>AZOBR_RS17960 FitnessBrowser__azobra:AZOBR_RS17960
MSPDQTQPLYDLAGVSFSVAGRAILSGLSLRLEQGRIYGLVGPNGSGKSTLIRLLARQQPPGGGTIRCLGTDLARIGDRDFARTVAYMPQFTPPAEGMTVRELVALGRFPWHGALGRFGAEDAAKVAEAIAETHLDAFADRLVDSLSGGERQRVWLAMMLAQDTRCLLLDEPTSALDIASQVELLGLVRRLSRARGIGAVIVLHDINMAASVCDEILAMRNGALIAQGTPDAIMTGETLGAIYHLAMTTVPHPVTGKPIGCVL
>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
>ecocyc__FECE-MONOMER ferric citrate ABC transporter ATP binding subunit (EC 7.2.2.18) (Escherichia coli K-12 substr. MG1655)
MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEIHPEPVSGRPMCLMR
>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
>TCDB__Q47087 CbrD, component of Iron-chrysobactine porter (Erwinia chrysanthemi)
MTAITSRELTLGYASQTIIDNLDIQLPEGKVSVLIGSNGSGKSTLLKSFARLLKPLKGAVILNGEDIHRQSTAAVARELAILPQMPDAPEGITVKQLVSLGRYPYQNWLQQWSEQDEAMVNQALRQTGTDMLAERPVDALSGGQRQRVWIAMTLGQDTEVVLLDEPTTFLDLAHQIEVLDLLRELNRQHGKTIIMVLHDLNLACRYGDHMVAVHNRTAFAQGAPAEILDEALVKTVFNLDCRIVPTRFSTRHCVFRSGARNHRRGRRWHKSAG
>CharProtDB__CH_088316 ferrichrome transport ATP-binding protein FhuC (Bacillus subtilis)
MNSLSTEQLGIGYGDRVIVEDLNISIPKGKITTLIGPNGCGKSTILKTMSRIMRSHAGAVYLNGKAIHKMSTKDIAKDMAILPQTPEAPSGLTVHELVSYGRFPHQSGFGRLNDEDRRIIKWALEETGMAEYAERPIEALSGGQRQRVWIAMALAQGTELLLLDEPTTYLDLAHQLEILQLLDRLNKEQGRTILMVIHDLNHAARFSHYMIALKKGTVIKEGTALEVMTPDILKQVFQIDAEIVTDPRTNKPVCLTYDLIKNEKELVTV
>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
>TCDB__Q9L177 DesC, component of Desferrioxamine B uptake porter, DesABC (Streptomyces coelicolor)
MRSGEDAAGTPRLRGHELSATGVTVAYDGVDVVHDAGVRLRPGEVTVLVGPNGSGKSTLLRTVARLQRARSATLSLDGATDGLALTSREFSRYVALLTQGRPTPGGLTVRDVVEFGRYPYRGRWGRPDPDGPAAVERALALTGVDGLADRGADHLSGGQLQRVWLASCLAQETGVLLLDEPTTYLDLRYQVELLDLIRDLADDHGIAVGVVLHDLDQAAAVADRITLLEAGRIVADGPPEDVLTPERLTAVYGIRIDVDTDPLTGRLRTRPIGRHHIRTPRTRTPERLGTTS
>SwissProt__O32188 Probable siderophore transport system ATP-binding protein YusV (Bacillus subtilis (strain 168))
MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQVTQDPLFGTPLCIPHGRGRCIVQEAAFTSHG
>SwissProt__Q81LM1 Petrobactin import ATP-binding protein FpuC; EC 7.2.2.- (Bacillus anthracis)
MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLMARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFGRGPHKSWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGVPEEVLCHEMFQHIFGIEVDIFQGSEKPFFTPKRISKKGGAKCEQKNVLPLS
>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__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
>SwissProt__P94420 Petrobactin import ATP-binding protein YclP; EC 7.2.2.- (Bacillus subtilis (strain 168))
MVEVRNVSKQYGGKVVLEETSVTIQKGKITSFIGPNGAGKSTLLSIMSRLIKKDSGEIYIDGQEIGACDSKELAKKMSILKQANQINIRLTIKDLVSFGRFPYSQGRLTEEDWVHINQALSYMKLEDIQDKYLDQLSGGQCQRAFIAMVIAQDTDYIFLDEPLNNLDMKHSVEIMKLLKRLVEELGKTIVIVIHDINFASVYSDYIVALKNGRIVKEGPPEEMIETSVLEEIYDMTIPIQTIDNQRIGVYFS
>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
>SwissProt__Q9HQ18 Cobalamin import ATP-binding protein BtuD; Vitamin B12-transporting ATPase; EC 7.6.2.8 (Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium))
MTLDVTGLDVELAGTRILDDVHASIRDGHLVGVVGPNGAGKSTLLRAMNGLITPTAGTVLVAGDDVHALSSAAASRRIATVPQDASVSFEFTVRQVVEMGRHPHTTRFGTDTDTAVVDRAMARTGVAQFAARDVTSLSGGERQRVLLARALAQAAPVLLLDEPTASLDVNHQIRTLEVVRDLADSEDRAVVAAIHDLDLAARYCDELVVVADGRVHDAGAPRSVLTPDTIRAAFDARVAVGTDPATGAVTVTPLPDRTSAAADTSVHVVGGGDSATPVVRRLVSAGASVSVGPVVEGDTDHETARRVGCPCTSVAPFTRLEDTTAASATRADIAAADVIAVPVAAAARPGVRGLLTGAVPTLAVGDAAGAPEWADRLVACDAVVSAVGALADTPSDGV
>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
>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
>ecocyc__POTA-MONOMER spermidine preferential ABC transporter ATP binding subunit (EC 7.6.2.11; EC 7.6.2.16) (Escherichia coli K-12 substr. MG1655)
MGQSKKLNKQPSSLSPLVQLAGIRKCFDGKEVIPQLDLTINNGEFLTLLGPSGCGKTTVLRLIAGLETVDSGRIMLDNEDITHVPAENRYVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLETFAQRKPHQLSGGQQQRVAIARAVVNKPRLLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAGFIGEINMFNATVIERLDEQRVRANVEGRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDDNHAEGLIGYVRERNYKGMTLESVVELENGKMVMVSEFFNEDDPDFDHSLDQKMAINWVESWEVVLADEEHK
>biolip__6mjpA Lptb(e163q)fgc from vibrio cholerae
AILKAQHLAKSYKKRKVVSDVSLQVESGQIVGLLGPNGAGKTTSFYMIVGLVARDEGTITIDDNDISILPMHSRSRMGIGYLPQEASIFRKLSVEDNIMAVLQTREELTHEERQDKLEDLLEEFHIQHIRKSAGMALSGGERRRVEIARALAANPQFILLDQPFAGVDPISVIDIKKIIEHLRDRGLGVLITDHNVRETLDVCEKAYIVSQGRLIAEGTPQDVLNNEQVKQVYLGEQFRL
>biolip__7chaI Cryo-em structure of p.Aeruginosa mlafebd with amppnp
AYAVELKGLTFKRGSRAIFDNIDVRIPRGKVTGIMGPSGCGKTTLLRLIASQLRPSKGEVWVNGQNLPQLSRGDLFDMRKQFGVLFQSGALFTDLDVFENVAFPLRVHTQLPEEMIRDIVLMKLQAVGLRGAVELMPDELSGGMKRRVALARAIALDPQILLYDEPFVGQDPIAMGVLVRLIRLLNDALGITSIVVSHDLAETASIADYIYIVGDGRVLGHGTPDVLKETDDPRIRQFVKGIPDGPVPFHYPARDYRADLLG
>PDB_6b8b_A E. Coli lptb in complex with adp and a novobiocin derivative
ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIG
YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL
DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY
>PDB_6mhz_A Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter
ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIG
YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL
DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG
>PDB_6s8n_B Cryo-em structure of lptb2fgc in complex with lipopolysaccharide
ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIG
YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL
DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDF
>PDB_6s8g_A Cryo-em structure of lptb2fgc in complex with amp-pnp
ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIG
YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL
DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDF
>PDB_6b89_A E. Coli lptb in complex with adp and novobiocin
ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIG
YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL
DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL
>PDB_4p31_A Crystal structure of a selenomethionine derivative of e. Coli lptb in complex with adp-magensium
ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIG
YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL
DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL
>biolip__6mbnA Lptb e163q in complex with atp
SATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDQPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFRL
>ecocyc__RBSA-MONOMER ribose ABC transporter ATP binding subunit (Escherichia coli K-12 substr. MG1655)
MEALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGTLLWLGKETTFTGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKTMYAEADKLLAKLNLRFKSDKLVGDLSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVASLTEDSLIEMMVGRKLEDQYPHLDKAPGDIRLKVDNLCGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGKLNRVNQE
>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__5l22B Prtd t1ss abc transporter
VLRSYLAKYKKTLIIVGLFSLFINILFLLPSIYMLAVYDIVVPSTSVPTLLVITALAVVLYFALGLLQSVRAKVMQIISLKLDSELNKEVFTSSFEYAIRNPSKASAQPINDLYQLKQFLTSPVLFAIFDLPWVPIYFGVLFVFHVYYGVMAILSMAVIVALAILNEYITKKKLKESNELLVRSTNFLNRALLNAEVVEALGMRNNLYKKWMNFYSKHLSAFEEATDRNNFLSNLTRIFRIMAQSLMLGLGGYLAIKHEITTGMIVAGSILLGRILGPIDTIVNGWRQIGNTKVAYTRLNEFLKFLPEPKGEIELSNVVVVPPEGKTPVLRNINMRILPGEFVAIIGPSGSGKSSLVRTILGIWLPVHGTVEIDGADLKQWDRDYFGKFVGYLPQDIELFEGTVAENIARFGELDSEKIIEAAKLSGAHDVIIKLPDGYDTYIGPGGITLSGGQRQRIALARALYGNPRIVILDEPDSNLDEQGEQALYNALIELKKRKVTTIIVSHRIRLLNLVDKIAIMQDGTLKAFGKADIIIQKLL
>biolip__5d3mA Folate ecf transporter: amppnp bound state
GSDNIISFDHVTFTYPDSPRPALSDLSFAIERGSWTALIGHNGSGKSTVSKLINGLLAPDDLDKSSITVDGVKLGADTVWEVREKVGIVFQNPDNQFVGATVSDDVAFGLENRAVPRPEMLKIVAQAVADVGMADYADSEPSNLSGGQKQRVAIAGILAVKPQVIILDESTSMLDPEGKEQILDLVRKIKEDNNLTVISITHDLEEAAGADQVLVLDDGQLLDQGKPEEIFPKVEMLKRIGLDIPFVYRLKQLLKERGIVLPDEIDDDEKLVQSLWQLNS
>ecocyc__ABC-MONOMER L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) (Escherichia coli K-12 substr. MG1655)
MIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV