>WP_011813608.1 NCBI__GCF_000015585.1:WP_011813608.1
MVDYTASPLLELSNVHCCYGGTTAVYQLSLRVMPGQIACLLGPSGCGKTTTLRAIAGFEPLCNGEIRVRGEPLSVPGYVMPPEKRRMGMVFQDYALFPHLNIYDNITFGLRKLSRRDRRRRADELLELVDLQGYGERFPHELSGGQQQRVSLARAVAPQPQLVLLDEPFSNLDVELRERLSREFHDIFRDQQITAILVTHDQHEAFAMADEIGLMRDGRIVQWDTPFNLYHEPADRFAAEFIGQGSMISGTLIDGERIQTSLGTLRGSHGFPWPAGTRVDVLLRPDDVRMGEAPSGLYGRVVKKAFKGAETLYTLRTPDGVELLALAPSHSDYDVGDDVGLTMDTEHLVAFPADGEVQAAVEQPTRFPVRAVNVG
>TCDB__Q82VN5 Putative iron transport system ATP-binding protein, component of The Fe-hydroxamate-type siderophore uptake porter (transports Fe+3 bound to ferrioxamine, ferrichrome or pyoverdine siderophores) (Nitrosomonas europaea)
MSTLLELDRISHAYGAQVIVNELSFELEKGEIGCLLGPSGCGKTTVLRCIAGFEPIVSGEIRLNEISVSRAGFVLPPEQRRVGMVFQEYALFPHLTVTANVGFGLHRSTKAERAHRVAELLQITGLMEVANRYPHELSGGQQQRVALVRALAPYPDLILLDEPFSNLDVSLREYLGQEIRELLKKLNITAILVTHDQAEAFAVADKIGVMHAGKMMQWGSAHELYHHPANRFIADFIGQGTLIPGKVTHSDKVETELGTLAGNIYHPGHSSREIAGSQVDVLIRPDDVIHDNDSSLRAVVVHKAFRGAQFLYTLRLASGQSVLSLISSHHDHAIGEKIGIRPQTDHIVVFDRVNSQ
>TCDB__P74127 FutC aka SLL1878, component of Ferric iron (Fe3+) porter
MTVAQFSPVARLSIEDSVLTVQDLGKSFRGQSTPVLQKINFNLAPGEILGLLGPSGCGKTTLLRIIAGFETPTSGTVHLEGDCVSGENGLTPPEQRQTGMVFQDYALFPHLTITDNIAFGLRHKSQKLNRQQIQGRVAEVLHLVGLTGLEKRYPHELSGGQQQRIALARALAPKPNLILLDEPLSNLDVQVRQRLRHEIRHILKATGTAAIFVTHDQEEAMAISDRIGVMYRGNLEQIGTPEEIYRSPASRFVAEFVTQANFVPAQRQGTLWATEFGQWPLTFQGIQPELPSVGELMLREEEIELSPASDGPVVIRDRQFLGREYRYCLETPAGRQIHARTSLQTVIPVGSRVNLTPTNPCPPLFAQG
>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
>BRENDA__Q8YM92 ABC-type polyamine transporter (subunit 3/3) (EC 7.6.2.11) (Nostoc sp. PCC 7120 = FACHB-418)
MNMAQTVTQNPRGVKTLLPLDVELRNVFKFFNQEPAVHGVDLDVRQGEFFSILGPSGCGKTTTLRLIAGFEQVDAGKLLIQGQPMTNIPPYRRPVNTVFQSYALFNHLNVWDNVAFGLRLKKSRKSEVESRVKEALKLVKMESLRSRFPSQLSGGQQQRVALARALVNRPAVVLLDEPLGALDLKLRKEMQVELSNLHKNLGLTFVMVTHDQEEALSLSDRIAVMNQGKIEQIGTPQEIYERPKTSFVADFIGDTNLFSGEITVLEAEYIQIVTKTGLTIVVARNEDTPAELLKPVVVSVRPEKIQLSLYPPSSLNNCFEGRLINVMYLGTHVNYVVQLINGMNINVLQPNTFGNLPDRETPIYAWWAESDCLAINQMTND
>TCDB__P44513 FbpC, component of Ferric iron (Fe3+) porter, FbpABC or HitABC (selective for trivalent cations, Fe3+, Ga3+ and Al3+) (Haemophilus influenzae)
MRLNKMINNPLLTVKNLNKFFNEQQVLHDISFSLQRGEILFLLGSSGCGKTTLLRAIAGFEQPSNGEIWLKERLIFGENFNLPTQQRHLGYVVQEGVLFPHLNVYRNIAYGLGNGKGKNSEEKTRIEQIMQLTGIFELADRFPHQLSGGQQQRVALARALAPNPELILLDEPFSALDEHLRQQIRQEMLQALRQSGASAIFVTHDRDESLRYADKIAIIQQGKILQIDTPRTLYWSPNHLETAKFMGESIVLPANLLDENTAQCQLGNIPIKNKSISQNQGRILLRPEQFSLFKTSENPTALFNGQIKQIEFKGKITSIQIEINGYAIWIENVISPDLSIGDNLPVYLHRKGLFYS
>ecocyc__POTG-MONOMER putrescine ABC transporter ATP binding subunit (EC 7.6.2.11; EC 7.6.2.16) (Escherichia coli K-12 substr. MG1655)
MNDAIPRPQAKTRKALTPLLEIRNLTKSYDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPSAGQIMLDGVDLSQVPPYLRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEDGLVLDSPGLVHPLKVDADASVVDNVPVHVALRPEKIMLCEEPPANGCNFAVGEVIHIAYLGDLSVYHVRLKSGQMISAQLQNAHRHRKGLPTWGDEVRLCWEVDSCVVLTV
>TCDB__O54370 BitD, component of The iron transporter, BitABCDEF (Treponema hyodysenteriae (Serpulina hyodysenteriae))
MSVSISIENVVKRYEKLTIIPDLSLEIKNGEFFTLLGPSGCGKTTLLRMIAGFNTIEGGEIKFDKDVINNIPAHKRNIGMVFQNYAIFPHMTVRENVEYGLKLRKENKESMKKKVDEMLHVVKIEEYQDRLPERLSGGQQQRVALARAIVITPSVLLMDEPLSNLDAKLRIEMRSAIKDIQRHVGITTVYVTHDQEEALAVSDRIAVMKNGVIQQVGSPVSIYTRPYNVFVATFIGHSNLFYATIKIEGNDTYLLFRCGYKLKMDNLLDVKDGDEVVVGIRPEEFFVNSENDEGIKAKILSKTFLGKYTNYFLHFNDNEVVPDQPSIEYSQDSSYTDRMYEKDEVITLKPNANKINVFTPDMEKSLIKGVKKYE
>TCDB__Q9KLQ5 Fe(3+) ions import ATP-binding protein FbpC, component of Hexose-phosphate transporter (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961))
MEKQNFVVLKNICKRFGSNTVIGNLDLEIKKGSLVTLLGPSGCGKTTVLRLVAGLEKPTSGQIFIDGEDVTERSIQQRDICMVFQSYALFPHMSLYENVAYGLKMLKLPSEEVRQRVDEALKIVDLEGMGERYVDQISGGQQQRVALARALVLKPKVLLFDEPLSNLDANLRRSMRETIRELQQRFDITSLYVTHDQAEAFAVSDTVIVMKQGDIMQIGTPQELYKAPKSMFMANFMGEANMFQGHFDGQQIHINGYAIDADLEVTRDKPNGEYQIGVRPEAITLHTQGSESQACQILKSAYMGSMYEVTVKWHDQELLLQLNSAQFNHTLTQHAYVVFNPRGLFLLPYAE
>ecocyc__CYSA-MONOMER sulfate/thiosulfate ABC transporter ATP binding subunit (EC 7.3.2.3; EC 7.3.2.5) (Escherichia coli K-12 substr. MG1655)
MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTKLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDQVWREPATRFVLEFMGEVNRLQGTIRGGQFHVGAHRWPLGYTPAYQGPVDLFLRPWEVDISRRTSLDSPLPVQVLEASPKGHYTQLVVQPLGWYNEPLTVVMHGDDAPQRGERLFVGLQHARLYNGDERIETRDEELALAQSA
>TCDB__Q72L52 Sugar-binding transport ATP-binding protein aka MalK1 aka TT_C0211, component of The trehalose/maltose/sucrose/palatinose porter (TTC1627-9) plus MalK1 (ABC protein, shared with 3.A.1.1.24) (Silva et al. 2005; Chevance et al., 2006). The receptor (TTC1627) binds disaccharide alpha-glycosides, namely trehalose (alpha-1,1), sucrose (alpha-1,2), maltose (alpha-1,4), palatinose (alpha-1,6) and glucose (Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039))
MAKVRLEHVWKRFGKVVAVKDFNLETEDGEFVVFVGPSGCGKTTTLRMIAGLEEISEGNIYIGDRLVNDVPPKDRDIAMVFQNYALYPHMNVYENMAFGLRLRRYPKDEIDRRVKEAARILKIEHLLNRKPRELSGGQRQRVAMGRAIVREPKVFLMDEPLSNLDAKLRVEMRAEIAKLQRRLGVTTIYVTHDQVEAMTLGHRIVVMKDGEIQQVDTPLNLYDFPANRFVAGFIGSPSMNFVRAGVEVQGEKVYLVAPGFRIRANAVLGSALKPYAGKEVWLGVRPEHLGLKGYTTIPEEENVLRGEVEVVEPLGAETEIHVAVNGTLLVAKVDGHAPVKPGDKVELLADTQRLHAFDLETDRTIGHAQERAAVAR
>TCDB__Q97Q42 Spermidine/putrescine import ATP-binding protein PotA, component of The spermidine/putrescine uptake porter, PotABCD (Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4))
MKKPIIEFKNVSKVFEDSNTKVLKDINFELEEGKFYTLLGASGSGKSTILNIIAGLLDATTGDIMLDGVRINDIPTNKRDVHTVFQSYALFPHMNVFENVAFPLRLRKIDKKEIEQRVAEVLKMVQLEGYEKRSIRKLSGGQRQRVAIARAIINQPRVVLLDEPLSALDLKLRTDMQYELRELQQRLGITFVFVTHDQEEALAMSDWIFVMNDGEIVQSGTPVDIYDEPINHFVATFIGESNILPGTMIEDYLVEFNGKRFEAVDGGMKPNEPVEVVIRPEDLRITLPEEGKLQVKVDTQLFRGVHYEIIAYDELGNEWMIHSTRKAIVGEEIGLDFEPEDIHIMRLNETEEEFDARIEEYVEIEEQEAGLINAIEEERDEENKL
>TCDB__Q1M7Q1 Putative ABC transporter component, component of The γ-aminobutyrate (GABA) uptake system, GtsABCD (Rhizobium leguminosarum bv. viciae (strain 3841))
MKEPFLQIRGIRKEYGPVVAVHDVNLDVRRGEFLTFLGPSGSGKSTTLYILAGFETPTKGDITLEGKTLLATPSHKRNIGMVFQRYTLFPHLTVGENIAFPLKVRRKSKAEVDSKVKEMLRLVRLEGFEDRKPAQMSGGQQQRVALARALAYDPPVLLMDEPLSALDKKLREEIQHEIRRIHQQTEVTILYVTHDQEEALRLSDRIAVFSKGVIDQIGTGPELYANPRTRFVAEFIGDSDFISCDLLSSSDGQATISLGGGSVFNHIPVHGKGTSGTRAALMLRPERIRLSRNQAAGAGLAATVSDITFLGNNIHVSTETATGEALAVRLPFGHEAIAGLSRGDIVHLNFDPGAAHVFC
>BRENDA__A0A142UTH4 ABC-type polyamine transporter (subunit 4/4) (EC 7.6.2.11) (Streptococcus suis)
MKKPIIEFKNVSKVFEDSGTTVLKDISFELEEGKFYTLLGASGSGKSTILNIIAGLLDASSGDIYLDGQRINDVPTNKRDVHTVFQSYALFPHMTVFENVAFPLKLRKIDKAEIERRVTEALQMVRLSGYENRSIQKLSGGQRQRVAIARAIINQPRVVLLDEPLSALDLKLRTEMQYELRELQQRLGITFVFVTHDQEEALAMSDWIFVMNEGEIVQSGTPVDIYDEPINHFVATFIGESNILPGRMIEDYLVEFNGKRFEAVDGGMRPNEEVEVVIRPEDLQITLPEEGKLQVKVDTQLFRGVHYEIIAYDDLGNEWMIHSTRKAIVGEVIGLSFEPEDIHIMRLNETEEEFDARIEEYVEVEEVEDGLINAIEEERNEENL
>biolip__2d62A Crystal structure of multiple sugar binding transport atp- binding protein
MIGMAEVKLINIWKRFGDVTAVKDLSLEIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTRGQIYIEDNLVADPEKGVFVPPKERDVAMVFQSYALYPHMTVYDNIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIIRRPKVFLMDEPLSNLDAKLRVKMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNKGELQQVGTPDEVYYKPVNTFVAGFIGSPPMNFLDATITDDGFLDFGEFKLKLLQDQFEVLEEENMVGKEVIFGIRPEDVHDASFTHIDVPEENTVKATVDIIENLGGEKIVHLRRGNISFTAKFPKESKVREGDEVSVVFDMKKIHIFRKDTEKAIF
>TCDB__A3N296 Ferric ABC transporter ATP-binding protein, component of Iron (Fe3+) uptake porter, AfuABC (FbpABC) (Chin et al. 1996). AfuA has been characterized (Actinobacillus pleuropneumoniae serotype 5b (strain L20))
MNNDFLVLKNITKSFGKATVIDNLDLVIKRGTMVTLLGPSGCGKTTVLRLVAGLENPTSGQIFIDGEDVTKSSIQNRDICIVFQSYALFPHMSIGDNVGYGLRMQGVSNEERKQRVKEALELVDLAGFADRFVDQISGGQQQRVALARALVLKPKVLLFDEPLSNLDANLRRSMREKIRELQQRLGITSLYVTHDQTEAFAVSDEVIVMNKGKIMQKAPAKDLYLRPNSLFLANFMGESTIFDGNLNQGTVSIGDYRFPLHNAADFSVADGACLVGVRPEAIRLTATGETSQRCQIKSAVYMGNHWEIVANWNGKDVLINANPDQFDPDATKAFIHFTEQGIFLLNKE
>ecocyc__YDCT-MONOMER putative ABC transporter ATP-binding protein YdcT (Escherichia coli K-12 substr. MG1655)
MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAEKLCGMTGSFALRPEHIRLNTPGELQANGTIQAVQYQGAATRFELKLNGGEKLLVSQANMTGEELPATLTPGQQVMVSWSRDVMVPLVEER
>TCDB__A1JLH0 Iron(III)-transport ATP-binding protein, component of Siderophore-independent iron uptake system, AfuABC (Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081))
MSTLELQQIGKSYQSVRVLEGIDLQVTAGSRTAIVGPSGSGKTTLLRIIAGFETPDSGKVILQGNPLFDQSTHVPAHKRGIGFVPQDGALFPHFTVAGNIAYGLKGSKQDKARRIDKLMEMVALDRRLAQLWPHEISGGQQQRVALARALAQSPVLMLLDEPFSALDTALRASTRKAVAELLSQANIASILVTHDQSEALSFADQVAVMRAGKLAHVGAPQELYLRPIDEPTATFLGETLILSANIEAEWADCALGRVKVDDATRQGQARIMLRPEQVTITPLPSAHHYPTHCLAKIVSIDFAGFISTLTLSIIEHNEIVAIKTISREGIHVGLMVDLTIMGQAHIFVE
>reanno__acidovorax_3H11_Ac3H11_2941 ABC transporter for D-Sorbitol, ATPase component (Acidovorax sp. GW101-3H11)
MAYLQLRGIEKFFGEHRAIKGIDLTIQQGEFIVFVGPSGCGKSTLLRLIAGLEAIDGGSLMLDGRDITDQPSSKRDLAMVFQSYALYPHMSVYENMSFALKLAKVDKQVIDEKVQNAARILNLTQYLQRTPKELSGGQRQRVAIGRAIVRAPKVFLFDEPLSNLDAALRGQTRVEIAKLHRDLGATTIYVTHDQVEAMTLADRVVVLRDGIIEQVGTPLELYDKPANQFVAQFIGTPQMNVVPVDKLPQPVQQQAPAAPAGAAVGAIGLRPENITVRTTGATPVGGQVDLIEALGAETLIYVTTPGGAQFVSRQNDRTDLRVGDAVSLDIDASQAHWFDTAGRVVAGHAA
>reanno__Phaeo_GFF2754 N-Acetyl-D-glucosamine ABC transport system, ATPase component (Phaeobacter inhibens BS107)
MTALQLTNVCKSFGPVEVLKDINLTVEDGEFVVFVGPSGCGKSTLLRVISGLEDATAGEISIGGQTVTTTPPAKRGIAMVFQSYALYPHLSVRENMALALKQERQPKEEIAARVAEASRMLSLEDYLDRRPSELSGGQRQRVAIGRAVVREPKLFLFDEPLSNLDAALRMNTRLEIARLHRQLSASMIYVTHDQIEAMTLADKIVVLRDGRIEQVGTPMELYNNPANRFVAEFIGAPAMNFVPAQRLGGNPGQFIGIRPEYARISPVGPLAGEVIHVEKLGGDTNILVDMGEDLTFTARLFGQHDTNVGETLQFDFDPANCLSFDEAGQRI
>reanno__pseudo1_N1B4_Pf1N1B4_5115 sucrose ABC transporter, ATPase component (Pseudomonas fluorescens FW300-N1B4)
VIKLKLDNVNKQLGGMRILRDVSLEIAAGEFVVFVGPSGCGKSTLLRLIAGLDSICGGDLLIDGRRVNDLEPRERGVGMVFQSYALYPHMSVYDNISFGLKLAKTDKTSLRERVLKTAQILQLDKLLQRKPKELSGGQRQRVAMGRAMAREPDILLFDEPLSNLDASLRVQMRNEIARLHDRLGSTMIYVTHDQVEAMTLADKIVVLNGGRVEQVGSPRELYERPASRFVAGFLGSPRMNFLSARLQTPGETSLVDTLVWGITSLPFDSSNLAAGTPLSLGIRPEHVSLKAADGTAGVVVTAVEYLGSETYVHLETGQDEPLICRCEVSAGWQAGDRVELLLDLDNLHLFDADGVALSRHPHAIETLPAGVPLRSARASAL
>TCDB__Q9KWT9 AlgS, component of Alginate (MW 27,000 Da) (and Alginate oligosaccharides) uptake porter. Sphingomonas species A1 is a 'pit-forming' bacterium that directly incorporates alginate into its cytoplasm through a pit-dependent transport system, termed a 'superchannel' (Murata et al., 2008). The pit is a novel organ acquired through the fluidity and reconstitution of cell surface molecules, and through cooperation with the transport machinery in the cells. It confers upon bacterial cells a more efficient way to secure and assimilate macromolecules (Sphingomonas sp)
MVASVSIQNVVKRYDKTTVVHGVSLDIEPGEFVVLVGPSGCGKSTTLRMVAGLEEISGGTIRIDGRVINDLAPKDRDVAMVFQNYALYPHLNVRDNISFGLRLKRTKKSVIDAAVKTAADILGLQPLLERKPSDLSGGQRQRVAMGRAIVRDPKVFLFDEPLSNLDAKLRTQMRAEIKRLHQRLGTTVIYVTHDQVEAMTLADRIVVMRDGLIEQIGKPMDLFLHPANTFVASFIGSPPMNLMPARIAVDSTQHVELNGGNRISLLPRAGTHLAPGQEVVFGIRPEDVTLDGVEGSERAQIKATVDIVEPLGSESILHATVGDHSLVVKVGGLNEVHPGDPVTLHVDLTRVHLFDAQSQASIY
>reanno__HerbieS_HSERO_RS17020 ABC transporter for D-sorbitol/xylitol, ATPase component (Herbaspirillum seropedicae SmR1)
MADIHCQALAKHYAGGPPVLHPLDLHIGDGEFVVLLGPSGCGKSTMLRMIAGLEDISGGTLRIGGTVVNDLPARERNVAMVFQNYALYPHMSVYDNIAFGLRRLKRPAAEIDRRVREVAALLNLEALLERKPRAMSGGQQQRAAIARAIIKTPSVFLFDEPLSNLDAKLRAQLRGDIKRLHQRLRTTTVYVTHDQLEAMTLADRVILMQDGRIVQAGSPAELYRYPRNLFAAGFIGTPAMNFLSGTVQRQDGQLFIETAHQRWALTGERFSRLRHAMAVKLAVRPDHVRIAGEREPAASLTCPVSVELVEILGADALLTTRCGDQTLTALVPADRLPQPGATLTLALDQHELHVFDVESGENLSLPDAALTAPGSDDGPHGKETKHESGSGAGPYPPGPIVQGLGA
>biolip__3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp
TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRAALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIVFPAALNADGTADCRLGRLPVQSGAPAGTRGTLLIRPEQYSLHPHSAPAASIHAVVLKTTPKARHTEISLRAGQTVLTLNLPSAPTLSDGISAVLHLDGPALFFPGNT
>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
>biolip__2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS
>ecocyc__MALK-MONOMER maltose ABC transporter ATP binding subunit (EC 7.5.2.1) (Escherichia coli K-12 substr. MG1655)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV
>PDB_3puy_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_3pux_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_3puw_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_3puv_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_1q12_A Crystal structure of the atp-bound e. Coli malk
VQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS
YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN
LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLP
VKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSI
RQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPG
>metacyc__G185E-5409-MONOMER ABC-type trehalose transporter ATP-binding protein (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MAEIVLDHVNKSYPDGHTAVRDLNLTIADGEFLILVGPSGCGKTTTLNMIAGLEDISSGELRIAGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKMRKADIAQKVSETAKILDLTNLLDRKPSQLSGGQRQRVAMGRAIVRHPKAFLMDEPLSNLDAKLRVQMRGEIAQLQRRLGTTTVYVTHDQTEAMTLGDRVVVMYGGIAQQIGTPEELYERPANLFVAGFIGSPAMNFFPARLTAIGLTLPFGEVTLAPEVQGVIAAHPKPENVIVGVRPEHIQDAALIDAYQRIRALTFQVKVNLVESLGADKYLYFTTESPAVHSVQLDELAEVEGESALHENQFVARVPAESKVAIGQSVELAFDTARLAVFDADSGANLTIPHRA
>biolip__1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp
VIKMVEVKLENLTKRFGNFTAVNKLNLTIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTEGRIYFGDRDVTYLPPKDRNISMVFQHMTVYENIAFPLKKFPKDEIDKRVRWAAELLQIEELLNRYPAQLSGGQRQRVAVARAIVVEPDVLLMDEPLSNLDAKLRVAMRAEIKKLQQKLKVTTIYVTHDQVEAMTMGDRIAVMNRGQLLQIGSPTEVYLRPNSVFVATFIGAPEMNILEVSVGDGYLEGRGFRIELPQMDLLKDYVGKTVLFGIRPEHMTVEGVHMKRTARLIGKVDFVEALGTDTILHVKFGDELVKVKLPGHIPIEPGREVKVIMDLDMIHVFDKDTEKAIV
>PDB_8hpr_D Lpqy-sugabc in state 4
AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV
FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP
LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN
FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH
FTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>BRENDA__Q8TTZ3 ABC-type molybdate transporter (EC 7.3.2.5) (Methanosarcina acetivorans)
MIEIESLSRKWKNFSLDNLSLKVESGEYFVILGPTGAGKTLFLELIAGFHVPDSGRILLDGKDVTDLSPEKHDIAFVYQNYSLFPHMNVKKNLEFGMRMKKIKDPKRVLDTARDLKIEHLLDRNPLTLSGGEQQRVALARALVTNPKILLLDEPLSALDPRTQENAREMLSVLHKKNKLTVLHITHDQTEARIMADRIAVVMDGKLIQVGKPEEIFEKPVEGRVASFVGFENVLKGRVISAEQGLLRIRVGEVVIDAAGDMEVGDQVYAFLRPENIALSKSSTQSSIRNSLQGRVTEAWVLGALVRVKVDCGVPLNVLITRRSAEEMELSPGVQIYARFKASSVHVLR
>biolip__2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS
>biolip__2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALEVINQRVNQVAEVLAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVAS