>WP_011022261.1 NCBI__GCF_000007345.1:WP_011022261.1
MRLGVKVDIKKHYTEAEINRKRSTGKAFTLDVSFEMDNELVVLFGPSGSGKTTLFKCISGITQPDNGKITVGSKIYYDKDKKINLPIQKRNLGYVFQNYTLFPHMNVRKNIECGLKKWEKEDREVRVMEMLNLLHIEELETHYPSQLSGGQKQRVALARALAPKPELLLLDEPFSALDRVLRIELAEKLKKLQKRIGIPLAFITHSLDEAFVLADRILILYRGEVQQFGAPEEIFYHPRNLHVAELAGLSNIFDDARVEEQVEKLVEGNNAGPKRTVLKSGEMRIAVNPLNLKEGDKVSWGIHPENITLLLPNSGSEDKDENVYSAYVHSITGKGPKKRIVLKLARHEKSLNAEVPAQFADALNLNTGDLCLVKMDMSKVVAF
>TCDB__O54370 BitD, component of The iron transporter, BitABCDEF (Treponema hyodysenteriae (Serpulina hyodysenteriae))
MSVSISIENVVKRYEKLTIIPDLSLEIKNGEFFTLLGPSGCGKTTLLRMIAGFNTIEGGEIKFDKDVINNIPAHKRNIGMVFQNYAIFPHMTVRENVEYGLKLRKENKESMKKKVDEMLHVVKIEEYQDRLPERLSGGQQQRVALARAIVITPSVLLMDEPLSNLDAKLRIEMRSAIKDIQRHVGITTVYVTHDQEEALAVSDRIAVMKNGVIQQVGSPVSIYTRPYNVFVATFIGHSNLFYATIKIEGNDTYLLFRCGYKLKMDNLLDVKDGDEVVVGIRPEEFFVNSENDEGIKAKILSKTFLGKYTNYFLHFNDNEVVPDQPSIEYSQDSSYTDRMYEKDEVITLKPNANKINVFTPDMEKSLIKGVKKYE
>TCDB__Q8TZQ3 MalK aka PF1933, component of Maltooligosaccharide porter (Maltose is not a substrate, but maltotriose is.) (Pyrococcus furiosus)
MAGVRLVGVWKQFGSFTAVKDLTLEVRDGEFLVLLGPSGCGKTTTLRMIAGLEEPTKGQIYIGDKLVADPEKGVFVPPKDRDIAMVFQSYALYPHMTVYENIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIVRRPQVFLMDEPLSNLDAKLRVKMRAELKKLQKQLGVTTIYVTHDQVEAMTMGDRIAVMNQGVLQQVGTPEEVYEKPANTFVAGFIGSPPMNFLDATITEDGFLDFGEFRLKLLPDQFEVLQDYVGKEVIFGIRPEDIYDALFAQVKIPGENMARGVVDIIENLGGEKIVHISIGGLIVTAKFPGESRVKEGDEIDIVFDMKKIHIFNKKTGKAIL
>biolip__2d62A Crystal structure of multiple sugar binding transport atp- binding protein
MIGMAEVKLINIWKRFGDVTAVKDLSLEIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTRGQIYIEDNLVADPEKGVFVPPKERDVAMVFQSYALYPHMTVYDNIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIIRRPKVFLMDEPLSNLDAKLRVKMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNKGELQQVGTPDEVYYKPVNTFVAGFIGSPPMNFLDATITDDGFLDFGEFKLKLLQDQFEVLEEENMVGKEVIFGIRPEDVHDASFTHIDVPEENTVKATVDIIENLGGEKIVHLRRGNISFTAKFPKESKVREGDEVSVVFDMKKIHIFRKDTEKAIF
>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
>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
>biolip__1g291 Malk
MAGVRLVDVWKVFGEVTAVREMSLEVKDGEFMILLGPSGCGKTTTLRMIAGLEEPSRGQIYIGDKLVADPEKGIFVPPKDRDIAMVFQSYALYPHMTVYDNIAFPLKLRKVPRQEIDQRVREVAELLGLTELLNRKPRELSGGQRQRVALGRAIVRKPQVFLMDEPLSNLDAKLRVRMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNRGVLQQVGSPDEVYDKPANTFVAGFIGSPPMNFLDAIVTEDGFVDFGEFRLKLLPDQFEVLGELGYVGREVIFGIRPEDLYDAMFAQVRVPGENLVRAVVEIVENLGSERIVRLRVGGVTFVGSFRSESRVREGVEVDVVFDMKKIHIFDKTTGKAIF
>TCDB__Q8U4K3 WtpC, component of Tungsten (KM=20pM)/molybdate (KM=10nM) porter (Pyrococcus furiosus)
MLEVQGISKKWKDFHLKDISFSVMDGEYFIVLGPSGAGKTVLLEIIAGIIPPDGGKVLLDGKDITLLPPEKRGIAYVPQNYALFPNMSVFDNIAFGLKVRRVPRSEIEKRVLEISEVLGIRHLLHRKPRTLSGGEQQRVAVARALVIEPEIILLDEPFANLDVQIRSRLINEMKRWRRELGFTAIHVTHSFEEALALGDRVGIMLNGKLVQVGEIREVFSRPNSEEVAKFLGFENIIEGIADGRVLHVGKLRIELPLEAKGRVRIGIRPEDILISTERIKTSARNVFKAKVEAIEDVGPLVKLTLNVCDITLRAFITRSSLVELGIEEGKEVYASFKASAIHVF
>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__Q88P35 GtsD (GLcK), component of Glucose porter, GtsABCD (Pseudomonas putida (strain KT2440))
MATLELRNVNKTYGSGLPDTLKDIQLSIKDGEFLILVGPSGCGKSTLMNCIAGLEQITGGAILIDEQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFGLKIRKLPQAAIDEEVARVAKLLQIEHLLARKPAQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPQQIYNDPANQFVASFIGSPPMNFIPVRLARQDGRLLALLDSGQARCELPLGEAADALEGREIILGIRPEQIALGAADGNGLPAIRAEVQVTEPTGPDLLVFVTLNQTKVCCRLAPDVACRVGDTLNLQFDPARVLLFDAANGERLHLASTGATAKDNVAHFKGR
>reanno__WCS417_GFF4321 glucose/xylose ABC transporter, ATPase component (Pseudomonas simiae WCS417)
MATLELRNVNKTYGAGLPDTLKNIELSIKEGEFLILVGPSGCGKSTLMNCIAGLETITGGAIMIGDQDVSGMSPKDRDIAMVFQSYALYPTMSVRENIEFGLKIRKMPQADIDAEVARVAKLLQIEHLLNRKPGQLSGGQQQRVAMGRALARRPKIYLFDEPLSNLDAKLRVEMRTEMKLMHQRLKTTTVYVTHDQIEAMTLGDKVAVMKDGIIQQFGTPKEIYNNPANQFVASFIGSPPMNFVPLRLQRKDGRLVALLDSGQARCELALNTTEAGLEDRDVILGLRPEQIMLAAGEGDSASSIRAEVQVTEPTGPDTLVFVQLNDTKVCCRLAPDVAPQVGETLTLQFDPSKVLLFDANTGERLGTASSLPAQGHADNVAQFKGR
>reanno__WCS417_GFF5296 putrescine ABC transporter, ATPase component (Pseudomonas simiae WCS417)
MAVASGAYKKALEGDQTPKKVLVKIDRVTKKFDETIAVDDVSLEIKKGEIFALLGGSGSGKSTLLRMLAGFERPTEGRIYLDGEDITDMPPYERPINMMFQSYALFPHMTVAQNIAFGLQQDKIPKAEIDARVAEMLKLVQMSQYAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRSQMQLELVEIIERVGVTCVMVTHDQEEAMTMAERIAIMHLGWIAQIGSPIDIYETPTSRLVCEFIGNVNIFDTQVVDDAEGHAVLKCPDLDRDIYVGYGIATSVEDKSVTYAIRPEKLLVTTEMPTCEHNWSSGKVHDIAYLGGHSVFYVELPSGKLVQSFVANAERRGQRPTWGDQVYVWWEDDSGVVLRS
>BRENDA__A0A142UTH4 ABC-type polyamine transporter (subunit 4/4) (EC 7.6.2.11) (Streptococcus suis)
MKKPIIEFKNVSKVFEDSGTTVLKDISFELEEGKFYTLLGASGSGKSTILNIIAGLLDASSGDIYLDGQRINDVPTNKRDVHTVFQSYALFPHMTVFENVAFPLKLRKIDKAEIERRVTEALQMVRLSGYENRSIQKLSGGQRQRVAIARAIINQPRVVLLDEPLSALDLKLRTEMQYELRELQQRLGITFVFVTHDQEEALAMSDWIFVMNEGEIVQSGTPVDIYDEPINHFVATFIGESNILPGRMIEDYLVEFNGKRFEAVDGGMRPNEEVEVVIRPEDLQITLPEEGKLQVKVDTQLFRGVHYEIIAYDDLGNEWMIHSTRKAIVGEVIGLSFEPEDIHIMRLNETEEEFDARIEEYVEVEEVEDGLINAIEEERNEENL
>reanno__BFirm_BPHYT_RS16095 ABC transporter for D-Sorbitol, ATPase component (Burkholderia phytofirmans PsJN)
MASVTLRNIRKAYDENEVMRDINLDIADGEFVVFVGPSGCGKSTLMRMIAGLEDISGGDLTIDGMRVNDVAPAKRGIAMVFQSYALYPHMTLYDNMAFGLKLAGTKKPEIDAAVRNAAKILHIDHLLDRKPKQLSGGQRQRVAIGRAITRKPKVFLFDEPLSNLDAALRVKMRLEFARLHDELKTTMIYVTHDQVEAMTLADKIVVLSAGNLEQVGSPTMLYHAPANRFVAGFIGSPKMNFMEGVVQSVTHDGVTVRYETGETQRVAVEPAAVKQGDKVTVGIRPEHLHVGMAEDGISARTMAVESLGDAAYLYAESSVAPDGLIARIPPLERHTKGETQKLGATPEHCHLFDSAGKAFQRKIVEVLAA
>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__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__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
>BRENDA__Q4QJQ0 ABC-type molybdate transporter (EC 7.3.2.5) (Haemophilus influenzae)
MLQINVKKQLGKLALQANIQVPDQGVTAIFGLSGSGKTSLINLVSGLIQPDEGFIRLNDRTLVDMESQESLPTHLRKIGYVFQDARLFPHYTVKGNLRYGMKHVSQDDFNYIVDLLGITHLLKRYPLTLSGGEKQRVAIGRALLTDPDILLMDEPLSALDVPRKRELMQYLERLSKEINIPILYVTHSLDELLRLADRVVLMENGIVQAYDSVEKIWNSPIFAPWKGENEQSSVLALPVHLHNPPYKMTALSLGEQALWIHQVPANVGERVLVCIYSSDVSIILQKPEQTSIRNILRGKITQIEIQDSRVDLAVLVEGNKIWASISKWAQNELRFAVGQDVYVQIKAVSVM
>biolip__8hplC Lpqy-sugabc in state 1
AEIVLDRVTKSYPRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQPLSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMNFFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVHFTTEGAGAESAQLAELAADSGAGTNQFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>biolip__1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp
VIKMVEVKLENLTKRFGNFTAVNKLNLTIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTEGRIYFGDRDVTYLPPKDRNISMVFQHMTVYENIAFPLKKFPKDEIDKRVRWAAELLQIEELLNRYPAQLSGGQRQRVAVARAIVVEPDVLLMDEPLSNLDAKLRVAMRAEIKKLQQKLKVTTIYVTHDQVEAMTMGDRIAVMNRGQLLQIGSPTEVYLRPNSVFVATFIGAPEMNILEVSVGDGYLEGRGFRIELPQMDLLKDYVGKTVLFGIRPEHMTVEGVHMKRTARLIGKVDFVEALGTDTILHVKFGDELVKVKLPGHIPIEPGREVKVIMDLDMIHVFDKDTEKAIV
>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
>BRENDA__Q8TTZ3 ABC-type molybdate transporter (EC 7.3.2.5) (Methanosarcina acetivorans)
MIEIESLSRKWKNFSLDNLSLKVESGEYFVILGPTGAGKTLFLELIAGFHVPDSGRILLDGKDVTDLSPEKHDIAFVYQNYSLFPHMNVKKNLEFGMRMKKIKDPKRVLDTARDLKIEHLLDRNPLTLSGGEQQRVALARALVTNPKILLLDEPLSALDPRTQENAREMLSVLHKKNKLTVLHITHDQTEARIMADRIAVVMDGKLIQVGKPEEIFEKPVEGRVASFVGFENVLKGRVISAEQGLLRIRVGEVVIDAAGDMEVGDQVYAFLRPENIALSKSSTQSSIRNSLQGRVTEAWVLGALVRVKVDCGVPLNVLITRRSAEEMELSPGVQIYARFKASSVHVLR
>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
>ecocyc__MALK-MONOMER maltose ABC transporter ATP binding subunit (EC 7.5.2.1) (Escherichia coli K-12 substr. MG1655)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV
>biolip__2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS
>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
>SwissProt__P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MASVQLRNVTKAWGDVVVSKDINLDIHDGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGETRMNDIPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVMNQRVNQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQIWLPVESRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGSACRRLHQEPGV
>biolip__2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS