>353365 FitnessBrowser__Btheta:353365
MIDIRGLYKSFEDKTVLSNINASFENGKTNLIIGQSGSGKTVLMKCIVGLLTPEKGEVLYDGRNLVLMGKKEKKMLRKEMGMIFQSAALFDSMSVLDNVMFPLNMFSNDTLRDRTKRAMFCLERVNLTEAKDKFPGEISGGMQKRVAIARAIALNPQYLFCDEPNSGLDPKTSLVIDDLIHDITQEYNMTTIINTHDMNSVLGIGEKVIYIYEGHKEWEGTKDDIFTSTNERLNNFIFASDLLRKVKDMEVQNMEG
>TCDB__Q0SD37 ABC superfamily, ATP-binding component, component of The cholesterol uptake porter (Mohn et al., 2008). Takes up cholesterol, 5-α-cholestanol, 5-α-cholestanone, β-sitosterol, etc. (It is not established that all of these proteins comprise the system or that other gene products are not involved.) (Rhodococcus sp. (strain RHA1))
MGVEVSVEGLTKSFGSQRIWQDVTLTLPAGEVSALLGPSGTGKSVFLKSLIGLLRPEQGSIVIDGTNILECSSKELYEIRKLFGVLFQDGALFGSMNLYDNVAFPLREHTKKSESEIRKIVMEKMELVGLLGAEDKLPGEISGGMRKRAGLARALVLDPQIILVDEPDSGLDPVRTTYISQTLIDINAEIDATILIVSHNINLARTVPDNIGMLFRRHLVMFGPREVLLTSEQPVVKQFLNGTMIGPIGMSEEKDEATMAAEQAMVDAGHHAGGVDDVEGIVPQMKATPAMSFRQAVARRQERVRHIMHTLPENAQIAIQESLDETSGYGFYDESTAPLEAVGDVR
>TCDB__Q0SFA1 Probable bifunctional ABC transport system, component of The cholesterol uptake porter (Mohn et al., 2008). Takes up cholesterol, 5-α-cholestanol, 5-α-cholestanone, β-sitosterol, etc. (It is not established that all of these proteins comprise the system or that other gene products are not involved.) (Rhodococcus sp. (strain RHA1))
MGVEVSVEGLTKSFGSQRIWQDVTLTLPAGEVSALLGPSGTGKSVFLKSLIGLLRPEQGSIVIDGTNILECSSKELYEIRKLFGVLFQDGALFGSMNLFDNVAFPLREHTKKSESEIRKIVMEKMELVGLLGAEDKLPGEISGGMRKRAGLARALVLDPQIILVDEPDSGLDPVRTTYISQTLIDINAEIDATILIVSHNINLARTVPDNIGMLFRRHLVMFGPREVLLTSEEPVVKQFLNGTMIGPIGMSEEKDEATMAQEQAMVDAGHHAGGVDDVEGIVPQMKATPGMPFRQAVARRQERVRHIMHTLPENAQIAIQESLDETSGGNGGGGYDYAYSQEDTQVIPAYRGEGYENTTHGQG
>TCDB__P63357 Probable ribonucleotide transport ATP-binding protein mkl, component of The Mce/Yrb/Mlk (Mammalian cell entry) ABC-type putative steroid uptake transporter (involved in several aspects of mycobacterial pathogenesis) (Mycobacterium tuberculosis)
MRYSDSYHTTGRWQPRASTEGFPMGVSIEVNGLTKSFGSSRIWEDVTLTIPAGEVSVLLGPSGTGKSVFLKSLIGLLRPERGSIIIDGTDIIECSAKELYEIRTLFGVLFQDGALFGSMNLYDNTAFPLREHTKKKESEIRDIVMEKLALVGLGGDEKKFPGEISGGMRKRAGLARALVLDPQIILCDEPDSGLDPVRTAYLSQLIMDINAQIDATILIVTHNINIARTVPDNMGMLFRKHLVMFGPREVLLTSDEPVVRQFLNGRRIGPIGMSEEKDEATMAEEQALLDAGHHAGGVEEIEGVPPQISATPGMPERKAVARRQARVREMLHTLPKKAQAAILDDLEGTHKYAVHEIGQ
>biolip__7d08B Acinetobacter mlafedb complex in atp-bound vtrans1 conformation
TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFLTGSAEGPVEYQFSHQAYLDNEVR
>PDB_6z5u_K Cryo-em structure of the a. Baumannii mlabdef complex bound to appnhp
SLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARAR
MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI
MYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFLTG
SAEGPVEYQFSHQ
>PDB_7d0a_B Acinetobacter mlafedb complex in adp-vanadate trapped vclose conformation
TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAAR
ARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD
LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFL
TGSAEGPVEYQFSHQAYLDNEVR
>CharProtDB__CH_107359 toluene tolerance protein Ttg2A (Pseudomonas putida)
MSVDSAYAVELKGVTFKRGSRSIFSNVDIRIPRGKVTGIMGPSGCGKTTLLRLMGAQLRPSSGEVWVAGQNLPTLSRSDLFDARKQMGVLFQSGALFTDLDVFENVAFPLRVHTQLSDEMIRDIVLMKLQAVGLRGAIDLMPDELSGGMKRRVALARAIALDPQILMYDEPFVGQDPIAMGVLVRLIRLLNDALGITSIVVSHDLAETASIADYIYVVGDGQVLGQGTPDELMGSDNPRIRQFMKGDPDGPVPFHFPAPDYRADLLGAR
>SwissProt__Q9AT00 Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic; ABC transporter I family member 13; ABC transporter ABCI.13; AtABCI13; Non-intrinsic ABC protein 11; AtNAP11 (Arabidopsis thaliana (Mouse-ear cress))
MLSLSCSSSSSSLLPPSLHYHGSSSVQSIVVPRRSLISFRRKVSCCCIAPPQNLDNDATKFDSLTKSGGGMCKERGLENDSDVLIECRDVYKSFGEKHILKGVSFKIRHGEAVGVIGPSGTGKSTILKIMAGLLAPDKGEVYIRGKKRAGLISDEEISGLRIGLVFQSAALFDSLSVRENVGFLLYERSKMSENQISELVTQTLAAVGLKGVENRLPSELSGGMKKRVALARSLIFDTTKEVIEPEVLLYDEPTAGLDPIASTVVEDLIRSVHMTDEDAVGKPGKIASYLVVTHQHSTIQRAVDRLLFLYEGKIVWQGMTHEFTTSTNPIVQQFATGSLDGPIRY
>TCDB__A4PCH8 Putative ATPase component of ABC transporter system aka LinL, component of The γ-hexachlorocyclohexane (γHCH) uptake permease, LinKLMN (most similar to 3.A.1.12.4, the QAT family) (Sphingobium japonicum)
MAQEEEISAEEARIEEAVQHDGIAISVRNLRNSFGDQVVHEGLNLDVRKGEILGVVGGSGTGKSVLMRSIIGLQTPDEGEIHVFGESMIGRLDNEALAIRKRWGVLFQGGALFSTLTVAENVEVPIREYYPNIGPKLRDEIAAYKIRLTGLPAEAGPKYPAELSGGMKKRAGLARALALDPDLLFLDEPTAGLDPIGAAAFDDQTRRLQQTLGLTVFLITHDLDTLYSICDRVAVLADRKVTAVGTIDELLATDHPWIQEYFNGPRGRAATAAVAREKDKRR
>biolip__7chaI Cryo-em structure of p.Aeruginosa mlafebd with amppnp
AYAVELKGLTFKRGSRAIFDNIDVRIPRGKVTGIMGPSGCGKTTLLRLIASQLRPSKGEVWVNGQNLPQLSRGDLFDMRKQFGVLFQSGALFTDLDVFENVAFPLRVHTQLPEEMIRDIVLMKLQAVGLRGAVELMPDELSGGMKRRVALARAIALDPQILLYDEPFVGQDPIAMGVLVRLIRLLNDALGITSIVVSHDLAETASIADYIYIVGDGRVLGHGTPDVLKETDDPRIRQFVKGIPDGPVPFHYPARDYRADLLG
>biolip__4u00A Crystal structure of ttha1159 in complex with adp
PIIRIRNLHKWFGPLHVLKGIHLEVAPGEKLVIIGPSGSGKSTLIRTINRLEDFQEGEVVVDGLSVKDDRALREIRREVGMVFQQFNLFPHMTVLENVTLAPMRVRRWPREKAEKKALELLERVGILDQARKYPAQLSGGQQQRVAIARALAMEPKIMLFDEPTSALDPEMVGEVLDVMRDLAQGGMTMVVVTHEMGFAREVADRVVFMDGGQIVEEGRPEEIFTRPKEERTRSFLQRVLH
>ecocyc__ABC-MONOMER L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) (Escherichia coli K-12 substr. MG1655)
MIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV
>biolip__6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein
HMIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDQATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNAIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV
>PDB_3tuz_C Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form
HMIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTK
ARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNP
KVLLCDQATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK
FIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGT
QQDTQAAIAWLQEHHVKVEVLGYV
>PDB_3tui_C Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form
HMIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTK
ARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNP
KVLLCDQATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK
FIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGT
QQDTQAAIAWLQEHHVKVEVLGYV
>SwissProt__P54954 Probable amino-acid import ATP-binding protein YxeO; EC 7.4.2.- (Bacillus subtilis (strain 168))
MITVKNIRKAFKDLVVLDGIDLEVKRGEVVAIIGPSGSGKSTLLRCLNLLERPDQGLIEIGEAKLNAEKFTRKEAHRLRQQTAMVFQNYNLFKNKTALQNITEALIVAQHKPRDEAKRIGMEILKQVGLEHKADSYPITMSGGQQQRIGIARALAVNPHAILLDEPTSALDPELVTGVLQVIKSIAEKQTTMIIVTHEMAFAKEVADQVIFMADGHIIEQGTPEELFDHPKNERTKRFIKQVGEPAELI
>TCDB__Q8NSN2 Methionine import ATP-binding protein metN, component of L-Methionine uptake porter, MetQNI (Corynebacterium glutamicum)
MSHTASTPTPEEYSAQQPSTQGTRVEFRGITKVFSNNKSAKTTALDNVTLTVEPGEVIGIIGYSGAGKSTLVRLINGLDSPTSGSLLLNGTDIVGMPESKLRKLRSNIGMIFQQFNLFQSRTAAGNVEYPLEVAKMDKAARKARVQEMLEFVGLGDKGKNYPEQLSGGQKQRVGIARALATNPTLLLADEATSALDPETTHEVLELLRKVNRELGITIVVITHEMEVVRSIADKVAVMESGKVVEYGSVYEVFSNPQTQVAQKFVATALRNTPDQVESEDLLSHEGRLFTIDLTETSGFFAATARAAEQGAFVNIVHGGVTTLQRQSFGKMTVRLTGNTAAIEEFYQTLTKTTTIKEITR
>biolip__4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps
MIFVNDVYKNFGSLEVLKGVTLKVNKGEVVVIIGPSGSGKSTLLRCINLLEEPTKGEVFIDGVKINNGKVNINKVRQKVGMVFQHFNLFPHLTAIENITLAPVKVKKMNKKEAEELAVDLLAKVGLLDKKDQYPIKLSGGQKQRLAIARALAMQPEVMLFDEPTSALDPEMVKEVLNVMKQLANEGMTMVVVTHEMGFAREVGDRVIFMDDGVIVEEGTPEEIFYRAKNERTREFLSKIL
>ecocyc__GLNQ-MONOMER L-glutamine ABC transporter ATP binding subunit (EC 7.4.2.1) (Escherichia coli K-12 substr. MG1655)
MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQHVS
>TCDB__P39456 TcyC (YckI), component of Uptake system for L-cystine (Bacillus subtilis)
MLTVKGLNKSFGENEILKKIDMKIEKGKVIAILGPSGSGKTTLLRCLNALEIPNRGELAFDDFSIDFSKKVKQADILKLRRKSGMVFQAYHLFPHRTALENVMEGPVQVQKRNKEEVRKEAIQLLDKVGLKDKMDLYPFQLSGGQQQRVGIARALAIQPELMLFDEPTSALDPELVGEVLKVIKDLANEGWTMVVVTHEIKFAQEVADEVIFIDGGVIVEQGPPEQIFSAPKEERTQRFLNRILNPL
>TCDB__Q9CES4 Glutamine ABC transporter ATP-binding protein, component of Glutamine transporter, GlnQP. Takes up glutamine, asparagine and glutamate which compete for each other for binding both substrate and the transmembrane protein constituent of the system (Fulyani et al. 2015). Tandem substrate binding domains (SBDs) differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. Analysis revealed the roles of individual residues in determining the substrate affinity (Lactococcus lactis subsp. lactis (strain IL1403))
MGINTQIEVTDLHKSFGKNEVLKGITTKFEKGDVVCIIGPSGSGKSTFLRALNGLETATSGDIIIDGFNLTDKNTNLNLVRQNVGMVFQHFNLFPNMTVMQNITYAPVELKKMSKDDADKKAIQLLETVGLLDKKDAMPEMLSGGQKQRVAIARALAMNPDVMLFDEPTSALDPEMVGDVLAVMQKLAEEGMTMLIVTHEMGFARKVANRVIFTDGGVILEDGTPEELFDSPKHPRLQDFLSKVLNA
>reanno__pseudo1_N1B4_Pf1N1B4_774 ABC transporter for L-asparagine and L-glutamate, ATPase component (Pseudomonas fluorescens FW300-N1B4)
MISIKNVNKWYGDFQVLTDCSTEVKKGEVIVVCGPSGSGKSTLIKCVNALEPFQKGDVIVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLSIMDNLTIAQVKVLGRSKEEASKKALQLLERVGLSAHAKKHPGQLSGGQQQRVAIARALAMDPIVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVADRVIFMDQGKIIEDCKKEEFFGDITARSDRAQHFLEKILQH
>reanno__BFirm_BPHYT_RS24015 L-histidine ABC transporter, ATPase component (Burkholderia phytofirmans PsJN)
MNATAPVALSVKNIHKSFGDHHVLKGISLDAHQGDVISILGASGSGKSTFLRCLNLLETPDDGSVSLAGEELKMKRRGDGKLQPSDRRQVDRVRSQLGMVFQNFNLWSHMTVLENLIEGPMRVQKRSRAESVEEAEALLAKVGLAEKRGHYPAHLSGGQQQRVAIARALAMHPKVMLFDEPTSALDPELVGEVLRVMRSLAEEGRTMLVVTHEMGFARHVSNRVMFLHQGQVEADGTPDEVFVECKSDRFRQFVSSHQDRTTN
>reanno__pseudo6_N2E2_Pf6N2E2_2050 ABC transporter for D-Glucosamine, putative ATPase component (Pseudomonas fluorescens FW300-N2E2)
MTDISTPSNTQPLLDIRGLRKQYGPLEVLKGVDLSMQRGNVVTLIGSSGSGKTTLLRCVNMLEEFQGGQIMLDGESIGYDDIDGKRVRHPEKVIARHRAMTGMAFQQFNLFPHLTALQNVTLGLLKVKKLPKDEAVALAEKWLERVGLLERRDHFPGQLSGGQQQRVAIARAIAMNPSLMLFDEVTSALDPELVGEVLNVIKGLAEDGMTMLLVTHEMRFAFEVSDKIVFMNQGRIEEQGPPKELFERPQSPRLAEFLKNTRF
>SwissProt__O32169 Methionine import ATP-binding protein MetN; EC 7.4.2.11 (Bacillus subtilis (strain 168))
MINLQDVSKVYKSKHGDVNAVQNVSLSIKKGEIFGIIGYSGAGKSSLIRLLNGLEKPTSGTVEVAGTKINEVNGRGLRKARHEISMIFQHFNLLWSRTVRDNIMFPLEIAGVKKSERIKRANELIKLVGLEGKEKSYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPQTTDSILDLLSDINERLGLTIVLITHEMHVIRKICNRVAVMENGKVVEEGEVLDVFKNPKEQMTKRFVQQVTEPEETKETLQHLLDDTASGKMVQLTFVGESAEQPLITEMIRNFNVSVNILQGKISQTKDGAYGSLFIHIDGDEEEVQNVIRFINDKQVKAEVITNV
>ecocyc__YAGC-MONOMER CP4-6 prophage; ABC transporter ATP-binding protein AfuC (Escherichia coli K-12 substr. MG1655)
MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATFSDGYVDIYGYHLPRPLHFGTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILLQVNATRLQPDVGEQYYLEIHPYGMFVLADAA
>reanno__pseudo5_N2C3_1_AO356_00465 ABC transporter for D-Glucosamine, putative ATPase component (Pseudomonas fluorescens FW300-N2C3)
MTDISTPSNTQPLLDIRGLRKQYGPLEVLKGVDLSMQRGNVVTLIGSSGSGKTTLLRCVNMLEEFQGGQIVLDGESIGYDDIDGKRVRHPEKLIARHRAMTGMAFQQFNLFPHLTALQNVTLGLLKVKKLPKDEAVALAEKWLERVGLLERRDHFPGQLSGGQQQRVAIARAIAMNPSLMLFDEVTSALDPELVGEVLNVIKGLAEDGMTMLLVTHEMRFAFEVSDKIVFMNQGRIEEQGPPKELFERPQSPRLAEFLKNTRF
>SwissProt__P48243 Glutamate transport ATP-binding protein GluA; Glutamate uptake system protein GluA; EC 7.4.2.1 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025))
MIKMTGVQKYFGDFHALTDIDLEIPRGQVVVVLGPSGSGKSTLCRTINRLETIEEGTIEIDGKVLPEEGKGLANLRADVGMVFQSFNLFPHLTIKDNVTLAPIKVRKMKKSEAEKLAMSLLERVGIANQADKYPAQLSGGQQQRVAIARALAMNPKIMLFDEPTSALDPEMVNEVLDVMASLAKEGMTMVCVTHEMGFARKAADRVLFMADGLIVEDTEPDSFFTNPKSDRAKDFLGKILAH
>biolip__3c41J Abc protein artp in complex with amp-pnp/mg2+
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREEVGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIMLFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSKVF
>TCDB__Q9I405 Amino acid ABC transporter ATP binding protein, component of Amino acid transporter, AatJMQP. Probably transports L-glutamic acid, D-glutamine acid, L-glutamine and N-acetyl L-glutamic acid (Johnson et al. 2008). Very similar to 3.A.1.3.19 of P. putida (Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228))
MISIKNVSKWYGDFQVLTDCSTEVAKGEVVVVCGPSGSGKSTLIKCVNALEPFQKGDIVVDGTSIADPKTNLPKLRSRVGMVFQHFELFPHLSITENLTIAQIKVLGRSKEEATKKGLALLERVGLKEHAHKHPGQLSGGQQQRVAIARALAMDPVVMLFDEPTSALDPEMVNEVLDVMVQLAHEGMTMMCVTHEMGFARKVANRVIFMDRGQIVEDCEKEEFFGDVSARSERAQQFLAKILPH
>PDB_3c4j_A Abc protein artp in complex with atp-gamma-s
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREE
VGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIM
LFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSK
VF
>PDB_2olk_A Abc protein artp in complex with adp-beta-s
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREE
VGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIM
LFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSK
VF
>PDB_2olj_A Abc protein artp in complex with adp/mg2+
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREE
VGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIM
LFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSK
VF
>PDB_7ch8_I Cryo-em structure of p.Aeruginosa mlafebd with adp-v
AYAVELKGLTFKRGSRAIFDNIDVRIPRGKVTGIMGSGCGKTTLLRLIASQLRPSKGEVWVNGQNLPQLSRGDLFDMRKQ
FGVLFQSGALFTDLDVFENVAFPLRVHTQLPEEMIRDIVLMKLQAVGLRGAVELMPDELSGGMKRRVALARAIALDPQIL
LYDEFVGQPIAMGVLVRLIRLLNDALGITSIVVSHDLAETASIADYIYIVGDGRVLGHGTPDVLKETDDPRIRQFVKGIP
DGPVPFHYPARDYRADLLG
>biolip__7ch6C Cryo-em structure of e.Coli mlafeb with amppnp
VANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPFRYPAGDYHADLLPGS
>PDB_6xgy_A Crystal structure of e. Coli mlafb abc transport subunits in the dimeric state
VANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR
KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD
LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFL
DGIADGPVPFRYPAGDYHADLLPG
>PDB_7cgn_B The overall structure of the mlafedb complex in atp-bound eqtall conformation (mutation of e170q on mlaf)
VANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR
KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD
LIMFDQPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFL
DGIADGPVPFRYPAGDYHADLLP
>PDB_7ahh_C Opua inhibited inward-facing, sbd docked
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTS
GKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYP
KQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGK
IMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAA
RKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>biolip__7aheC Opua inhibited inward facing
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTSGKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYPKQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGKIMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAARKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>PDB_7ahd_C Opua (e190q) occluded
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTS
GKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYP
KQLSGGMQQRVGLARALANDPEILLMDQAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGK
IMQIGTGEEILTNPANDYVK
>PDB_1oxv_D Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus
MVRIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPE
DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS
LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL
IGEINELEGKVTNEGVVIGSLRFPVSVSSDRAIIGIRPEDVKLSKDVIKDDSWILVGKGKVKVIGYQGGLFRITITPLDS
EEEIFTYSDHPIHSGEEVLVYVRKDKIKVFEKN
>PDB_1oxv_A Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus
MVRIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPE
DRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPS
LLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASL
IGEINELEGKVTNEGVVIGSLRFPVSVSSDRAIIGIRPEDVKLSKDVIKDDSWILVGKGKVKVIGYQGGLFRITITPLDS
EEEIFTYSDHPIHSGEEVLVYVRKDKIKVFEKN
>SwissProt__Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- (Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus))
MVRIIVKNVSKVFKKGKVVALDNVNINIENGERFGILGPSGAGKTTFMRIIAGLDVPSTGELYFDDRLVASNGKLIVPPEDRKIGMVFQTWALYPNLTAFENIAFPLTNMKMSKEEIRKRVEEVAKILDIHHVLNHFPRELSGGQQQRVALARALVKDPSLLLLDEPFSNLDARMRDSARALVKEVQSRLGVTLLVVSHDPADIFAIADRVGVLVKGKLVQVGKPEDLYDNPVSIQVASLIGEINELEGKVTNEGVVIGSLRFPVSVSSDRAIIGIRPEDVKLSKDVIKDDSWILVGKGKVKVIGYQGGLFRITITPLDSEEEIFTYSDHPIHSGEEVLVYVRKDKIKVFEKN
>SwissProt_P0AAH0 Phosphate import ATP-binding protein PstB; ABC phosphate transporter; Phosphate-transporting ATPase; EC 7.3.2.1 from Escherichia coli (strain K12)
MSMVETAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNIL
TNSQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQ
RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF
TKPAKKQTEDYITGRYG
>biolip__2d62A Crystal structure of multiple sugar binding transport atp- binding protein
MIGMAEVKLINIWKRFGDVTAVKDLSLEIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTRGQIYIEDNLVADPEKGVFVPPKERDVAMVFQSYALYPHMTVYDNIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIIRRPKVFLMDEPLSNLDAKLRVKMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNKGELQQVGTPDEVYYKPVNTFVAGFIGSPPMNFLDATITDDGFLDFGEFKLKLLQDQFEVLEEENMVGKEVIFGIRPEDVHDASFTHIDVPEENTVKATVDIIENLGGEKIVHLRRGNISFTAKFPKESKVREGDEVSVVFDMKKIHIFRKDTEKAIF