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ecce/ proteins of the inner membrane/ iron and peptide transport
Peptide Transport

Iron Transport

IronIII dicitrate transport system permease protein FecC (fecC )
functionpart of the binding-protein dependent transport system for citrate-dependent ironIII, pobably responsible for the translocation of the substrate across the membrane
interaction 
regulation 
 transmembrane domains: 8 (potential)

TMHMM gives 7-29 59-81 94-116 121-143 152-174 198-220 241-263 306-328
SP gives 8-28 65-85 119-139 153-173 200-220 245-265 281-301 308-328

mtaikhpVLL WGLPVAALII IFWLSLFCYs aipvsgadat rallpghtpt
lpealvqnlr lprSLVAVLI GASLALAGTL LQTLthnpma spsLLGINSG
AALAMALTSA LSPTPIagys LSFIAACGGG VSWLLVMTAG GGFrhthdrn
kLILAGIALS AFCMGLTRIT LLLAedhayg ifywlaggvs harwqdVWQL 200
LPVVVTAVPV VLLLANQLNL Lnlsdstaht lgvnltrlrL VINMLVLLLV
GACVSVAGPV AFIgllvphl arfwagfdqr nvlpvsmllg atlmlladvl
aralaFPGDL PAGAVLALIG SPCFVWLVrr rg

MW34892 Da; 332 aa


IronIII dicitrate transport system permease protein FecD (fecD )
functionpart of the binding-protein dependent transport system for citrate-dependent ironIII, pobably responsible for the translocation of the substrate across the membrane
interaction 
regulation 
 transmembrane domains: 8 (potential), TMHMM has 7, SP has 9

TMHMM gives 4-26 55-77 108-130 180-202 226-248 268-290 296-315
SP gives 3-23 56-76 85-105 106-126 138-158 180-200 226-246 270-290 295-315

mkiALVIFIT LALAGCALLS LHMGVIpvpw ralltdwqag hehyyvlmey
rlprLLLALF VGAALAVAGV LIQGIVrnpl aspdILGVNH AASLASVGAL
LLMpslpVMV LPLLAFAGGM AGLILLKMLA kthqpmklal tgvalsacwa
sltdylmlsr pqdvnnallw ltgslwgrdW SFVKIAIPLM ILFLPLSLSF 200
Crdldllalg darattlgvs vphtrFWALL LAVAMTSTGV AACGPISFig
lvvphmmrsi tggrhrrLLP VSALTGALLL VVADLLARII hppleLPVGV
LTAIIGAPWF VWLLVrmr

MW34131 Da; 318 aa


Ferrous iron transport protein B (feoB )
functionprobable GTP driven transporter of ferrous iron
interaction 
regulation 
 transmembrane domains: 10 (potential), SP has 13

TMHMM gives 277-299 309-331 344-366 386-408 421-443 453-475 510-532 663-685 692-714 720-742
SP gives 102-122 282-302 309-329 334-354 383-403 427-447 453-473 482-502 518-538 568-588 664-684 691-711 722-742

mkkltiglig npnsgkttlf nqltgsrqrv gnwagvtver kegqfsttdh
qvtlvdlpgt yslttissqt sldeqiachy ilsgdadlli nvvdasnler
nlyltlqlle lgipcivaln mldiaekqni rieidalsar lgcpviplvs
trgrgiealk laidrykane nvelvhyaqp llneadslak vmpsdiplkq 200
rrwlglqmle gdiysrayag easqhldaal arlrnemddp alhiadaryq
ciaaicdvvs ntltaepsrf ttavdkIVLN RFLGLPIFLF VMYLMFLLAi
niggalqpLF DVGSVALFVH GIQWIGYTLH Fpdwltifla qglGGGINTV
LPLVPQIGMM YLFLSFleds gymaraafvm drlmqALGLP GKSFVPLIVG 400
FGCNVPSVmg artldaprer LMTIMMAPFM SCGARLAIFA VFAaaffgqn
gaLAVFSLYM LGIVMAVLTG LMLkytimrg eatpfvmelp vyhvphvksl
iiqtwqrlkG FVLRAGKVII IVSIFLSAFN SFslsgkivd nindsalasv
srvitpvfkp igvhednwqa tvglftgama kevvvgtlnt lytaeniqde 600
efnpaefnlg eelfsaidet wqslkdtfsl svlmnpieas kgdgemgtga
mgvmdqkfgs aaAAYSYLIF VLLYVPCISV MGAIAressr gWMGFSILWG
LNIAYSLATL FYQVasysqh PTYSLVCILA VILFNIVVIG LLrrarsrvd
iellatrksv ssccaasttg dch

MW84473 Da; 773 aa


Ferric enterobactin transport protein FepD (fepD )
functionpart of the binding-protein dependent transport system for ferric enterobactin, pobably responsible for the translocation of the substrate across the membrane
interaction 
regulationcontrolled in part by the amount of available iron
 transmembrane domains: 9 (potential)

TMHMM gives 10-32 65-84 94-116 121-140 150-172 193-215 240-262 282-304 308-326
SP gives 10-30 64-84 93-113 121-141 152-172 193-213 242-262 280-300 306-326

msgsvavtrA IAVPGLLLLL IIATALSLLI GAkslpasvv leafsgtcqs
adctivldar lprtLAGLLA GGALGLAGAL MQTLtrnpla dpgLLGVNAG
ASFAIVLGAA LFGYSSaqeq LAMAFAGALV ASLIVAFTGS qgggqlspvr
LTLAGVALAA VLEGLTSGIA LLnpdvydql rfwqagsldi rnLHTLKVVL 200
IPVLIAGATA LLLSralnsl slgsdtatal gsrvartqLI GLLAITVLCG
SATAIVGPIA FIglmmphma rwlvgadhrw sLPVTLLATP ALLLFADIIG
RVIVpgelrV SVVSAFIGAP VLIFLVrrkt rgga

MW33871 Da; 334 aa


Ferric enterobactin transport protein FepE (fepE/eepE )
functionpart of the ferric enterobactin transport system
interaction 
regulation 
 transmembrane domains: 2 (potential)

TMHMM gives 43-62 339-361
SP gives 42-62 339-359

msslnikqgs dahfpdypla spsnneidll nlisvlwrak ktVMAVVFAF
ACAGLLISFI Lpqkwtsaav vtppepvqwq eleksftklr vldldikidr
teafnlfikk fqsvslleey lrsspyvmdq lkeakideld lhraivalse
kmkavddnas kkkdepslyt swtlsftapt seeaqtvlsg yidyistlvv 200
keslenvrnk leiktqfeke klaqdriktk nqldaniqrl nysldianaa
gikkpvysng qavkddpdfs islgadgier kleiekavtd vaelngelrn
rqylveqltk ahvndvnftp fkyqlspslp vkkdgpgkAI IVILSALIGG
MVACGGVLLr yamasrkqda mmadhlv

MW42099 Da; 377 aa


Ferric enterobactin transporter protein FepG (fepG )
functionpart of the binding-protein dependent transport system for ferric enterobactin, pobably responsible for hte translocation of the substrate across the membrane
interaction 
regulationcontrolled in part by the amount of available iron
 transmembrane domains: 8 (potential), SP has 9

TMHMM gives 7-29 58-80 93-112 116-138 145-167 187-209 240-262 302-324
SP gives 8-28 63-83 93-113 118-138 147-167 191-211 236-256 276-296 304-324

miyvsrrLLI TCLLLVSACV VAGIWGLrsg avtletsqvf aalmgdaprs
mtmvvtewrl prVLMALLIG AALGVSGAIF QSLMrnplgs pdVMGFNTGA
WSGVLVAMVL FGqdLTAIAL SAMVGGIVTS LLVWLLAWrn gidtfrLIII
GIGVRAMLVA FNTWLLLkas letaltaglw nagslnGLTW AKTSPSAPII 200
ILMLIAAALL Vrrmrllemg ddtacalgvs versrLLMML VAVVLTAAAT
ALAGPISFIA LVaphiarri sgtarWGLTQ AALCGALLLL AADLCaqqlf
mpYQLPVGVV TVSLGGIYLI VLLIqesrkk

MW34910 Da; 330 aa



Ferrichrome transporter FhuB (fhuB )
functionpart of the binding-protein dependent transport system (ABC transporter)
interaction 
regulation 
 transmembrane domains: 17 TM, SP has 18

TMHMM gives 7-29 57-79 92-111 115-137 144-166 239-261 273-291 301-323 347-369 389-411 424-442 446-468 480-499 525-547 568-590 605-624 631-653
SP gives 5-25 63-83 93-113 118-138 147-167 197-217 240-260 277-297 303-323 348-368 391-411 424-444 447-467 479-499 528-548 567-587 607-627 635-655

mskriaLFPA LLLALLVIVA TALTWMNFSq alprsqwaqa awspdidvie
qmifhySLLP RLAISLLVGA GLGLVGVLFq qvlrnplaep tTLGVATGAQ
LGITVTTLWA IpgaMASQFA AQAGACVVGL IVFGVAWgkr lspVTLILAG
LVVSLYCGAI NQLLVIfhhd qlqsmflwst gtltqtdwgg verlwpqllg 200
gvmltllllr pltlmglddg varnlglals larlaalsLA IVISALLVNA
VGIIGFIGLF Apllakmlga rrLLPRLMLA SLIGALILWL Sdqiilwltr
VWMEVSTGSV TALIGAPLLL WLLprlrsis apdmkvndrv aaerqhVLAF
ALAGGVLLLM AVVVALSFGr dahgwtwasg alledlmpWR WPRIMAALFA 400
GVMLAVAGCI Iqrltgnpma speVLGISSG AAFGVVLMLF LVpgnAFGWL
LPAGSLGAAV TLLIIMIAag rggfsphrmL LAGMALSTAF TMLLMMLQAs
gdprmaqvlt wisgstynat daqvWRTGIV MVILLAITPL CRRWLTIlpl
ggdtaravgm altptriALL LLAACLTATA TMTIGPLSFV glmaphiarm 600
mgfrRTMPHI VISALVGGLL LVFAdwcgrm VLFPFQIPAG LLSTFIGAPY
FIYllrkqsr

MW70422 Da; 660 aa



Peptide Transport

Dipeptide transport system permease protein DppB (dppB )
functionpart of the binding-protein-dependent transport system for dipeptides, probably responsible for the translocation of the substrate across the membrane
interaction 
regulation 
 transmembrane domains: 6 (potential), SP has 7

TMHMM gives 9-31 99-121 134-156 202-221 258-280 309-331
SP gives 10-30 103-123 136-156 172-192 201-221 260-280 311-331

mlqfilrrLG LVIPTFIGIT LLTFAFVHMI pgdpvmimag ergisperha
qllaelgldk pmwqqylhyi wgvmhgdlgi smksripvwe efvprfqaTL
ELGVCAMIFA TAVGIPVGVL Aavkrgsifd htaVGLALTG YSMPIFWWGM
MLIMLVsvhw nltpvsgrvs dmvflddsnp ltgfmlidta iwgedgnfid 200
aVAHMILPAI VLGTIPLAVI Vrmtrssmle vlgedyirta rakgltrmrv
iivhalrnAM LPVVTVIGLQ VGTLLAGAIL tetifswpgl grwlidalqr
rdypvvqgGV LLVATMIILV NLLVDLLYGV Vnprirhkk

MW37497 Da; 339 aa


Dipeptide transport system permease protein DppC (dppC )
functionpart of the binding-protein-dependent transport system for dipeptides, probably responsible for the translocation of the substrate across the membrane
interaction 
regulation 
 transmembrane domains: 5 (potential), SP has 6

TMHMM gives 31-53 103-125 140-162 210-232 265-287
SP gives 33-53 102-122 137-157 207-227 231-251 266-286

msqvtenkvi sapvpmtplq efwhyfkrnk GAVVGLVYVV IVLFIAIFAN
WIApynpaeq frdallappa wqeggsmahl lgtddvgrdv lsrlmygarl
sLLVGCLVVV LSLIMGVILG LIAGYFgglv dniimrvvdI MLALPSLLLA
LVLVAIFGPS IGnaalaltf valphyvrlt raavlvevnr dyvtasrvag 200
agamrqMFIN IFPNCLAPLI VQASLGFsna ildMAALGFL GMGAQPPTPE
WGTMLsdvlq faqsAWWVVT FPGLAILLTV LAFNLMGdgl rdaldpklkq

MW32308 Da; 300 aa


Oligopeptide transport system permease protein OppB (oppB )
functionpart of the binding-protein-dependent transport system for oligopeptides, probably responsible for the translocation of the substrate across the membrane
interaction 
regulation 
 transmembrane domains: 6 (potential)

TMHMM gives 13-30 102-121 134-156 166-188 228-250 278-300
SP gives 10-30 100-121 138-158 173-190 227-250 272-293

mlkfilrrcl eaIPTLFILI TISFFMMRLA pgspftgert lppevmanie
akyhlndpim tqyfsylkql ahgdfgpsfk ykdysvndlv assfpvsakl
gAAAFFLAVI LGVSAGVIAA Lkqntkwdyt vmgLAMTGVV IPSFVVAPLL
VMIFAIILhw lpgggWNGGA LKFMILPMVA LSLAYIASIa ritrgsmiev 200
lhsnfirtar akglpmrrii lrhalkpALL PVLSYMGPAF VGIITGSMVI
etiyglpgig qlfvngalnr dyslvlsLTI LVGALTILFN AIVDVLYAVI
dpkiry

MW33443 Da; 306aa


Oligopeptide transport system permease protein OppC (oppC )
functionpart of the binding-protein-dependent transport system for oligopeptides, probably responsible for the translocation of the substrate across the membrane
interaction 
regulation 
 transmembrane domains: 6 (potential)

TMHMM gives 40-62 103-125 138-160 164-183 214-236 268-290
SP gives 38-59 103-122 140-160 164-180 216-236 268-290

mmlskknset lenfseklev egrslwqdar rrfmhnraaV ASLIVLVLIA
LFVILAPMLS QFayddtdwa mmssapdmes ghyfgtdssg rdllvrvaig
grISLMVGVA AALVAVVVGT LYGSLsgylg gkvdsvmmrL LEILNSFPFM
FFVILLVTFF gqnILLIFVA IGMVSWLDMA RIVrgqtlsl krkefieaaq 200
vggvstsgiv irhIVPNVLG VVVVYASLLV PSMILFesfl sflglgtqep
lsswgallsd gansmevspW LLLFPAGFLV VTLFCFNFIG dglrdaldpk
dr

MW33022 Da; 302 aa


Peptide transport system permease protein SapB (sapB )
function 
interactioninvolved in a peptide intake transport system that plays a role in the resistance to antimicrobioal peptides
regulation 
 transmembrane domains: 6 (potential), TMHMM has 5

TMHMM gives 9-31 80-102 109-131 251-273 286-308
SP gives 9-29 81-101 114-134 175-195 249-269 281-301

miiftlrrIL LLIVTLFLLT FVGFSLSYFT phaplqgasl wnawvfwfng
lihwdfgvss ingqpiaeql kevfpatmeL CILAFGFALI VGIPVGMIAG
ITrhkwqdNL INAIALLGFS IPVFWLALLL Tlfcsltlgw lpvsgrfdll
yevkpitgfa lidawlsdsp wrdeMIMSAI RHMILPVITL SVApttevir 200
lmristievy dqnyvkaaat rglsrftilr rhvlhnalpp viprlglqfs
TMLTLAMITE MVFSWPGLGR WLInairqqd yaaisAGVMV CGSLVIIVNV
ISDILGAMan plkhkewyal r

MW36038 Da; 321 aa


Peptide transport system permease protein SapC (sapC )
functioninvolved in a peptide intake transport system that plays a role in the resistance to antimicrobioal peptides
interaction 
regulation 
 transmembrane domains: 6 (potential), has 5

TMHMM gives 30-52 100-122 137-170 201-223 261-283
SP gives 30-50 99-119 134-154 197-217 223-243 259-279

mpydsvysek rppgtlrtaw rkfysdasaM VGLYGCAGLA VLCIFGGWFA
PYgidqqflg yqllppswsr ygevsfflgt ddlgrdvlsr llsgaaptvG
GAFVVTLAAT ICGLVLGTFA GAthglrsav lnhildTLLA IPSLLLAIIV
VAFAGPSLSH AMFAVWLALL prmvrsiysm vhdelekeyv iaarldgasT 200
LNILWFAVMP NITAGLVTei trALSMAILD IAALGFLDLG AQLpspewga
mlgdaleliy VAPWTVMLPG AAIMISVLLV NLLgdgvrra iiagve

MW00 Da; 31548 aa