddqytfl qriprshyvl avgpvpylyy lhqmrlldIA LIAFIAISLA
FPVFIWmrph wqdmlkleaa aqrfgdghln erihfdegss ferlgvafnq 200
madninalia skkqlidgia helrtplvrl ryrlemsdnl saaesqalnr
disqlealie elltyarldr pqnelhlsep dlplwlsthl adiqavtpdk
tvriktlvqg hyaaldmrlm ervldnllnn alrychstve tslllsgnra
tliveddgpg iapenrehif epfvrldpsr drstggcglg laivhsiala 400
mggtvncdts elggarfsfs wplwhnipqf tsa

MW49282 Da; 433 aa


Sensor protein TorS (torS )
function 
interactionprobabaly activates TorR by phosphorylation
cofactors 
regulation 
topologytransmembrane domains: 2 (potential), SP has 1

TMHMM gives 14-31 331-353
SP gives 333-353

mnltltrrlw
mgfALMALLT LTSTLVGWYN Lrfisqvekd ntqaliptmn marqlseasa
welfaaqnlt sadnekmwqa qgrmltaqsl kinallqalr eqgfdttaie
qqeqeisrsl rqqgelvgqr lqlrqqqqql sqqivaaade iarlaqgqan
nattsagatq agiydlieqd qrqaaesald rlididleyv nqmnelrlsa 210
lrvqqmvmnl gleqiqknap tlekqlnnav kilqrrqiri edpgvraqva
ttlttvsqys dllalyqqds eisnhlqtla qnniaqfaqf ssevsqlvdt
ielrnqhgla hlekasargq YSLLLLGMVS LCALILILWR VVYrsvtrpl
aeqtqalqrl ldgdidspfp etagvreldt igrlmdafrs nvhalnrhre 410
qlaaqvkart aelqelvieh rqaraeaeka sqaksaflaa msheirtply
gilgtaqlla dnpalnaqrd dlraitdsge slltilndil dysaieaggk
nvsvsdepfe prpllestlq lmsgrvkgrp irlataiadd mpcalmgdpr
rirqvitnll snalrftdeg yiilrsrtdg eqwlveveds gcgidpakla 610
eifqpfvqvs gkrggtglgl tissrlaqam ggelsatstp evgscfclrl
plrvatapvp ktvnqavrld glrllliedn pltqritiem lktsgaqiva
vgnaaqalet lqnsepfaaa lvdfdlpdid gitlarqlaq qypslvligf
sahvidetlr qrtsslfrgi ipkpvprevl gqllahylql qvnndqsldv 810
sqlnedaqlm gtekihewlv lftqhalpll deidiarasq dsekikraah
qlksscsslg mhiasqlcaq leqqplsapl pheeitrsva aleawlhkkd
lnai

MW101024 Da; 914 aa


Sensor protein UhpB (uhpB )
functioninvolved in the regulation of the uptake of hexose phosphates
interactionphosphorylates UhpA in response to environmental signals
cofactors 
regulation 
topologytransmembrane domains: 8 (potential), TMHMM has 7

TMHMM gives 7-29 78-100 112-131 141-163 184-201 221-243 255-274
SP gives 8-27 37-56 78-100 141-162 185-204 210-228 230-248 255-273

mktlfsRLIT VIACFFIFSA AWFCLWSISl hlverpdMAV LLFPFGLRLG
LMLQCprgyw pvllgaewll iywltqaVGL THFPLLMIGS LLTLLPVALI
sryrhqrdwr tLLLQGAALT AAALLQSLPW Lwhgkeswna LLLTLTGGLT
LAPICLVFWH YLAnntwlpl gpslvsqpin wrgRHLVWYL LLFVISLWLQ 200
Lglpdelsrf tpfclalpii ALAWHYGWQG ALIATLMNAI ALIasqtwrd
hpvdLLLSLL VQSLTGLLLG AGIQrlreln qslqkelarn qhlaerllet
eesvrrdvar elhddigqti tairtqagiv qrlaadnasv kqsgqlieql
slgvydavrr llgrlrprql ddltleqair slmremeleg rgivshlewr 400
idesalsenq rvtlfrvcqe glnnivkhad asavtlqgwq qderlmlvie
ddgsglppgs gqqgfgltgm rervtalggt lhisclhgtr vsvslpqryv

MW56305 Da; 500 aa


Hydrolases Acting on Acid Anhydrides in Phosphorous-Containing Anhydrides

ATP synthase a chain (atpB )
functionkey component of the proton channel, may play a direct role in translocation of protons across the channel
interaction 
cofactors 
regulation 
topology3d structurePDB

transmembrane domains: 0

MW 50194 Da; 459 aa


ATP synthase c chain (atpE )
functionpart of the membrane proton channel (CF0) of F-type ATPase
interaction 
cofactors 
regulation 
topology3-d structurePDB

transmembrane domains: 0

MW14937 Da; 138 aa


ATP synthase b chain (atpF )
functionpart of the membrane proton channel (CF0) of F-type ATPase
interaction 
cofactors 
regulation 
topology3-d structurePDB

transmembrane domains: 1 (potential)

TMHMM gives 5-27
SP gives 11-31

mnlnATILGQ AIAFVLFVLF CMKYVWPplm aaiekrqkei adglasaera
hkdldlakas atdqlkkaka eaqviieqan krrsqildea kaeaeqertk
ivaqaqaeie aerkrareel rkqvailava gaekiiersv deaansdivd
klvael

MW17264 Da; 156 aa


Potassium transporting ATPase A chain (kdpA )
functionone of the components of the high affinity repressible ATP-driven potassium-transport system
interaction 
cofactors 
regulation 
topologytransmembrane domains: 12 (potential)

TMHMM gives 5-24 62-84 130-152 173-195 253-275 282-304 327-349 354-376 380-399 416-438 483-505 526-548
SP gives 6-26 63-83 132-152 170-190 253-273 283-303 329-349 356-376 379-399 416-436 484-504 527-547

maaqgFLLIA TFLLVLMVLA RPLGSGLarl indiplpgtt gvervlfral
gvsdremnwk qYLCAILGLN MLGLAVLFFM LLGQQQNfls aasgiavifa
liraftrqsm stlgnawvdl lrITLWVLVP VALLIALFFI QQGALqnflp 200
yqavntvega qqllpmgpva sqeaikmlgt ngggffnans shpfenptal
tnFVQMLAIF LIPTALCFAF GEVMGdrrqg rMLLWAMSVI FVICVGVVMW
AEVqgnphll algtdssinm egkesrFGVL VSSLFAVVTT AASCGAVIAm
hdsFTALGGM VPMWLMQIGE VVFGGVgsgL YGMMLFVLLA VFIAGLMIGr 400
tpeylgkkid vremkLTALA ILVTPTLVLM GAALAMMTda grsamlnpgp
hgfsevlyav ssaannngsa faglsanspf wnCLLAFCMF VGRFGVIIPV
MAIAGslvsk ksqaassgtl pthgpLFVGL LIGTVLLVGA LTFIPALALg
pvaeyls

MW59189 Da; 557 aa


Potassium transporting ATPase B chain (kdpB )
functionone of the components of the high affinity repressible ATP-driven potassium-transport system
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential), SP has 6

TMHMM gives 36-58 63-85 220-242 252-274 578-600 615-634 654-676
SP gives 35-54 62-82 219-240 252-271 616-636 662-682

msrkqlalfe ptlvvqalke avkklnpqaq wrnpvMFIVW IGSLLTTCIS
IAMASGAMpg naLFSAAISG WLWITVLFAN FAealaegrs kaqanslkgv
kktafarklr epkygaaadk vpadqlrkgd ivlveagdii pcdgeviegg
asvdesaitg esapviresg gdfasvtggt rilsdwlvie csvnpgetfl 200
drmiamvega qrrktpneIA LTILLIALTI VFLLATATLW PFsawggnav
sVTVLVALLV CLIPTTIGGL LSAIgvagms rmlganviat sgraveaagd
vdvllldktg titlgnrqas efipaqgvde ktladaaqla sladetpegr
sivilakqrf nlrerdvqsl hatfvpftaq srmsginidn rmirkgsvda 400
irrhveangg hfptdvdqkv dqvarqgatp lvvvegsrvl gvialkdivk
ggikerfaql rkmgiktvmi tgdnrltaaa iaaeagvddf laeatpeakl
alirqyqaeg rlvamtgdgt ndapalaqad vavamnsgtq aakeagnmvd
ldsnptklie vvhigkqmlm trgslttFSI ANDVAKYFAI IPAAFAATYP 600
qlnalnimcl hspdSAILSA VIFNALIIVF LIPLalkgvs ykpltasaml
rrnLWIYGLG GLLVPFIGIK VIDLLLtvcg lv

MW72199 Da; 682 aa


Potassium transporting ATPase C chain (kdpC )
functionone of the components of the high affinity repressible ATP-driven potassium-transport system
interaction 
cofactors 
regulation 
topologytransmembrane domains: 1 (potential)

TMHMM gives 12-34
SP gives 10-30

msglrpalst FIFLLLITGG VYPLLTTVLG QWWFpwqang sliregdtvr
gsaligqnft gngyfhgrps ataempynpq asggsnlavs npeldkliaa
rvaalraanp dasasvpvel vtasasgldn nitpqaaawq iprvakarnl
sveqltqlia kysqqplvky igqpvvnive lnlaldklde

MW20267 Da; 190 aa


Mg2+ transport ATPase, P-type1 (mgtA )
functionmediates magnesium influx to the cytosol
Belongs to the cation transport ATPases family (E1-E2 ATPases), Subfamily IIIB
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential), SP has 10

TMHMM gives 118-137 291-310 320-342 710-732 769-791 832-854 869-891
SP gives 91-111 118-138 287-307 318-338 679-720 724-744 765-785 800-818 836-854 868-887

mfkeiftrli rhlpsrlvhr dplpgaqqtv ntvvppslsa hclkmavmpe
eelwktfdth peglnqaeve sareqhgenk lpaqqpspww vhlwvcyrnp
fnilltilga isyatedLFA AGVIALMVAI STLLNFIqea rstkaadalk
amvsntatvl rvindkgeng wleipidqlv pgdiiklaag dmipadlril 200
qardlfvaqa sltgeslpve kaattrqpeh snplecdtlc fmgttvvsgt
aqamviatga ntwfgqlagr vseqesepna fqqgisrvsm LLIRFMLVMA
PVVLLINGYT kgdwweaalF ALSVAVGLTP EMLPMIVTST LArgavklsk
qkvivkhlda iqnfgamdil ctdktgtltq dkivlenhtd isgktservl 400
hsawlnshyq tglknlldta vlegtdeesa rslasrwqki deipfdferr
rmsvvvaent ehhqlvckga lqeilnvcsq vrhngeivpl ddimlrkikr
vtdtlnrqgl rvvavatkyl paregdyqra desdlilegy iafldppket
tapalkalka sgitvkiltg dselvaakvc hevgldagev vigsdietls 600
ddelanlaqr ttlfarltpm hkerivtllk reghvvgfmg dgindapalr
aadigisvdg avdiareaad iillekslmv leegviegrr tfanmlkyik
mtassnfgnV FSVLVASAFL PFLPMLPLHL LIqnllydvs qvaipfdnvd
deqiqkpqrw npadlgrFMI FFGPISSIFD ILTFCLMWWV Fhantpetqt 800
lfqsgwfvvg llsqtlivhm irtrrvpfiq sCASWPLMIM TVIVMIVGIA
LPFSplasyl qlqalplsYF PWLVAILAGY MTLTQLVkgf ysrrygwq

MW99466 Da; 898 aa


Probable copper-transporting ATPase (ybaR )
functioninvolved in copper transport
Belongs to the cation transport ATPases family (E1-E2 ATPases), Subfamily IB
interaction 
cofactors 
regulation 
topologytransmembrane domains: 8 (potential), SP has 11

TMHMM gives 189-206 216-238 245-267 282-299 436-458 463-485 778-797 802-824
SP gives 187-207 218-238 254-274 284-304 438-458 464-484 485-505 627-647 733-753 779-799 801-821

msqtidltld glscghcvkr vkesleqrpd veqadvsite ahvtgtasae
qlietikqag ydasvshpka kplaessips ealtavseal paatadddds
qqlllsgmsc ascvtrvqna lqsvpgvtqa rvnlaertal vmgsaspqdl
vqavekagyg aeaieddakr rerqqetava tmkrfrwqAI VALAVGIPVM 200
VWGMIGdnmm vtadnrSLWL VIGLITLAVM VFAGGHFYrs awksLLNGAA
TMDTLVALGT GVAWLYSmsv nlwpqwfpme arhLYYEASA MIIGLINLGH
MLeararqrs skaleklldl tpptarlvtd egeksvplae vqpgmllrlt
tgdrvpvdge itqgeawlde amltgepipq qkgegdsvha gtvvqdgsvl 400
frasavgsht tlsriirmvr qaqsskpeig qladkISAVF VPVVVVIALV
SAAIWYFFgp apqIVYTLVI ATTVLIIACP CALGLatpms iisgvgraae
fgvlvrdada lqrastldtv vfdktgtlte gkpqvvavkt fadvdeaqal
rlaaaleqgs shplaraild kagdmqlpqv ngfrtlrglg vsgeaeghal 600
llgnqallne qqvgtkaiea eitaqasqga tpvllavdgk avallavrdp
lrsdsvaalq rlhkagyrlv mltgdnptta naiakeagid eviagvlpdg
kaeaikhlqs egrqvamvgd gindapalaq advgiamggg sdvaietaai
tlmrhslmgv adalaisrat lhnmkqnLLG AFIYNSIGIP VAAGILWpft 800
gTLLNPVVAG AAMALSSITV VSNAnrllrf kpke

MW87873 Da; 834 aa