>SMa1754 FitnessBrowser__Smeli:SMa1754
MESSVAEFIQFDRITKFYGPLCVVENLVLGIGQGEFVSLLGPSGSGKTTLLMMLAGFEQPTSGNILLDGTAINDVPTHKRDMGVVFQSYALFPHMSVGENVAFPLQMRGLGKAEIAECVARALDMVQLSAFADRRPSQLSGGQQQRVALSRALVFEPRVVLMDEPLGALDKQLREQMQFDIRDLHRRLGLTIVFVTHDQSEALTMSDRVAVFNRGKIEQIGTPRQVYDEPATRFVAEFIGETNLVEGVVETVQGQEAIVRLPSGAHIVSAGSGSLVSGQSVFLSIRPERVDLSETRGDARNCLETEVTDSVYQGDHLRVQLQSAAHPLIAKLGRRSREFPPGTKVYAAFSANDCRVIAP
>TCDB__Q1M7Q1 Putative ABC transporter component, component of The γ-aminobutyrate (GABA) uptake system, GtsABCD (Rhizobium leguminosarum bv. viciae (strain 3841))
MKEPFLQIRGIRKEYGPVVAVHDVNLDVRRGEFLTFLGPSGSGKSTTLYILAGFETPTKGDITLEGKTLLATPSHKRNIGMVFQRYTLFPHLTVGENIAFPLKVRRKSKAEVDSKVKEMLRLVRLEGFEDRKPAQMSGGQQQRVALARALAYDPPVLLMDEPLSALDKKLREEIQHEIRRIHQQTEVTILYVTHDQEEALRLSDRIAVFSKGVIDQIGTGPELYANPRTRFVAEFIGDSDFISCDLLSSSDGQATISLGGGSVFNHIPVHGKGTSGTRAALMLRPERIRLSRNQAAGAGLAATVSDITFLGNNIHVSTETATGEALAVRLPFGHEAIAGLSRGDIVHLNFDPGAAHVFC
>BRENDA__Q8YM92 ABC-type polyamine transporter (subunit 3/3) (EC 7.6.2.11) (Nostoc sp. PCC 7120 = FACHB-418)
MNMAQTVTQNPRGVKTLLPLDVELRNVFKFFNQEPAVHGVDLDVRQGEFFSILGPSGCGKTTTLRLIAGFEQVDAGKLLIQGQPMTNIPPYRRPVNTVFQSYALFNHLNVWDNVAFGLRLKKSRKSEVESRVKEALKLVKMESLRSRFPSQLSGGQQQRVALARALVNRPAVVLLDEPLGALDLKLRKEMQVELSNLHKNLGLTFVMVTHDQEEALSLSDRIAVMNQGKIEQIGTPQEIYERPKTSFVADFIGDTNLFSGEITVLEAEYIQIVTKTGLTIVVARNEDTPAELLKPVVVSVRPEKIQLSLYPPSSLNNCFEGRLINVMYLGTHVNYVVQLINGMNINVLQPNTFGNLPDRETPIYAWWAESDCLAINQMTND
>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
>BRENDA__A0A142UTH4 ABC-type polyamine transporter (subunit 4/4) (EC 7.6.2.11) (Streptococcus suis)
MKKPIIEFKNVSKVFEDSGTTVLKDISFELEEGKFYTLLGASGSGKSTILNIIAGLLDASSGDIYLDGQRINDVPTNKRDVHTVFQSYALFPHMTVFENVAFPLKLRKIDKAEIERRVTEALQMVRLSGYENRSIQKLSGGQRQRVAIARAIINQPRVVLLDEPLSALDLKLRTEMQYELRELQQRLGITFVFVTHDQEEALAMSDWIFVMNEGEIVQSGTPVDIYDEPINHFVATFIGESNILPGRMIEDYLVEFNGKRFEAVDGGMRPNEEVEVVIRPEDLQITLPEEGKLQVKVDTQLFRGVHYEIIAYDDLGNEWMIHSTRKAIVGEVIGLSFEPEDIHIMRLNETEEEFDARIEEYVEVEEVEDGLINAIEEERNEENL
>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
>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
>ecocyc__YDCT-MONOMER putative ABC transporter ATP-binding protein YdcT (Escherichia coli K-12 substr. MG1655)
MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAEKLCGMTGSFALRPEHIRLNTPGELQANGTIQAVQYQGAATRFELKLNGGEKLLVSQANMTGEELPATLTPGQQVMVSWSRDVMVPLVEER
>TCDB__Q9AI63 PalK, component of Palatinose (isomaltulose; 6-O-α-D-glucopyranosyl-D-fructose) uptake porter (Erwinia rhapontici)
MAQLTLDKIQKRYGAKAEVIRSLNLQIKSGEFVVIVGPSGCGKSTLLRMIAGLEEISGGGMYIDGHYANDDSPAERGIGMVFQSYALYPHMSVYQNMAFALELAHCSKAEIDQRVRECARILQLEPLLERRPKDLSGGQRQRVAIGRAIIREPRLFLFDEPLSNLDASLRVQMRMEVSALHKRLGVTIIYVTHDQVEAMTLADRIVVLNQGNIEQVGTPLELYDQPANEFVAQFIGSPKMNLIPATLRRSGEQQSVVELDNGKTLVLSIATPAEAEGRSVNIGIRPEHIRSGNVEQCEYQGEVMFVEQMGNETLLYLDNGNAGEPWVVRHAERSAIHVGQTVGVRLPVECCYLFDSHGQAFQRHLAKVH
>TCDB__Q9WYQ2 Glycerol-3-phosphate-transporting ATPase, component of Inositol phosphate porter (Rodionova et al. 2013). Binds inositol phosphate with low Kd and inositol with a lower affinity (Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099))
MPSIRVVNLKKYFGKVKAVDGVSFEVKDGEFVALLGPSGCGKTTTLLMLAGIYKPTSGEIYFDDVLVNDIPPKYREVGMVFQNYALYPHMTVFENIAFPLRARRISKDEVEKRVVEIARKLLIDNLLDRKPTQLSGGQQQRVALARALVKQPKVLLFDEPLSNLDANLRMIMRAEIKHLQQELGITSVYVTHDQAEAMTMASRIAVFNQGKLVQYGTPDEVYDSPKNMFVASFIGNPPTNFLRDFSVSVENKQTILKRDDVIIKLPEPVDVKLKEVVVGIRPEHCRISRERVENSIPGVVYVVEPLGRDIIVNVKTEKGEIIKVFGDTGKAPQPGENVFLVPDLRKIHLFNPETEETIL
>TCDB__O50559 ChtG, component of Chrysopine porter (Agrobacterium sp)
FALLGSSGSGKTTLLMLLAGFDQPSEGKVLMSGTSVTEVPPHRRSIGVVFQNYALFPHMTAAENVAYPLKMRGVGRSERDERVKAALSLVNLTDRGASYPIQMSGGQQQRVALARSLVFGPDILLMDEPLGALDRRLRDQMQHELKRIQHELGITVIYVTHDQSEAMAMADRIGIMSGGELLQVADPETIYAAPSNHFVARFIGDCSILRVTNLDEGRGYEIAGGRQLLPSPAKTPFDIVVRPESVSIRSVAEANSDEGFAVPATIRDITYLGSGWRVALQISDGQSLLANVMRGDLLAGSLEPGKSVIARWAPASVAVLPTEG
>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
>TCDB__Q44383 MotB, component of Mannopine porter (Agrobacterium tumefaciens)
MIRIKGELVSLAGMKMRSRSDRGPNMQNQPEPAINKLQPSSLPISIAGVTKSYGPVKVLSDINLHIRSGEFMTLLGPSGSGKTTLLMTLAGFIRPDFGSLKFGEEEVILRAPHLRGVGMMFQNYALFPHMSVEANIAYPLKIRGEDRETIKARVRDVLETVQLGGYGSRRISELSGGQRQRIALARAIVFKPKILLMDEPLSALDKNLRELMQLELRTMHEQLGMTTVLVTHDQREALTMSDRIAVLRNGKIAQIDTSETLYSEPNSEFVAAFMGESSFLTVEHDGASFCFHGRKLATESVTVEGARRHLLVLRPEKLDFITERERSSYNSFDGIVEKFLFQGESCLVHVRLTTGELVQVRRNLRESNKSVLPKVNDQVLLGLHPNETRIVTGE
>ecocyc__YAGC-MONOMER CP4-6 prophage; ABC transporter ATP-binding protein AfuC (Escherichia coli K-12 substr. MG1655)
MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATFSDGYVDIYGYHLPRPLHFGTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILLQVNATRLQPDVGEQYYLEIHPYGMFVLADAA
>TCDB__O54370 BitD, component of The iron transporter, BitABCDEF (Treponema hyodysenteriae (Serpulina hyodysenteriae))
MSVSISIENVVKRYEKLTIIPDLSLEIKNGEFFTLLGPSGCGKTTLLRMIAGFNTIEGGEIKFDKDVINNIPAHKRNIGMVFQNYAIFPHMTVRENVEYGLKLRKENKESMKKKVDEMLHVVKIEEYQDRLPERLSGGQQQRVALARAIVITPSVLLMDEPLSNLDAKLRIEMRSAIKDIQRHVGITTVYVTHDQEEALAVSDRIAVMKNGVIQQVGSPVSIYTRPYNVFVATFIGHSNLFYATIKIEGNDTYLLFRCGYKLKMDNLLDVKDGDEVVVGIRPEEFFVNSENDEGIKAKILSKTFLGKYTNYFLHFNDNEVVPDQPSIEYSQDSSYTDRMYEKDEVITLKPNANKINVFTPDMEKSLIKGVKKYE
>reanno__Smeli_SM_b20002 ABC transporter for Lactose, ATPase component (Sinorhizobium meliloti 1021)
MSELQLSDVRKSYGGLEVIKGVDLDIKSGEFVVFVGPSGCGKSTLLRMIAGLEEISSGDLTIDDVRMNDVDPSKRGIAMVFQSYALYPHMTVRENMGFALRFAGVPRAEIEKRVNEAAHILELGALLDRKPKQLSGGQRQRVAIGRAIVRHPKIFLFDEPLSNLDAELRVHMRIEIARLHKQLATTIVYVTHDQVEAMTLADKIVVMRAGVVEQVGSPLDLYDDPANLFVAGFIGSPKMNFLKGVIEIDEDQAYARLPDYGDAKIPVTLQAAAGTAVTIGIRPEHFDEAGPAALDLAIDMLEHLGGETFAYARHHGNGELIVVETKNGRGLKTGDRLTARFDPVSVLVFDGEGKRLRS
>reanno__Koxy_BWI76_RS01840 maltose ABC transporter, ATPase component (MalK) (Klebsiella michiganensis M5al)
MASVQLRNVTKAWGDVVVSKDINLEIQDGEFVVFVGPSGCGKSTLLRMIAGLETVTSGDLLIGDTRMNDVPPAERGIGMVFQSYALYPHLSVAENMSFGLKLAGAKKELINQRVTQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQVWLPVDSARVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV
>reanno__pseudo1_N1B4_Pf1N1B4_5115 sucrose ABC transporter, ATPase component (Pseudomonas fluorescens FW300-N1B4)
VIKLKLDNVNKQLGGMRILRDVSLEIAAGEFVVFVGPSGCGKSTLLRLIAGLDSICGGDLLIDGRRVNDLEPRERGVGMVFQSYALYPHMSVYDNISFGLKLAKTDKTSLRERVLKTAQILQLDKLLQRKPKELSGGQRQRVAMGRAMAREPDILLFDEPLSNLDASLRVQMRNEIARLHDRLGSTMIYVTHDQVEAMTLADKIVVLNGGRVEQVGSPRELYERPASRFVAGFLGSPRMNFLSARLQTPGETSLVDTLVWGITSLPFDSSNLAAGTPLSLGIRPEHVSLKAADGTAGVVVTAVEYLGSETYVHLETGQDEPLICRCEVSAGWQAGDRVELLLDLDNLHLFDADGVALSRHPHAIETLPAGVPLRSARASAL
>TCDB__O32151 Uncharacterized ABC transporter ATP-binding protein YurJ, component of The arabinosaccharide transporter AraNPQMsmX. Transports α-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units; the key transporter for α-1,5-arabinotriose and α-1,5-arabinotetraose, but not for α-1,5-arabinobiose which is transported by AraE. MsmX is also used by the MdxEFG-MsmX system (3.A.1.1.36) (Ferreira and Sá-Nogueira, 2010). Involved in the uptake of pectin oligosaccharides with either MsmX or YurJ as the ATPase (Bacillus subtilis (strain 168))
MASLTFEHVKKSYHSQLTVKDFDLDVKDKELLVLVGPSGCGKSTTLRMVAGLESISEGNLLIDGERVNDLPPKERDIAMVFQNYALYPHMTVFDNMAFGLKLRKMAKQEIAERVHAAARILEIEHLLKRKPKALSGGQRQRVALGRSIVREPKVFLMDEPLSNLDAKLRVTMRTEISKLHQRLEATIIYVTHDQTEAMTMGDRIVVMNEGEIQQVAKPHDIYHYPANLFVAGFIGSPGMNFLKGIIEQQHGELFFTNSSIRLHIPEEKAKRLKEKGYAGEQMIAGVRPEHITQMTGNDQLFDSVFQANVEVNENLGSELIVHVMAGDERLKVRLDGNTRIDAGDSIQLSVKMDHVVFFDAETEEAVY
>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
>SwissProt__P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MASVQLRNVTKAWGDVVVSKDINLDIHDGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGETRMNDIPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVMNQRVNQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQIWLPVESRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGSACRRLHQEPGV
>BRENDA__B9J850 pterin deaminase (EC 3.5.4.11) (Agrobacterium tumefaciens)
MAGINIKSVTKHFGAVQVLNDIDLTIEPGEFVVFLGGSGCGKSTLLRMIAGLEAITSGEVWIGGRRVDQLPPGERGVSMVFQSYALYPHMTVRDNMSFGLRNIGTPKAEIAKRIDIAATILEMPHLLDRKPSELSGGQRQRVAIGRAIVREPDVFLFDEPLSNLDAGLRNRTRVELAQLHERLGATMVFVTHDQIEAMTLADRIVLLNNKKIEQVATPVEIYTRPATRYVAQFIGSPGMNFVNVAGVGEAGGFATATLPDGSIIKTAVSVNGMARSELTLGIRPEYLVATTADKGDIAGTVETVERLGDRSLVHVRLKDGSKIIGTDPGMTSITSGAPIAFAVDGAKLTIFDQNDVAHHAAH
>BRENDA__Q70HW1 ABC-type maltose transporter (EC 7.5.2.1) (Alicyclobacillus acidocaldarius)
MARVLLEHIYKTYPGQTEPTVKDFNLDIQDKEFTVFVGPSGCGKTTTLRMIAGLEDITEGNLYIGDRRVNDVPPKDRDIAMVFQNYALYPHMTVYQNMAFGLKLRKVPKAEIDRRVQEAAKILDIAHLLDRKPKALSGGQRQRVALGRAIVREPQVFLMDEPLSNLDAKLRVQMRAEIRKLHQRLQTTVIYVTHDQTEAMTMGDRIVVMRDGVIQQADTPQVVYSQPKNMFVAGFIGSPAMNFIRGEIVQDGDAFYFRAPSISLRLPEGRYGVLKASGAIGKPVVLGVRPEDLHDEEVFMTTYPDSVLQMQVEVVEHMGSEVYLHTSIGPNTIVARVNPRHVYHVGSSVKLAIDLNKIHIFDAETEESIGFAAGPAGERQEALV
>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
>ecocyc__UGPC-MONOMER <i>sn</i>-glycerol 3-phosphate ABC transporter ATP binding subunit (EC 7.6.2.10) (Escherichia coli K-12 substr. MG1655)
MAGLKLQAVTKSWDGKTQVIKPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTEGDIWINDQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKQQIAERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNGGVAEQIGTPVEVYEKPASLFVASFIGSPAMNLLTGRVNNEGTHFELDGGIELPLNGGYRQYAGRKMTLGIRPEHIALSSQAEGGVPMVMDTLEILGADNLAHGRWGEQKLVVRLAHQERPTAGSTLWLHLAENQLHLFDGETGQRV
>reanno__pseudo6_N2E2_Pf6N2E2_1960 ABC transporter for D-sorbitol, ATPase component (Pseudomonas fluorescens FW300-N2E2)
MATLKIENLKKGFEGLSIIKGIDLEVKDKEFVVFVGPSGCGKSTLLRLIAGLEDVTSGTIELDGRDITEVTPAKRDLAMVFQTYALYPHMTVRKNLSFALDLAGEKKPDVERKVAEAARILELGSLLDRKPKQLSGGQRQRVAIGRAIVRNPKIFLFDEPLSNLDAALRVQTRLELSRLHKELQATMIYVTHDQVEAMTLATKVVVLNAGRIEQIGSPLELYHHPANLFVAGFLGTPKMGFLQATVHAVHASGVEVRFASGTTLLIPRDSSALSVGQSVTIGIRPEHLTLSAEGQVPVTTDVTERLGSDTFCHVNVDSGESLTVRVQGDCEVPYAARRYLTLDVAHCHLFDESGLSVSPAASRAA
>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
>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__BFirm_BPHYT_RS16095 ABC transporter for D-Sorbitol, ATPase component (Burkholderia phytofirmans PsJN)
MASVTLRNIRKAYDENEVMRDINLDIADGEFVVFVGPSGCGKSTLMRMIAGLEDISGGDLTIDGMRVNDVAPAKRGIAMVFQSYALYPHMTLYDNMAFGLKLAGTKKPEIDAAVRNAAKILHIDHLLDRKPKQLSGGQRQRVAIGRAITRKPKVFLFDEPLSNLDAALRVKMRLEFARLHDELKTTMIYVTHDQVEAMTLADKIVVLSAGNLEQVGSPTMLYHAPANRFVAGFIGSPKMNFMEGVVQSVTHDGVTVRYETGETQRVAVEPAAVKQGDKVTVGIRPEHLHVGMAEDGISARTMAVESLGDAAYLYAESSVAPDGLIARIPPLERHTKGETQKLGATPEHCHLFDSAGKAFQRKIVEVLAA
>TCDB__Q8DT25 MalK, component of Maltose/Maltotriose/maltodextrin (up to 7 glucose units) transporters MalXFGK (MsmK (3.A.1.1.28) can probably substitute for MalK; Webb et al., 2008) (Streptococcus mutans)
MTTLKLDNIYKRYPNAKHYSVENFNLDIHDKEFIVFVGPSGCGKSTTLRMIAGLEDITEGNLYIDDKLMNDASPKDRDIAMVFQNYALYPHMSVYENMAFGLKLRKYKKDDINKRVHEAAEILGLTEFLERKPADLSGGQRQRVAMGRAIVRDAKVFLMDEPLSNLDAKLRVAMRAEIAKIHRRIGATTIYVTHDQTEAMTLADRIVIMSATPNPDKTGSIGRIEQIGTPQELYNEPANKFVAGFIGSPAMNFFEVTVEKERLVNQDGLSLALPQGQEKILEEKGYLGKKVTLGIRPEDISSDQIVHETFPNASVTADILVSELLGSESMLYVKFGSTEFTARVNARDSHSPGEKVQLTFNIAKGHFFDLETEKRIN
>reanno__pseudo5_N2C3_1_AO356_00010 ABC transporter for D-Sorbitol, ATPase component (Pseudomonas fluorescens FW300-N2C3)
MATLKIENLKKGFEGLSIIKGIDLEVKDKEFVVFVGPSGCGKSTLLRLIAGLEDVTSGTIELDGRDITEVTPAKRDLAMVFQTYALYPHMTVRKNLSFALDLAGEKKPDVERKVAEAARILELGSLLDRKPKQLSGGQRQRVAIGRAIVRNPKIFLFDEPLSNLDAALRVQTRLELSRLHKELQATMIYVTHDQVEAMTLATKVVVLNAGRIEQIGSPLELYHHPANLFVAGFLGTPKMGFLQATVHAVHASGVEVRFASGTTLLIPRDSSALSVGQSVTIGIRPEHLTLGAEGQVLVTTDVTERLGSDTFCHVNVDSGESLTVRVQGDCEVPYAARRYLTLDVAHCHLFDESGLSVSPAASRAA
>reanno__psRCH2_GFF857 maltose ABC transporter, ATPase component MalK (Pseudomonas stutzeri RCH2)
MASVTLRDICKSYDGTPITRHIDLDIEDGEFVVFVGPSGCGKSTLLRLIAGLEDITSGDLLIDNQRVNDLPPKDRSVGMVFQSYALYPHMTVAENMAFGLKLASVDKREIKRRVEAVAEILQLDKLLERKPKDLSGGQRQRVAIGRTMVREPKVFLFDEPLSNLDAFLRVQMRIEIARLHQRIRSTMIYVTHDQVEAMTLADKIVVLNAGEIAQVGQPLHLYHYPKNRFVAGFLGSPQMNFVEVRAISASPETVTIELPSGYPLTLPVDGSAVSPGDPLTLGIRPEHFVMPDEADFTFHGQITVAERLGQYNLLYLTLERLQDVITLCVDGNLRVTEGETFAAGLKADKCHLFRENGEACTRHYREPAIYG
>TCDB__P54933 SmoK aka POLK, component of Hexitol (glucitol; mannitol) porter (Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides))
MGKITLRNVQKRFGEAVVIPSLDLDIEDGEFVVFVGPSGCGKSTLLRLIAGLEDVSDGQIMIDGRDATEMPPAKRGLAMVFQSYALYPHMTVKKNIAFPLRMAKMEPQEIERRVSNAAKILNLTNYLDRRPGQLSGGQRQRVAIGRAIVREPAAFLFDEPLSNLDAALRVNMRLEITELHQSLETTMIYVTHDQVEAMTMADKIVVLNAGRIEQVGSPLTLYRNPANLFVAGFIGSPKMNLIEGPEAAKHGATTIGIRPEHIDLSREAGAWEGEVGVSEHLGSDTFLHVHVAGMPTLTVRTGGEFGVHHGDRVWLTPQADKIHRFGADGKAL
>SwissProt__Q9L0Q1 Diacetylchitobiose uptake system ATP-binding protein MsiK; EC 7.5.2.- (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
MATVTFDKATRVYPGSTKPAVDGLDIDIADGEFLVLVGPSGCGKSTSLRMLAGLEDVNGGAIRIGDRDVTHLPPKDRDIAMVFQNYALYPHMSVADNMGFALKIAGVNKAEIRQKVEEAAKILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPQVFLMDEPLSNLDAKLRVSTRTQIASLQRRLGITTVYVTHDQVEAMTMGDRVAVLKDGLLQQVDSPRNMYDKPANLFVAGFIGSPAMNLVEVPITDGGVKFGNSVVPVNRDALKAASDKGDRTVTVGVRPEHFDVVELNGGAAKTLSKDSADAPAGLAVSVNVVEETGADGYIYGTVEVGGETKDLVVRVSSRAVPEKGATVHVVPRPGEIHVFSSSTGERLTD
>BRENDA__Q8TTZ3 ABC-type molybdate transporter (EC 7.3.2.5) (Methanosarcina acetivorans)
MIEIESLSRKWKNFSLDNLSLKVESGEYFVILGPTGAGKTLFLELIAGFHVPDSGRILLDGKDVTDLSPEKHDIAFVYQNYSLFPHMNVKKNLEFGMRMKKIKDPKRVLDTARDLKIEHLLDRNPLTLSGGEQQRVALARALVTNPKILLLDEPLSALDPRTQENAREMLSVLHKKNKLTVLHITHDQTEARIMADRIAVVMDGKLIQVGKPEEIFEKPVEGRVASFVGFENVLKGRVISAEQGLLRIRVGEVVIDAAGDMEVGDQVYAFLRPENIALSKSSTQSSIRNSLQGRVTEAWVLGALVRVKVDCGVPLNVLITRRSAEEMELSPGVQIYARFKASSVHVLR
>biolip__8hplC Lpqy-sugabc in state 1
AEIVLDRVTKSYPRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQPLSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMNFFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVHFTTEGAGAESAQLAELAADSGAGTNQFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>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
>metacyc__MONOMER-124208 polyol ABC-type transporterATP-binding component MtlK (Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5))
MAHLKISNLQKGFEGFEIIKGIDLEVNDKEFVVFVGPSGCGKSTLLRLIAGLEEVSGGSIELDGRDITEVSPAKRDLAMVFQTYALYPHMSVRKNMSFALDLAGVDKALVQQKVDEAARILELGPMLERKPKQLSGGQRQRVAIGRAIVRNPKIFLFDEPLSNLDAALRVQMRLELARLHKELQATMIYVTHDQVEAMTLADKVVVLNGGRVEQVGSPLELYHRPANLFVAGFLGTPKMGFLKGRISHVDGQGCEVQLDAGARLRLEQSGAQLSLGSEVTLGIRPEHLELGEPGPGSLAVTSDVAERLGSDTFCHVRSSCGEALTLRIRGDLASRYGEQLHLHLAPQHCHLFDAQGVAVSRPLRAAA
>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
>biolip__1g291 Malk
MAGVRLVDVWKVFGEVTAVREMSLEVKDGEFMILLGPSGCGKTTTLRMIAGLEEPSRGQIYIGDKLVADPEKGIFVPPKDRDIAMVFQSYALYPHMTVYDNIAFPLKLRKVPRQEIDQRVREVAELLGLTELLNRKPRELSGGQRQRVALGRAIVRKPQVFLMDEPLSNLDAKLRVRMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNRGVLQQVGSPDEVYDKPANTFVAGFIGSPPMNFLDAIVTEDGFVDFGEFRLKLLPDQFEVLGELGYVGREVIFGIRPEDLYDAMFAQVRVPGENLVRAVVEIVENLGSERIVRLRVGGVTFVGSFRSESRVREGVEVDVVFDMKKIHIFDKTTGKAIF
>PDB_8hpr_C Lpqy-sugabc in state 4
AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV
FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP
LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN
FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH
FTTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>PDB_8hpr_D Lpqy-sugabc in state 4
AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV
FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP
LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN
FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH
FTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>biolip__1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp
VIKMVEVKLENLTKRFGNFTAVNKLNLTIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTEGRIYFGDRDVTYLPPKDRNISMVFQHMTVYENIAFPLKKFPKDEIDKRVRWAAELLQIEELLNRYPAQLSGGQRQRVAVARAIVVEPDVLLMDEPLSNLDAKLRVAMRAEIKKLQQKLKVTTIYVTHDQVEAMTMGDRIAVMNRGQLLQIGSPTEVYLRPNSVFVATFIGAPEMNILEVSVGDGYLEGRGFRIELPQMDLLKDYVGKTVLFGIRPEHMTVEGVHMKRTARLIGKVDFVEALGTDTILHVKFGDELVKVKLPGHIPIEPGREVKVIMDLDMIHVFDKDTEKAIV
>biolip__2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS
>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__2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALEVINQRVNQVAEVLAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVAS