>WP_012590119.1 NCBI__GCF_000021745.1:WP_012590119.1 MQIRAQDIVKSFPGARRSALEGVSLNVGSGELVALLGPSGGGKTTLLRIIAGLDLPDSGKVFFGDEDASEKSVQERRVGFVFQNYALFKHLTVEDNIGFGLDVRDRAQRPPKAEIRRRALELLDLVQLKGLEKRRPSQLSGGQRQRVALARALAVEPRVLLLDEPFGALDAKVRRELRSWLREFHARTGHTTIFVTHDQDEALELADRVAVLNGGHIEQIGTPDEIYDHPATPFVNGFIGESTAISAHLREGQVFLGDHRLELPKANRLATSSDGEGQLFVRPQDILIGEEGPGALQAEVLSVRRSGPTRRAEIALPYEQSSIEVDTPASVTFQPGERVPVRFLRGTFFLKADAAGAAAHARS >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__Q6QJE1 Chloroplast ATP-binding protein, component of The chloroplast sulfate transporter, SulP/SulP2/Sabc/Sbp (Chlamydomonas reinhardtii) MASLLAQTTSRLGARPAAQAGPVAQMAPMASRVQPAMPSALLPLHARATTTSVACRAASIDKPVVYTPRDSSQQSSNGAGEVSMSISSMDEVGPSYEGIITDAPTRPTGLYVRVRNMVKHFSTAKGLFRAVDGVDVDIEPSSIVALLGPSGSGKTTLLRLIAGLEQPTGGNIYFDDTDATNLSVQDRQIGFVFQSYALFNHKTVAENIKFGLEVRKLNIDHDKRVAELLALVQLTGLGDRYPRQLSGGQRQRVALARALASNPRLLLLDEPFGALDAVVRKQLRTGLREIVRSVGVTTIIVTHDQEEAFDLADKVVVFNRGLVEQQGSPTEIIKRPRTPFIMKFVGETNVVPATSLLAKRMRFNTSKTSVMFRPHDIKLFKTVPPESGEGALTTVGANVADKANLGWVVKYTLRFDDDVECELQLSRDQDEREYNLVVGSRVFVHVPHRTMMGFNASDVDSTPIV >ecocyc__YAGC-MONOMER CP4-6 prophage; ABC transporter ATP-binding protein AfuC (Escherichia coli K-12 substr. MG1655) MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATFSDGYVDIYGYHLPRPLHFGTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILLQVNATRLQPDVGEQYYLEIHPYGMFVLADAA >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__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 >reanno__acidovorax_3H11_Ac3H11_2066 glucose ABC transporter, ATPase component (Acidovorax sp. GW101-3H11) MASSLDIAGINKRFGKGDKSVEVLRKVDIHVAPGEFLILVGPSGCGKSTLLNIIAGLDEPTEGEIRIGGKNVVGMPPRDRDIAMVFQSYALYPTLSVADNIGFALEMRKMPKPERQKRIDEVAAMLQISHLLDRRPSQLSGGQRQRVAMGRALARQPQLFLFDEPLSNLDAKLRVEMRAEIKRLHQASGITSVYVTHDQVEAMTLGSRIAVMKGGVVQQLGTPDEIYNRPANTYVATFIGSPTMNLLRGAVTGGQFGIQGAALNLAPPPSSANEVLLGVRPEHLVMQETAPWRGRVSVVEPTGPDTYVMVDTAAGSVTLRTDAQTRVQPGEHVGLALAPAHAHWFDAQSEERLVA >TCDB__O54370 BitD, component of The iron transporter, BitABCDEF (Treponema hyodysenteriae (Serpulina hyodysenteriae)) MSVSISIENVVKRYEKLTIIPDLSLEIKNGEFFTLLGPSGCGKTTLLRMIAGFNTIEGGEIKFDKDVINNIPAHKRNIGMVFQNYAIFPHMTVRENVEYGLKLRKENKESMKKKVDEMLHVVKIEEYQDRLPERLSGGQQQRVALARAIVITPSVLLMDEPLSNLDAKLRIEMRSAIKDIQRHVGITTVYVTHDQEEALAVSDRIAVMKNGVIQQVGSPVSIYTRPYNVFVATFIGHSNLFYATIKIEGNDTYLLFRCGYKLKMDNLLDVKDGDEVVVGIRPEEFFVNSENDEGIKAKILSKTFLGKYTNYFLHFNDNEVVPDQPSIEYSQDSSYTDRMYEKDEVITLKPNANKINVFTPDMEKSLIKGVKKYE >reanno__WCS417_GFF5296 putrescine ABC transporter, ATPase component (Pseudomonas simiae WCS417) MAVASGAYKKALEGDQTPKKVLVKIDRVTKKFDETIAVDDVSLEIKKGEIFALLGGSGSGKSTLLRMLAGFERPTEGRIYLDGEDITDMPPYERPINMMFQSYALFPHMTVAQNIAFGLQQDKIPKAEIDARVAEMLKLVQMSQYAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRSQMQLELVEIIERVGVTCVMVTHDQEEAMTMAERIAIMHLGWIAQIGSPIDIYETPTSRLVCEFIGNVNIFDTQVVDDAEGHAVLKCPDLDRDIYVGYGIATSVEDKSVTYAIRPEKLLVTTEMPTCEHNWSSGKVHDIAYLGGHSVFYVELPSGKLVQSFVANAERRGQRPTWGDQVYVWWEDDSGVVLRS >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__Q9X103 MalK; aka Sugar ABC transporter, ATP-binding protein, component of The maltose, maltotriose, mannotetraose (MalE1)/maltose, maltotriose, trehalose (MalE2) porter (Nanavati et al., 2005). For MalG1 (823aas) and MalG2 (833aas), the C-terminal transmembrane domain with 6 putative TMSs is preceded by a single N-terminal TMS and a large (600 residue) hydrophilic region showing sequence similarity to MLP1 and 2 (9.A.14; e-12 & e-7) as well as other proteins (Thermotoga maritima) MRMAQVVLENVTKVYENKVVAVKNANLVVEDKEFVVLLGPSGCGKTTTLRMIAGLEEITDGKIYIDGKVVNDVEPKDRDIAMVFQNYALYPHMTVYENMAFGLKLRKYPKDEIDRRVREAAKILGIENLLDRKPRQLSGGQRQRVAVGRAIVRNPKVFLFDEPLSNLDAKLRVQMRSELKKLHHRLQATIIYVTHDQVEAMTMADKIVVMKDGEIQQIGTPHEIYNSPANVFVAGFIGSPPMNFVNARVVRGEGGLWIQASGFKVKVPKEFEDKLANYIDKEIIFGIRPEDIYDKLFALAPSPENTITGVVDVVEPLGSETILHVKVGDDLIVASVNPRTQAKEEQKIDLVLDMTRMHAFDKETEKAII >TCDB__Q9AI63 PalK, component of Palatinose (isomaltulose; 6-O-α-D-glucopyranosyl-D-fructose) uptake porter (Erwinia rhapontici) MAQLTLDKIQKRYGAKAEVIRSLNLQIKSGEFVVIVGPSGCGKSTLLRMIAGLEEISGGGMYIDGHYANDDSPAERGIGMVFQSYALYPHMSVYQNMAFALELAHCSKAEIDQRVRECARILQLEPLLERRPKDLSGGQRQRVAIGRAIIREPRLFLFDEPLSNLDASLRVQMRMEVSALHKRLGVTIIYVTHDQVEAMTLADRIVVLNQGNIEQVGTPLELYDQPANEFVAQFIGSPKMNLIPATLRRSGEQQSVVELDNGKTLVLSIATPAEAEGRSVNIGIRPEHIRSGNVEQCEYQGEVMFVEQMGNETLLYLDNGNAGEPWVVRHAERSAIHVGQTVGVRLPVECCYLFDSHGQAFQRHLAKVH >TCDB__Q8TZQ3 MalK aka PF1933, component of Maltooligosaccharide porter (Maltose is not a substrate, but maltotriose is.) (Pyrococcus furiosus) MAGVRLVGVWKQFGSFTAVKDLTLEVRDGEFLVLLGPSGCGKTTTLRMIAGLEEPTKGQIYIGDKLVADPEKGVFVPPKDRDIAMVFQSYALYPHMTVYENIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIVRRPQVFLMDEPLSNLDAKLRVKMRAELKKLQKQLGVTTIYVTHDQVEAMTMGDRIAVMNQGVLQQVGTPEEVYEKPANTFVAGFIGSPPMNFLDATITEDGFLDFGEFRLKLLPDQFEVLQDYVGKEVIFGIRPEDIYDALFAQVKIPGENMARGVVDIIENLGGEKIVHISIGGLIVTAKFPGESRVKEGDEIDIVFDMKKIHIFNKKTGKAIL >ecocyc__UGPC-MONOMER sn-glycerol 3-phosphate ABC transporter ATP binding subunit (EC 7.6.2.10) (Escherichia coli K-12 substr. MG1655) MAGLKLQAVTKSWDGKTQVIKPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTEGDIWINDQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKQQIAERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNGGVAEQIGTPVEVYEKPASLFVASFIGSPAMNLLTGRVNNEGTHFELDGGIELPLNGGYRQYAGRKMTLGIRPEHIALSSQAEGGVPMVMDTLEILGADNLAHGRWGEQKLVVRLAHQERPTAGSTLWLHLAENQLHLFDGETGQRV >biolip__1g291 Malk MAGVRLVDVWKVFGEVTAVREMSLEVKDGEFMILLGPSGCGKTTTLRMIAGLEEPSRGQIYIGDKLVADPEKGIFVPPKDRDIAMVFQSYALYPHMTVYDNIAFPLKLRKVPRQEIDQRVREVAELLGLTELLNRKPRELSGGQRQRVALGRAIVRKPQVFLMDEPLSNLDAKLRVRMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNRGVLQQVGSPDEVYDKPANTFVAGFIGSPPMNFLDAIVTEDGFVDFGEFRLKLLPDQFEVLGELGYVGREVIFGIRPEDLYDAMFAQVRVPGENLVRAVVEIVENLGSERIVRLRVGGVTFVGSFRSESRVREGVEVDVVFDMKKIHIFDKTTGKAIF >SwissProt__Q9YGA6 Trehalose/maltose import ATP-binding protein MalK; EC 7.5.2.1 (Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)) MAGVRLVDVWKVFGEVTAVREMSLEVKDGEFMILLGPSGCGKTTTLRMIAGLEEPSRGQIYIGDKLVADPEKGIFVPPKDRDIAMVFQSYALYPHMTVYDNIAFPLKLRKVPRQEIDQRVREVAELLGLTELLNRKPRELSGGQRQRVALGRAIVRKPQVFLMDEPLSNLDAKLRVRMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNRGVLQQVGSPDEVYDKPANTFVAGFIGSPPMNFLDAIVTEDGFVDFGEFRLKLLPDQFEVLGELGYVGREVIFGIRPEDLYDAMFAQVRVPGENLVRAVVEIVENLGSERIVHLRVGGVTFVGSFRSESRVREGVEVDVVFDMKKIHIFDKTTGKAIF >BRENDA__Q8NMV1 ABC-type maltose transporter (EC 7.5.2.1) (Corynebacterium glutamicum) MATVTFKDASLSYPGAKEPTVKKFNLEIADGEFLVLVGPSGCGKSTTLRMLAGLENVTDGAIFIGDKDVTHVAPRDRDIAMVFQNYALYPHMTVGENMGFALKIAGKSQDEINKRVDEAAATLGLTEFLERKPKALSGGQRQRVAMGRAIVRNPQVFLMDEPLSNLDAKLRVQTRTQIAALQRKLGVTTVYVTHDQTEALTMGDRIAVLKDGYLQQVGAPRELYDRPANVFVAGFIGSPAMNLGTFSVKDGDATSGHARIKLSPETLAAMTPEDNGRITIGFRPEALEIIPEGESTDLSIPIKLDFVEELGSDSFLYGKLVGEGDLGSSSEDVPESGQIVVRAAPNAAPAPGSVFHARIVEGGQHNFSASTGKRLP >ecocyc__YDCT-MONOMER putative ABC transporter ATP-binding protein YdcT (Escherichia coli K-12 substr. MG1655) MTYAVEFDNVSRLYGDVRAVDGVSIAIKDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGAISIFGKPASNLPPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGVNKKQRHAMAQEALEKVALGFVHQRKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQLELKKLQQSLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDSPRDLYMRPRTPFVAGFVGTSNVFDGLMAEKLCGMTGSFALRPEHIRLNTPGELQANGTIQAVQYQGAATRFELKLNGGEKLLVSQANMTGEELPATLTPGQQVMVSWSRDVMVPLVEER >reanno__pseudo13_GW456_L13_PfGW456L13_1897 ABC transporter for D-Galactose and D-Glucose, ATPase component (Pseudomonas fluorescens GW456-L13) MATLELRNVNKTYGPGLPDTLKNIELKIDDGEFLILVGPSGCGKSTLMNCIAGLETISGGAILVDDADISGMSPKDRDIAMVFQSYALYPTMSVRDNIAFGLKIRKMPTAEIDEEVARVSKLLQIEHLLSRKPGQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPKDIYNNPANLFVASFIGSPPMNFIPLRLQRKDGRLLALLDSGQARCELPLGMQDAGLEDREVILGIRPEQIILANGEANGLPTIRAEVQVTEPTGPDTLVFVNLNDTKVCCRLAPDVAPAVGETLTLQFDPAKVLLFDAKTGERLGVAGVPKAEAHADNVAQFKGR >reanno__WCS417_GFF4321 glucose/xylose ABC transporter, ATPase component (Pseudomonas simiae WCS417) MATLELRNVNKTYGAGLPDTLKNIELSIKEGEFLILVGPSGCGKSTLMNCIAGLETITGGAIMIGDQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFGLKIRKMPQADIDAEVARVAKLLQIEHLLNRKPGQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPKEIYNNPANQFVASFIGSPPMNFVPLRLQRKDGRLVALLDSGQARCELALNTTEAGLEDRDVILGLRPEQIMLAAGEGDSASSIRAEVQVTEPTGPDTLVFVQLNDTKVCCRLAPDVAPQVGETLTLQFDPSKVLLFDANTGERLGTASSLPAQGHADNVAQFKGR >biolip__8hplC Lpqy-sugabc in state 1 AEIVLDRVTKSYPRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQPLSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMNFFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVHFTTEGAGAESAQLAELAADSGAGTNQFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD >PDB_8hpr_D Lpqy-sugabc in state 4 AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH FTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD >PDB_8hpr_C Lpqy-sugabc in state 4 AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH FTTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD >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 >biolip__2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS >SwissProt__P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) MASVQLRNVTKAWGDVVVSKDINLDIHDGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGETRMNDIPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVMNQRVNQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQIWLPVESRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGSACRRLHQEPGV >PDB_1q12_A Crystal structure of the atp-bound e. Coli malk VQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLP VKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSI RQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPG >biolip__1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp VIKMVEVKLENLTKRFGNFTAVNKLNLTIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTEGRIYFGDRDVTYLPPKDRNISMVFQHMTVYENIAFPLKKFPKDEIDKRVRWAAELLQIEELLNRYPAQLSGGQRQRVAVARAIVVEPDVLLMDEPLSNLDAKLRVAMRAEIKKLQQKLKVTTIYVTHDQVEAMTMGDRIAVMNRGQLLQIGSPTEVYLRPNSVFVATFIGAPEMNILEVSVGDGYLEGRGFRIELPQMDLLKDYVGKTVLFGIRPEHMTVEGVHMKRTARLIGKVDFVEALGTDTILHVKFGDELVKVKLPGHIPIEPGREVKVIMDLDMIHVFDKDTEKAIV >metacyc__G185E-5409-MONOMER ABC-type trehalose transporter ATP-binding protein (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)) MAEIVLDHVNKSYPDGHTAVRDLNLTIADGEFLILVGPSGCGKTTTLNMIAGLEDISSGELRIAGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKMRKADIAQKVSETAKILDLTNLLDRKPSQLSGGQRQRVAMGRAIVRHPKAFLMDEPLSNLDAKLRVQMRGEIAQLQRRLGTTTVYVTHDQTEAMTLGDRVVVMYGGIAQQIGTPEELYERPANLFVAGFIGSPAMNFFPARLTAIGLTLPFGEVTLAPEVQGVIAAHPKPENVIVGVRPEHIQDAALIDAYQRIRALTFQVKVNLVESLGADKYLYFTTESPAVHSVQLDELAEVEGESALHENQFVARVPAESKVAIGQSVELAFDTARLAVFDADSGANLTIPHRA >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__2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) ASVQLQNVTVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS >BRENDA__Q8TTZ3 ABC-type molybdate transporter (EC 7.3.2.5) (Methanosarcina acetivorans) MIEIESLSRKWKNFSLDNLSLKVESGEYFVILGPTGAGKTLFLELIAGFHVPDSGRILLDGKDVTDLSPEKHDIAFVYQNYSLFPHMNVKKNLEFGMRMKKIKDPKRVLDTARDLKIEHLLDRNPLTLSGGEQQRVALARALVTNPKILLLDEPLSALDPRTQENAREMLSVLHKKNKLTVLHITHDQTEARIMADRIAVVMDGKLIQVGKPEEIFEKPVEGRVASFVGFENVLKGRVISAEQGLLRIRVGEVVIDAAGDMEVGDQVYAFLRPENIALSKSSTQSSIRNSLQGRVTEAWVLGALVRVKVDCGVPLNVLITRRSAEEMELSPGVQIYARFKASSVHVLR >biolip__3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp TAALHIGHLSKSFQNTPVLNDISLSLDPGEILFIIGASGCGKTTLLRCLAGFEQPDSGEISLSGKTIFSKNTNLPVRERRLGYLVQEGVLFPHLTVYRNIAYGLGNGKGRTAQERQRIEAMLELTGISELAGRYPHELSGGQQQRAALARALAPDPELILLDEPFSALDEQLRRQIREDMIAALRANGKSAVFVSHDREEALQYADRIAVMKQGRILQTASPHELYRQPADLDAALFIGEGIVFPAALNADGTADCRLGRLPVQSGAPAGTRGTLLIRPEQYSLHPHSAPAASIHAVVLKTTPKARHTEISLRAGQTVLTLNLPSAPTLSDGISAVLHLDGPALFFPGNT >biolip__2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALEVINQRVNQVAEVLAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVAS