>BWI76_RS05130 FitnessBrowser__Koxy:BWI76_RS05130
MQENIPHSDTTFSLDRVTFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSDGDILLDGQPLDSWGSKAFARKVAYLPQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAIALVGLKPLAQRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQQRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAALMRSETLEQIYGIPMGILPHPAGAAPVSFVY
>ecocyc__FHUC-MONOMER iron(III) hydroxamate ABC transporter ATP binding subunit (EC 7.2.2.16) (Escherichia coli K-12 substr. MG1655)
MQEYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLSLVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGILPHPAGAAPVSFVY
>TCDB__Q8GRB0 PvuE, component of The iron-vibrioferrin uptake porter (Vibrio parahaemolyticus)
MLRTQNLSVAYGKQTIIPDLSLSIPQGKITALVGPNGCGKSTLLKTLVRINKPASGQVLYDDKPLSSYGDKRLARSLSFVPQILVSPEGITVRKLVEYGRSPYLSHWGRLSQQDKALVEQAMQDTGVIEFADKPVESLSGGQRQRAWIAMVMAQDTDVVMLDEPTTYLDLSHQVELMKLMRKMNDKGKTVVVVLHDLNQACRYCDHLVVLEKGQLVTQGTPQEVLTEGMLASVFDLQARVFNDPISGTPMCVAV
>TCDB__Q9X665 FhuC aka FhuA, component of Iron (Fe3+)-hydroxamate porter (transports Fe3+-ferrichrome and Fe3+-ferrioxamine B with FhuD1, and these compounds plus aerobactin and coprogen with FhuD2)
MNRLHGQQVKIGYGDNTIINKLDVEIPDGKVTSIIGPNGCGKSTLLKALSRLLAVKEGEVFLDGENIHTQSTKEIAKKIAILPQSPEVADGLTVGELVSYGRFPHQKGFGRLTAEDKKEIDWAMEVTGTDTFRHRSINDLSGGQRQRVWIAMALAQRTDIIFLDEPTTYLDICHQLEILELVQKLNQEQGCTIVMVLHDINQAIRFSDHLIAMKEGDIIATGSTEDVLTQEILEKVFNIDVVLSKDPKTGKPLLVTYDLCRRAYS
>ecocyc__FEPC-MONOMER ferric enterobactin ABC transporter ATP binding subunit (EC 7.2.2.17) (Escherichia coli K-12 substr. MG1655)
MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVAGTPLVVPLGRTAPSTANS
>TCDB__Q9RCF3 ViuC, component of The iron-vibriobactin/enterobactin uptake porter (Vibrio cholerae)
MDTIWDADLQSAALKAEHHRLKTERLSLGYEGKSVCDALDLAIPHGKFSVIVGPNGCGKSTLLKSLCRLLKPLAGQVLLDGQNIHQLPTKVVAKQLGLLPQSALTPEGIKVVDLVSRGRYPHQGLFRQWSRVDERAVEEAMRATHVHELAQHSVDQLSGGQRQRVWVAMGLAQQTPYLLLDEPTTYLDIAHQIELLDLFWRLNRQQGHTLVAVLHDLNQACRYADHLIVLQEGKIVAQGDPHSLVTPALVKQVFGIDCVVMPDPISCTPLIIPYSLKRG
>SwissProt__Q81V82 Petrobactin import ATP-binding protein FpuD; EC 7.2.2.- (Bacillus anthracis)
MQKALETKRLTLSYGETIIIDELNLEIPKGEITIFIGSNGCGKSTLLRSLARLLKPTTGDILLDNQAIQSMQTKQIARQMAILPQGPQAPEGLTVLQLVKQGRYPYQTWLKQWSEKDEEMVQNALAATGMTEFAERDVHALSGGQRQRAWIAMTLAQDTDIILLDEPTTYLDMTHQIEVLDLLFELNETEQRTIVMVLHDLNLACRYADNIVAIQDKQIYAQGKPEEVVDEKLVRDVFRMECQISTDPLFGTPLCIPHGKGRRVRKEVAHAMR
>TCDB__Q47087 CbrD, component of Iron-chrysobactine porter (Erwinia chrysanthemi)
MTAITSRELTLGYASQTIIDNLDIQLPEGKVSVLIGSNGSGKSTLLKSFARLLKPLKGAVILNGEDIHRQSTAAVARELAILPQMPDAPEGITVKQLVSLGRYPYQNWLQQWSEQDEAMVNQALRQTGTDMLAERPVDALSGGQRQRVWIAMTLGQDTEVVLLDEPTTFLDLAHQIEVLDLLRELNRQHGKTIIMVLHDLNLACRYGDHMVAVHNRTAFAQGAPAEILDEALVKTVFNLDCRIVPTRFSTRHCVFRSGARNHRRGRRWHKSAG
>TCDB__Q9A197 Putative ferrichrome ABC transporter aka SiuA aka Spy0386, component of The Fe3+ /Fe3+ferrichrome/Fe3+heme uptake porter; SiuABDG (FTSABCD) (Streptococcus pyogenes serotype M1)
MTTISAEDLTIAYEQRTIIDKLSFYIPEGKITTIIGANGCGKSSLLKALTRLLPPKQGVVYLNGQNIATLETKEVAKKLALLPQVQEATNGITVYELVSYGRFPHQSYFGNLSPADKKAIHWAMQATNVMAYADQPVDALSGGQRQRVWLAMALAQGTDTIFLDEPTTYLDLNHQLEILELVKSLNKDAGKTIVMVLHDLNLSARYSDHLIAMKHGKIHYTGTIADVMTSPIIQDIFQIKPVLVDDPIHNCPIVLTYQLQ
>ecocyc__FECE-MONOMER ferric citrate ABC transporter ATP binding subunit (EC 7.2.2.18) (Escherichia coli K-12 substr. MG1655)
MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEIHPEPVSGRPMCLMR
>CharProtDB__CH_088316 ferrichrome transport ATP-binding protein FhuC (Bacillus subtilis)
MNSLSTEQLGIGYGDRVIVEDLNISIPKGKITTLIGPNGCGKSTILKTMSRIMRSHAGAVYLNGKAIHKMSTKDIAKDMAILPQTPEAPSGLTVHELVSYGRFPHQSGFGRLNDEDRRIIKWALEETGMAEYAERPIEALSGGQRQRVWIAMALAQGTELLLLDEPTTYLDLAHQLEILQLLDRLNKEQGRTILMVIHDLNHAARFSHYMIALKKGTVIKEGTALEVMTPDILKQVFQIDAEIVTDPRTNKPVCLTYDLIKNEKELVTV
>SwissProt__Q81LM1 Petrobactin import ATP-binding protein FpuC; EC 7.2.2.- (Bacillus anthracis)
MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLMARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFGRGPHKSWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGVPEEVLCHEMFQHIFGIEVDIFQGSEKPFFTPKRISKKGGAKCEQKNVLPLS
>SwissProt__O32188 Probable siderophore transport system ATP-binding protein YusV (Bacillus subtilis (strain 168))
MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQVTQDPLFGTPLCIPHGRGRCIVQEAAFTSHG
>SwissProt__P94420 Petrobactin import ATP-binding protein YclP; EC 7.2.2.- (Bacillus subtilis (strain 168))
MVEVRNVSKQYGGKVVLEETSVTIQKGKITSFIGPNGAGKSTLLSIMSRLIKKDSGEIYIDGQEIGACDSKELAKKMSILKQANQINIRLTIKDLVSFGRFPYSQGRLTEEDWVHINQALSYMKLEDIQDKYLDQLSGGQCQRAFIAMVIAQDTDYIFLDEPLNNLDMKHSVEIMKLLKRLVEELGKTIVIVIHDINFASVYSDYIVALKNGRIVKEGPPEEMIETSVLEEIYDMTIPIQTIDNQRIGVYFS
>TCDB__Q99YA4 Putative ABC transporter aka SiaC, component of The heme porter, Shp/SiaABC (HtsABC). Shp is a cell surface heme binding protein that transfers the heme directly to HstA (Nygaard et al., 2006). The crystal structure of the heme binding domain of Shp has been solved (Aranda et al., 2007). HtsABC is required for the uptake of staphyloferrin A (Beasley et al. 2009). The Shp cell surface heme receptor feeds iron-heme to the transporter in preparation for uptake (Streptococcus pyogenes serotype M1)
MSKNSSHIQVQNLSFAYEEKLVLDDLTFSIPKGKITTIMGANGSGKSTLLQLLTKNLPLKQGQVWLEQEELATISLKAFAKKVAVVHQYHQVVEGLLVGELVAMARLARRSFFKTTTKEDEERLAWALEVTALSDYVYRDIQHLSGGEQQRVWIAMALAQDTDIIFLDEPTTYLDIKYQLDILKLITKINQELGLTIVLVLHDINQALSLSDHLIGLKDGRLYAQGQPRDLLDQQFIRDVFGVELPFVERNGQQFVLTSLVNETNGIRTQRRDRNKNR
>TCDB__Q9RK11 CchE, component of Ferric iron-coelichelin uptake porter, CchCDEF (Streptomyces coelicolor)
MVVQSITGTETEVDGASRLAARGVTVGYGTRSVIDGLDVAIPPGVITTIIGPNGCGKSTLLRTLSRLLRPTGGTVVLDGEDIAALRTRDVAKKLGLLPQAPVAPEGLTVSDLVARGRHPHQSWLRQWSSDDADVVRQALAMTGVSDLADRPVDSLSGGQRQRVWISMTLAQGTDLLLLDEPTTYLDLAHAVDVLDLVDDLHESGRTVVMVLHDLNLAARYSDNLVVMREGAILAQGHPRDVITAGLLHEAFGLRAKVIDDPVGDRPLIVPIGRTHVELDRSAPELLK
>TCDB__Q56993 HmuV aka YPO0279 aka Y0539, component of Heme (hemin) uptake porter. The receptor, HmuT, binds two parallel stacked heme molecules, and two are transported per reaction cycle (Yersinia pestis)
MVDMAVTPVALLEASHLHYHVQQQALINDVSLHIASGEMVAIIGPNGAGKSTLLRLLTGYLSPSHGECHLLGQNLNSWQPKALARTRAVMRQYSELAFPFSVSEVIQMGRAPYGGSQDRQALQQVMAQTDCLALAQRDYRVLSGGEQQRVQLARVLAQLWQPQPTPRWLFLDEPTSALDLYHQQHTLRLLRQLTRQEPLAVCCVLHDLNLAALYADRIMLLAQGKLVACGTPEEVLNAETLTQWYQADLGVSRHPESALPQIYLRQ
>TCDB__Q32AY3 Hemin import ATP-binding protein hmuV, component of The heme uptake porter, ShuTUV (Burkhard and Wilks, 2008). Transports a single heme per reaction cycle (Mattle et al., 2010). (3-d structure of ShuT is known (2RG7) (Shigella dysenteriae serotype 1 (strain Sd197))
MISAQNLVYSLQGRRLTDNVSLTFPGGEIVAILGPNGAGKSTLLRQLTGYLQPDSGECRLFNKPLNEWSITELAKHRAVMRQNSHMAFPFSVQEVIQMGRHPHRTGNQDNETAQIMALCDCQALANRDYRQLSGGEQQRVQLARLLVQLWEPTPSPKWLFLDEPTSALDIHHQQHLFRLLRQLVHERQFNVCCVLHDLNLAARYADRIVLMQKGKVIANGKPQDVLTQQALTMLYGADITVLEDPANHSPLIVLDH
>TCDB__Q9L177 DesC, component of Desferrioxamine B uptake porter, DesABC (Streptomyces coelicolor)
MRSGEDAAGTPRLRGHELSATGVTVAYDGVDVVHDAGVRLRPGEVTVLVGPNGSGKSTLLRTVARLQRARSATLSLDGATDGLALTSREFSRYVALLTQGRPTPGGLTVRDVVEFGRYPYRGRWGRPDPDGPAAVERALALTGVDGLADRGADHLSGGQLQRVWLASCLAQETGVLLLDEPTTYLDLRYQVELLDLIRDLADDHGIAVGVVLHDLDQAAAVADRITLLEAGRIVADGPPEDVLTPERLTAVYGIRIDVDTDPLTGRLRTRPIGRHHIRTPRTRTPERLGTTS
>SwissProt__Q81XB3 Petrobactin import ATP-binding protein FatE; EC 7.2.2.- (Bacillus anthracis)
MIKIDNVKKFYTDKVKIGPLDIEIPKAGFTSLIGPNGAGKSTTLLMIGRLLDMDEGQIQVANMDVSESKSKDLAKVLTILRQENHFVTRLTVRQLVGFGRFPYSKGRLTKEDEVIISKYIDFLDLTNLENRYLDELSGGQRQRAYVAMVLCQETEYVLLDEPLNNLDVARSVQMMEHLRRAANEFGRTILTVMHDINFAAKYSDKICAMKDGQIAAFGTVEEVMDSTLLTDIFETRIEIIKGPYGPIAVY
>TCDB__A8GDS6 HemV, component of The heme-specific uptake porter, HemTUV (Serratia proteamaculans (strain 568))
MDNTASLTAQQLRYSLGSRRLINDVSLSINSGEMVAIIGPNGAGKSTLLRLLTGYLAPGCGECQLLGRPLEQWQPQQLAKVRAVMRQHSDLAFPFTVEEVVSMGRAPHGKRDAQRAVQQVMAQTDCLELAQRDYRQLSGGEQQRVQLARVLAQLWQPQPTPAWLFLDEPTSALDLYHQQHTLRLLRTLTRQQPIAVCCVLHDLNLAALYADRILLMHQGQLVATGTPQEVLQAEILTRWYQADLGVVHHPEVALPQVYLRQ
>TCDB__O68877 Hemin import ATP-binding protein HmuV, component of The heme uptake porter, PhuTUV (transports one heme per reaction cycle) (Pseudomonas aeruginosa)
MLRVENLSIRRGGKTVLEGLELELRPGEMLGVLGPNGAGKSTLLGALCGELEPAEGLVLLDERGLDDWPGVARAQRLAVLPQSSSLGFAFPVEAVVGFGRLPHSSGRERDVQIVAEALAAADASHLAGRSYLALSGGERQRVHLARVLAQLWPGEPGQVLLLDEPTSALDPLHQHTTLQAVHDFARRGASVLVILHDLNLAARYCDRLLLLQNGRPHLLGTPEEVLRPEPLRAVFGLEVLVQRHPERGHPLIVAR
>TCDB__Q93SS1 Hemin import ATP-binding protein hmuV, component of Heme uptake porter, HugBCD (Villarreal et al., 2008); also called HmuTUV (Plesiomonas shigelloides)
MRNLTLQRGRRQILSQLSLDLRAGELTVLLGPNGTGKSTLLKCISGEMAAQGEIRLFGQPQSQWPAPILARRMAILPQSSALSFSFLAREVVALGRLPHASGKIADEVIIQRCLQAVGAEHLADSAYTVLSGGEKQRIHFARVLAQLDEHMVDSPQTEREPTAAAPKLLMLDEPTSALDLSHQHQTLQTAQRRARQGDAVLVILHDLNLAARYADRILLLNHGQIQADGSPEEVLTAERIKQIFAFDAQVFRHPETGRLHIS
>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
>PDB_8bmp_A Cryo-em structure of the folate-specific ecf transporter complex in msp2n2 lipid nanodiscs bound to atp and adp
GSDNIISFDHVTFDSPRPALSDLSFAIERGSWTALIGHNGSGKSTVSKLINGLLAPDDLDKSSITVDGVKLGADTVWEVR
EKVGIVFQNPDNQFVGATVSDDVAFGLENRAVPRPEMLKIVAQAVADVGMADYADSEPSNLSGGQKQRVAIAGILAVKPQ
VIILDESTSMLDPEGKEQILDLVRKIKEDNNLTVISITHDLEEAAGADQVLVLDDGQLLDQGKPEEIFPKVEMLKRIGLD
IPFVYRLKQLLKERGIVLPDEIDDDEKLVQSLWQLNSK
>biolip__5d3mA Folate ecf transporter: amppnp bound state
GSDNIISFDHVTFTYPDSPRPALSDLSFAIERGSWTALIGHNGSGKSTVSKLINGLLAPDDLDKSSITVDGVKLGADTVWEVREKVGIVFQNPDNQFVGATVSDDVAFGLENRAVPRPEMLKIVAQAVADVGMADYADSEPSNLSGGQKQRVAIAGILAVKPQVIILDESTSMLDPEGKEQILDLVRKIKEDNNLTVISITHDLEEAAGADQVLVLDDGQLLDQGKPEEIFPKVEMLKRIGLDIPFVYRLKQLLKERGIVLPDEIDDDEKLVQSLWQLNS
>PDB_8bms_A Cryo-em structure of the mutant solitary ecf module 2eq in msp2n2 lipid nanodiscs in the atpase closed and atp-bound conformation
SDNIISFDHVTFTDSPRPALSDLSFAIERGSWTALIGHNGSGKSTVSKLINGLLAPDDLDKSSITVDGVKLGADTVWEVR
EKVGIVFQNPDNQFVGATVSDDVAFGLENRAVPRPEMLKIVAQAVADVGMADYADSEPSNLSGGQKQRVAIAGILAVKPQ
VIILDQSTSMLDPEGKEQILDLVRKIKEDNNLTVISITHDLEEAAGADQVLVLDDGQLLDQGKPEEIFPKVEMLKRIGLD
IPFVYRLKQLLKERGIVLPDEIDDDEKLVQSLWQLNSK
>biolip__4fi3C Structure of vitamin b12 transporter btucd-f in a nucleotide-bound state
SIVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQQTPPFATPVWHYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDQPMCSLDVAQQSALDKILSALSQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGMNFRRLDIEGHRMLISTI
>PDB_1l7v_C Bacterial abc transporter involved in b12 uptake
SIVMQLQDVAESTRLGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMTSGKGSIQFAGQPLEAWSATKLALHRAYLSQQ
QTPPFATPVWHYLTLHQHDKTRTELLNDVAGALALDDKLGRSTNQLSGGEWQRVRLAAVVLQITPQANPAGQLLLLDEPM
NSLDVAQQSALDKILSALCQQGLAIVMSSHDLNHTLRHAHRAWLLKGGKMLASGRREEVLTPPNLAQAYGM
>SwissProt__O06967 Multidrug resistance ABC transporter ATP-binding/permease protein BmrA; EC 7.6.2.- (Bacillus subtilis (strain 168))
MPTKKQKSKSKLKPFFALVRRTNPSYGKLAFALALSVVTTLVSLLIPLLTKQLVDGFSMSNLSGTQIGLIALVFFVQAGLSAYATYALNYNGQKIISGLRELLWKKLIKLPVSYFDTNASGETVSRVTNDTMVVKELITTHISGFITGIISVIGSLTILFIMNWKLTLLVLVVVPLAALILVPIGRKMFSISRETQDETARFTGLLNQILPEIRLVKASNAEDVEYGRGKMGISSLFKLGVREAKVQSLVGPLISLVLMAALVAVIGYGGMQVSSGELTAGALVAFILYLFQIIMPMGQITTFFTQLQKSIGATERMIEILAEEEEDTVTGKQIENAHLPIQLDRVSFGYKPDQLILKEVSAVIEAGKVTAIVGPSGGGKTTLFKLLERFYSPTAGTIRLGDEPVDTYSLESWREHIGYVSQESPLMSGTIRENICYGLERDVTDAEIEKAAEMAYALNFIKELPNQFDTEVGERGIMLSGGQRQRIAIARALLRNPSILMLDEATSSLDSQSEKSVQQALEVLMEGRTTIVIAHRLSTVVDADQLLFVEKGEITGRGTHHELMASHGLYRDFAEQQLKMNADLENKAG
>biolip__7qkrA Cryo-em structure of abc transporter ste6-2p from pichia pastoris with verapamil at 3.2 a resolution
DPRVTEILERQIKADSYGASLVDLYGMLQGWEYCLAVAAYICSIVAGAALPLMTLIFGDMAQQFTDYSSGLHSNNQFVDKIDENALYFVYLGVGLLVFNYFATLLHIVVSEIIASRVREKFIWSILHQNMAYLDSLGSGEITSSITSDSQLIQQGVSEKIGLAAQSIATVVSALTVAFVIYWKLALVLLSVMVALILSSTPTILMLMQAYTDSIASYGKASSVAEEAFAAIKTATAFGAHEFQLQKYDEFILESKGYGKKKAISLALMMGSIWFIVFATYALAFWQGSRFMVSDNSGIGKILTACMAMLFGSLIIGNATISLKFVMVGLSAASKLFAMINREPYFDSASDAGEKINEFDGSISFRNVTTRYPSRPDITVLSDFTLDIKPGQTIALVGESGSGKSTVIALLERFYEYLDGEILLDGVDLKSLNIKWVRQQMALVQQEPVLFAASIYENVCYGLVGSKYENVTEKVKRELVEKACKDANAWEFISQMSNGLDTEVGERGLSLSGGQKQRIAIARAVISEPKILLLDEATSALDTRSEGIVQDALNRLSETRTTIVIAHRLSTIQNADLIVVLSKGKIVETGSHKELLKKKGKYHQLVQIQNIRTKINLFLMLLQINKGDYYLLIPCLFLALIAGMGFPSFALLAGRVIEAFQVTGPQDFPHMRSLINKYTGFLFMIGCVLLIVYLFLTSFMVLSSESLVYKMRYRCFKQYLRQDMSFFDRPENKVGTLVTTLAKDPQDIEGLSGGTAAQLAVSVVIVVAGIILAVAVNWRLGLVCTATVPILLGCGFFSVYLLMVFEERILKDYQESASYACEQVSALKTVVSLTREVGIYEKYSNSIKDQVKRSARSVSRTTLLYALIQGMNPWVFALGFWYGSRLLLEGRATNREFFTVLMAILFGCQSAGEFFSYAPGMGKAKQAAINIRQVLDTRPKSIDIESEDGLKIDRLNLKGGIELRDVTFRYPTRPEVPVLTDLNLIIKPGQYVGLVGASGCGKSTTVGLIERFYDPESGQVLLDGVDIRDLHLRTYREVLALVQQEPVLFSGSIRDNIMVGSISEEDMIKACKDANIYDFISSLPEGFDTLCGNKGTMLSGGQKQRVAIARALIRNPRVLLLDEATSALDSESEMVVQDAIDKASKGRTTITIAHRLSTVQNCDVIYVFDAGRIVESGKHDELLQLRGKYYDLVQLQGLNA
>biolip__4hluC Structure of the ecfa-a' heterodimer bound to adp
GSGRIELNSVSFRYNGDYVLKDVNAEFETGKIYVVVGKNGSGKTTLLKILAGLLAAAGEIFLDGSPADPFLLRKNVGYVFQNPSSQIIGATVEEDVAFSLEIMGLDESEMRKRIKKVLELVGLSGLAAADPLNLSGGQKQRLAIASMLARDTRFLALDEPVSMLDPPSQREIFQVLESLKNEGKGIILVTHELEYLDDMDFILHISNGTIDFCGSWEEFVEREFDDVEIPFKWKLWKKCGKINLWEDRY
>PDB_4zir_B Crystal structure of ecfaa' heterodimer bound to amppnp
SGRIELNSVSFRYNGDYVLKDVNAEFETGKIYVVVGKNGSGKTTLLKILAGLLAAAGEIFLDGSPADPFLLRKNVGYVFQ
NPSSQIIGATVEEDVAFSLEIDESEMRKRIKKVLELVGLSGLAAADPLNLSGGQKQRLAIASMLARDTRFLALDEPVSML
DPPSQREIFQVLESLKNEGKGIILVTHELEYLDDMDFILHISNGTIDFCGSWEEFVEREFDDVEIPFKWKLWKKCGKINL
WEDRYEN
>PDB_4myh_B Structure of the glutathione bound mitochondrial abc transporter, atm1
YIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLFGELRNA
VFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILTYQFGAS
FAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDSQIKVSQ
SLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFKLRKNEV
KIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESGRILING
RDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGLMISGGE
KQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVREEGKHL
ELLAMPGSLYRELWTIQEDLDHLENELKDQQELWSHPQ
>PDB_7psn_A S. Cerevisiae atm1 in msp1e3d1 nanodiscs with bound amp-pnp and mg2+
LKDLFRYIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLF
GELRNAVFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILT
YQFGASFAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDS
QIKVSQSLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFK
LRKNEVKIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESG
RILINGRDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGL
MISGGEKQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVR
EEGKHLELLAMPGSLYRELWTIQED
>PDB_7psm_A S. Cerevisiae atm1 in msp1d1 nanodiscs with bound amp-pnp and mg2+
LKDLFRYIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLF
GELRNAVFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILT
YQFGASFAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDS
QIKVSQSLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFK
LRKNEVKIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESG
RILINGRDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGL
MISGGEKQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVR
EEGKHLELLAMPGSLYRELWTIQED
>biolip__7pslA S. Cerevisiae atm1 in msp1d1 nanodiscs in nucleotide-free state
LKDLFRYIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLFGELRNAVFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILTYQFGASFAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDSQIKVSQSLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFKLRKNEVKIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESGRILINGRDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGLMISGGEKQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVREEGKHLELLAMPGSLYRELWTIQEDLDHLENELKDQQELW
>SwissProt__P40416 Iron-sulfur clusters transporter ATM1, mitochondrial; EC 7.-.-.- (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast))
MLLLPRCPVIGRIVRSKFRSGLIRNHSPVIFTVSKLSTQRPLLFNSAVNLWNQAQKDITHKKSVEQFSSAPKVKTQVKKTSKAPTLSELKILKDLFRYIWPKGNNKVRIRVLIALGLLISAKILNVQVPFFFKQTIDSMNIAWDDPTVALPAAIGLTILCYGVARFGSVLFGELRNAVFAKVAQNAIRTVSLQTFQHLMKLDLGWHLSRQTGGLTRAMDRGTKGISQVLTAMVFHIIPISFEISVVCGILTYQFGASFAAITFSTMLLYSIFTIKTTAWRTHFRRDANKADNKAASVALDSLINFEAVKYFNNEKYLADKYNGSLMNYRDSQIKVSQSLAFLNSGQNLIFTTALTAMMYMGCTGVIGGNLTVGDLVLINQLVFQLSVPLNFLGSVYRDLKQSLIDMETLFKLRKNEVKIKNAERPLMLPENVPYDITFENVTFGYHPDRKILKNASFTIPAGWKTAIVGSSGSGKSTILKLVFRFYDPESGRILINGRDIKEYDIDALRKVIGVVPQDTPLFNDTIWENVKFGRIDATDEEVITVVEKAQLAPLIKKLPQGFDTIVGERGLMISGGEKQRLAIARVLLKNARIMFFDEATSALDTHTEQALLRTIRDNFTSGSRTSVYIAHRLRTIADADKIIVLDNGRVREEGKHLELLAMPGSLYRELWTIQEDLDHLENELKDQQEL
>biolip__7ow8A Cryoem structure of the abc transporter bmra e504a mutant in complex with atp-mg
SKLKPFFALVRRTNPSYGKLAFALALSVVTTLVSLLIPLLTKQLVDGFSMSNLSGTQIGLIALVFFVQAGLSAYATYALNYNGQKIISGLRELLWKKLIKLPVSYFDTNASGETVSRVTNDTMVVKELITTHISGFITGIISVIGSLTILFIMNWKLTLLVLVVVPLAALILVPIGRKMFSISRETQDETARFTGLLNQILPEIRLVKASNAEDVEYGRGKMGISSLFKLGVREAKVQSLVGPLISLVLMAALVAVIGYGGMQVSSGELTAGALVAFILYLFQIIMPMGQITTFFTQLQKSIGATERMIEILAEEEEDTVTGKQIENAHLPIQLDRVSFGYKPDQLILKEVSAVIEAGKVTAIVGPSGGGKTTLFKLLERFYSPTAGTIRLGDEPVDTYSLESWREHIGYVSQESPLMSGTIRENICYGLERDVTDAEIEKAAEMAYALNFIKELPNQFDTEVGERGIMLSGGQRQRIAIARALLRNPSILMLDAATSSLDSQSEKSVQQALEVLMEGRTTIVIAHRLSTVVDADQLLFVEKGEITGRGTHHELMASHGLYRDFAEQQLKMNADLEN
>PDB_7bg4_A Multidrug resistance transporter bmra mutant e504a bound with atp, mg, and rhodamine 6g solved by cryo-em
KSKLKPFFALVRRTNPSYGKLAFALALSVVTTLVSLLIPLLTKQLVDGFSMSNLSGTQIGLIALVFFVQAGLSAYATYAL
NYNGQKIISGLRELLWKKLIKLPVSYFDTNASGETVSRVTNDTMVVKELITTHISGFITGIISVIGSLTILFIMNWKLTL
LVLVVVPLAALILVPIGRKMFSISRETQDETARFTGLLNQILPEIRLVKASNAEDVEYGRGKMGISSLFKLGVREAKVQS
LVGPLISLVLMAALVAVIGYGTAGALVAFILYLFQIIMPMGQITTFFTQLQKSIGATERMIEILAEEEEDTVTGKQIENA
HLPIQLDRVSFGYKPDQLILKEVSAVIEAGKVTAIVGPSGGGKTTLFKLLERFYSPTAGTIRLGDEPVDTYSLESWREHI
GYVSQESPLMSGTIRENICYGLERDVTDAEIEKAAEMAYALNFIKELPNQFDTEVGERGIMLSGGQRQRIAIARALLRNP
SILMLDAATSSLDSQSEKSVQQALEVLMEGRTTIVIAHRLSTVVDADQLLFVEKGEITGRGTHHELMASHGLYRDFAEQQ
LKMNADLENKAG
>PDB_7ph2_A Nanodisc reconstituted msba in complex with nanobodies, spin-labeled at position a60c
TFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISW
VSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIIL
IVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSIS
DPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEG
KRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT
LASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAI
ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGV
YAQLHKMQF
>ecocyc__EG10613-MONOMER ATP-binding lipopolysaccharide transport protein (EC 7.5.2.6) (Escherichia coli K-12 substr. MG1655)
MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQFGQ
>PDB_7mew_A E. Coli msba in complex with g247
STWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSY
CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQL
SIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSA
SSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQE
KDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL
REYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ
RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLE
HRGVYAQLHKMQ
>biolip__7ph3A Amp-pnp bound nanodisc reconstituted msba with nanobodies, spin- labeled at position a60c
NDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQ
>PDB_7bcw_A Structure of msba in salipro with adp vanadate
DLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVS
SYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSW
QLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMV
SASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSE
QEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH
DLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ
RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDL
LEHRGVYAQLHKMQ
>PDB_6bpp_A E. Coli msba in complex with lps and inhibitor g092
DKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSY
VSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY
SWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMK
MVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILD
SEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMD
GHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSG
GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHN
DLLEHRGVYAQLHKMQ
>PDB_6bpl_A E. Coli msba in complex with lps and inhibitor g907
DKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSY
VSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY
SWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMK
MVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILD
SEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMD
GHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSG
GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHN
DLLEHRGVYAQLHKMQ
>PDB_8dmm_A Structure of the vanadate-trapped msba bound to kdl
KDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYV
SSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYS
WQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKM
VSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDS
EQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDG
HDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGG
QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHND
LLEHRGVYAQLHKMQF
>biolip__4u00A Crystal structure of ttha1159 in complex with adp
PIIRIRNLHKWFGPLHVLKGIHLEVAPGEKLVIIGPSGSGKSTLIRTINRLEDFQEGEVVVDGLSVKDDRALREIRREVGMVFQQFNLFPHMTVLENVTLAPMRVRRWPREKAEKKALELLERVGILDQARKYPAQLSGGQQQRVAIARALAMEPKIMLFDEPTSALDPEMVGEVLDVMRDLAQGGMTMVVVTHEMGFAREVADRVVFMDGGQIVEEGRPEEIFTRPKEERTRSFLQRVLH