>NP_661230.1 NCBI__GCF_000006985.1:NP_661230.1
MIELRNVTLRYGEKVILDKVSLTVQDNTIKAILGPSGVGKSTIIKLMLGLIKPNSGQVFVDGVDITPLKEADLYPIRRKMGIVFQGNALFDSMTISQNMSFFLRENLQLPDDEIDRRVAEQIRFAGLEGYEDQLPESLSGGMQKRVAIGRALIFNPKMILFDEPTAGLDPVSSHKILNLIASLKKSNDLGAVFVTHIIDDVFAIADEVAVLYQSKIIFDGPTGQLHDSQHPFIKSILSDKILEL
>biolip__7d08B Acinetobacter mlafedb complex in atp-bound vtrans1 conformation
TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFLTGSAEGPVEYQFSHQAYLDNEVR
>PDB_7d0a_B Acinetobacter mlafedb complex in adp-vanadate trapped vclose conformation
TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAAR
ARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD
LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFL
TGSAEGPVEYQFSHQAYLDNEVR
>PDB_6z5u_K Cryo-em structure of the a. Baumannii mlabdef complex bound to appnhp
SLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARAR
MGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLI
MYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFLTG
SAEGPVEYQFSHQ
>TCDB__Q0SD37 ABC superfamily, ATP-binding component, component of The cholesterol uptake porter (Mohn et al., 2008). Takes up cholesterol, 5-α-cholestanol, 5-α-cholestanone, β-sitosterol, etc. (It is not established that all of these proteins comprise the system or that other gene products are not involved.) (Rhodococcus sp. (strain RHA1))
MGVEVSVEGLTKSFGSQRIWQDVTLTLPAGEVSALLGPSGTGKSVFLKSLIGLLRPEQGSIVIDGTNILECSSKELYEIRKLFGVLFQDGALFGSMNLYDNVAFPLREHTKKSESEIRKIVMEKMELVGLLGAEDKLPGEISGGMRKRAGLARALVLDPQIILVDEPDSGLDPVRTTYISQTLIDINAEIDATILIVSHNINLARTVPDNIGMLFRRHLVMFGPREVLLTSEQPVVKQFLNGTMIGPIGMSEEKDEATMAAEQAMVDAGHHAGGVDDVEGIVPQMKATPAMSFRQAVARRQERVRHIMHTLPENAQIAIQESLDETSGYGFYDESTAPLEAVGDVR
>TCDB__Q0SFA1 Probable bifunctional ABC transport system, component of The cholesterol uptake porter (Mohn et al., 2008). Takes up cholesterol, 5-α-cholestanol, 5-α-cholestanone, β-sitosterol, etc. (It is not established that all of these proteins comprise the system or that other gene products are not involved.) (Rhodococcus sp. (strain RHA1))
MGVEVSVEGLTKSFGSQRIWQDVTLTLPAGEVSALLGPSGTGKSVFLKSLIGLLRPEQGSIVIDGTNILECSSKELYEIRKLFGVLFQDGALFGSMNLFDNVAFPLREHTKKSESEIRKIVMEKMELVGLLGAEDKLPGEISGGMRKRAGLARALVLDPQIILVDEPDSGLDPVRTTYISQTLIDINAEIDATILIVSHNINLARTVPDNIGMLFRRHLVMFGPREVLLTSEEPVVKQFLNGTMIGPIGMSEEKDEATMAQEQAMVDAGHHAGGVDDVEGIVPQMKATPGMPFRQAVARRQERVRHIMHTLPENAQIAIQESLDETSGGNGGGGYDYAYSQEDTQVIPAYRGEGYENTTHGQG
>TCDB__P63357 Probable ribonucleotide transport ATP-binding protein mkl, component of The Mce/Yrb/Mlk (Mammalian cell entry) ABC-type putative steroid uptake transporter (involved in several aspects of mycobacterial pathogenesis) (Mycobacterium tuberculosis)
MRYSDSYHTTGRWQPRASTEGFPMGVSIEVNGLTKSFGSSRIWEDVTLTIPAGEVSVLLGPSGTGKSVFLKSLIGLLRPERGSIIIDGTDIIECSAKELYEIRTLFGVLFQDGALFGSMNLYDNTAFPLREHTKKKESEIRDIVMEKLALVGLGGDEKKFPGEISGGMRKRAGLARALVLDPQIILCDEPDSGLDPVRTAYLSQLIMDINAQIDATILIVTHNINIARTVPDNMGMLFRKHLVMFGPREVLLTSDEPVVRQFLNGRRIGPIGMSEEKDEATMAEEQALLDAGHHAGGVEEIEGVPPQISATPGMPERKAVARRQARVREMLHTLPKKAQAAILDDLEGTHKYAVHEIGQ
>SwissProt__Q9AT00 Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic; ABC transporter I family member 13; ABC transporter ABCI.13; AtABCI13; Non-intrinsic ABC protein 11; AtNAP11 (Arabidopsis thaliana (Mouse-ear cress))
MLSLSCSSSSSSLLPPSLHYHGSSSVQSIVVPRRSLISFRRKVSCCCIAPPQNLDNDATKFDSLTKSGGGMCKERGLENDSDVLIECRDVYKSFGEKHILKGVSFKIRHGEAVGVIGPSGTGKSTILKIMAGLLAPDKGEVYIRGKKRAGLISDEEISGLRIGLVFQSAALFDSLSVRENVGFLLYERSKMSENQISELVTQTLAAVGLKGVENRLPSELSGGMKKRVALARSLIFDTTKEVIEPEVLLYDEPTAGLDPIASTVVEDLIRSVHMTDEDAVGKPGKIASYLVVTHQHSTIQRAVDRLLFLYEGKIVWQGMTHEFTTSTNPIVQQFATGSLDGPIRY
>ecocyc__YAGC-MONOMER CP4-6 prophage; ABC transporter ATP-binding protein AfuC (Escherichia coli K-12 substr. MG1655)
MTQKNFVELRNVTKRFGSNTVIDNINLTIPQGQMVTLLGPSGCGKTTILRLVAGLEKPSEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPRAELKARVKEALAMVDLEGFEDRFVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRDKIRELQKQFDITSLYVTHDQSEAFAVSDTVLVMNKGHIMQIGSPQDLYRQPASRFMASFMGDANLFPATFSDGYVDIYGYHLPRPLHFGTQGEGMVGVRPEAITLSDRGEESQRCVIRHVAYMGPQYEVTVEWHGQEILLQVNATRLQPDVGEQYYLEIHPYGMFVLADAA
>CharProtDB__CH_107359 toluene tolerance protein Ttg2A (Pseudomonas putida)
MSVDSAYAVELKGVTFKRGSRSIFSNVDIRIPRGKVTGIMGPSGCGKTTLLRLMGAQLRPSSGEVWVAGQNLPTLSRSDLFDARKQMGVLFQSGALFTDLDVFENVAFPLRVHTQLSDEMIRDIVLMKLQAVGLRGAIDLMPDELSGGMKRRVALARAIALDPQILMYDEPFVGQDPIAMGVLVRLIRLLNDALGITSIVVSHDLAETASIADYIYVVGDGQVLGQGTPDELMGSDNPRIRQFMKGDPDGPVPFHFPAPDYRADLLGAR
>ecocyc__YRBF-MONOMER intermembrane phospholipid transport system, ATP binding subunit MlaF (Escherichia coli K-12 substr. MG1655)
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPFRYPAGDYHADLLPGS
>biolip__7ch6C Cryo-em structure of e.Coli mlafeb with amppnp
VANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPFRYPAGDYHADLLPGS
>PDB_6xgy_A Crystal structure of e. Coli mlafb abc transport subunits in the dimeric state
VANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR
KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD
LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFL
DGIADGPVPFRYPAGDYHADLLPG
>PDB_7cgn_B The overall structure of the mlafedb complex in atp-bound eqtall conformation (mutation of e170q on mlaf)
VANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR
KRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD
LIMFDQPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFL
DGIADGPVPFRYPAGDYHADLLP
>biolip__7chaI Cryo-em structure of p.Aeruginosa mlafebd with amppnp
AYAVELKGLTFKRGSRAIFDNIDVRIPRGKVTGIMGPSGCGKTTLLRLIASQLRPSKGEVWVNGQNLPQLSRGDLFDMRKQFGVLFQSGALFTDLDVFENVAFPLRVHTQLPEEMIRDIVLMKLQAVGLRGAVELMPDELSGGMKRRVALARAIALDPQILLYDEPFVGQDPIAMGVLVRLIRLLNDALGITSIVVSHDLAETASIADYIYIVGDGRVLGHGTPDVLKETDDPRIRQFVKGIPDGPVPFHYPARDYRADLLG
>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__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__ABC-MONOMER L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) (Escherichia coli K-12 substr. MG1655)
MIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV
>biolip__6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein
HMIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDQATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNAIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV
>PDB_3tuz_C Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form
HMIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTK
ARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNP
KVLLCDQATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK
FIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGT
QQDTQAAIAWLQEHHVKVEVLGYV
>PDB_3tui_C Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form
HMIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTK
ARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNP
KVLLCDQATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK
FIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGT
QQDTQAAIAWLQEHHVKVEVLGYV
>reanno__WCS417_GFF5296 putrescine ABC transporter, ATPase component (Pseudomonas simiae WCS417)
MAVASGAYKKALEGDQTPKKVLVKIDRVTKKFDETIAVDDVSLEIKKGEIFALLGGSGSGKSTLLRMLAGFERPTEGRIYLDGEDITDMPPYERPINMMFQSYALFPHMTVAQNIAFGLQQDKIPKAEIDARVAEMLKLVQMSQYAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRSQMQLELVEIIERVGVTCVMVTHDQEEAMTMAERIAIMHLGWIAQIGSPIDIYETPTSRLVCEFIGNVNIFDTQVVDDAEGHAVLKCPDLDRDIYVGYGIATSVEDKSVTYAIRPEKLLVTTEMPTCEHNWSSGKVHDIAYLGGHSVFYVELPSGKLVQSFVANAERRGQRPTWGDQVYVWWEDDSGVVLRS
>TCDB__P54933 SmoK aka POLK, component of Hexitol (glucitol; mannitol) porter (Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides))
MGKITLRNVQKRFGEAVVIPSLDLDIEDGEFVVFVGPSGCGKSTLLRLIAGLEDVSDGQIMIDGRDATEMPPAKRGLAMVFQSYALYPHMTVKKNIAFPLRMAKMEPQEIERRVSNAAKILNLTNYLDRRPGQLSGGQRQRVAIGRAIVREPAAFLFDEPLSNLDAALRVNMRLEITELHQSLETTMIYVTHDQVEAMTMADKIVVLNAGRIEQVGSPLTLYRNPANLFVAGFIGSPKMNLIEGPEAAKHGATTIGIRPEHIDLSREAGAWEGEVGVSEHLGSDTFLHVHVAGMPTLTVRTGGEFGVHHGDRVWLTPQADKIHRFGADGKAL
>TCDB__A4PCH8 Putative ATPase component of ABC transporter system aka LinL, component of The γ-hexachlorocyclohexane (γHCH) uptake permease, LinKLMN (most similar to 3.A.1.12.4, the QAT family) (Sphingobium japonicum)
MAQEEEISAEEARIEEAVQHDGIAISVRNLRNSFGDQVVHEGLNLDVRKGEILGVVGGSGTGKSVLMRSIIGLQTPDEGEIHVFGESMIGRLDNEALAIRKRWGVLFQGGALFSTLTVAENVEVPIREYYPNIGPKLRDEIAAYKIRLTGLPAEAGPKYPAELSGGMKKRAGLARALALDPDLLFLDEPTAGLDPIGAAAFDDQTRRLQQTLGLTVFLITHDLDTLYSICDRVAVLADRKVTAVGTIDELLATDHPWIQEYFNGPRGRAATAAVAREKDKRR
>TCDB__Q8NSN2 Methionine import ATP-binding protein metN, component of L-Methionine uptake porter, MetQNI (Corynebacterium glutamicum)
MSHTASTPTPEEYSAQQPSTQGTRVEFRGITKVFSNNKSAKTTALDNVTLTVEPGEVIGIIGYSGAGKSTLVRLINGLDSPTSGSLLLNGTDIVGMPESKLRKLRSNIGMIFQQFNLFQSRTAAGNVEYPLEVAKMDKAARKARVQEMLEFVGLGDKGKNYPEQLSGGQKQRVGIARALATNPTLLLADEATSALDPETTHEVLELLRKVNRELGITIVVITHEMEVVRSIADKVAVMESGKVVEYGSVYEVFSNPQTQVAQKFVATALRNTPDQVESEDLLSHEGRLFTIDLTETSGFFAATARAAEQGAFVNIVHGGVTTLQRQSFGKMTVRLTGNTAAIEEFYQTLTKTTTIKEITR
>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
>SwissProt__Q9RR46 Glycine betaine/carnitine transport ATP-binding protein GbuA; EC 7.6.2.9 (Listeria monocytogenes serotype 1/2a (strain 10403S))
MSKIKVEELTKIFGKKASKASSLLSQGKSKTDILKETGATIGVNKASFSVEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTSGKIWLDGKELSSLNKKELLEVRRKSMSMVFQNFGLFPNRTINRNVEYGLEIQGMDKEEREKNAAESLALVGLAGYGDQYPSQLSGGMQQRVGLARALANNPDILLMDEAFSALDPLNRKDMQDQLLDLQDKMKKTIIFITHDLDEALRIGDHIMIMRDGSVVQTGSPEEILAHPANEYVEKFIEDVDRSKVYTASNVMIRPEIVNFEKDGPRVALKRMREAGTSSVFVVKRNRELVGIVHAAEVSKLVKENITSLETALHRDVPTTGLDTPLAEIMDTISTTTIPIAVTEDGKLKGIIIRGSVLAALSGNEVNVNA
>SwissProt__A0A0H2ZLL3 Probable ergothioneine transport ATP-binding protein EgtUA; EC 7.6.2.9 (Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466))
MIEYKNVALRYTEKDVLRDVNLQIEDGEFMVLVGPSGSGKTTMLKMINRLLEPTDGNIYMDGKRIKDYDERELRLSTGYVLQAIALFPNLTVEENIALIPEMKGWTKEEIAQKTEELLAKVGLPVAEYGHRLPSELSGGEQQRVGIVRAMIGQPKILLMDEPFSALDAISRKQLQVLTKELHKEFGMTTIFVTHDTDEALKLADRIAVLQDGEIRQVSNPETILKAPATDFVADLFGGSIHD
>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
>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
>SwissProt__P96063 Putative 2-aminoethylphosphonate import ATP-binding protein PhnT (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MLMKTTTVHAPASQGTSGIVLDSLRVAYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAVAGFVQPAGGRILIGDTDVTHLPPYKRGLAMVVQNYALFPHLKVEDNVAFGLRAQKQPKALINERVTQALKTVGMSDYAARYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETRALYQHPPNRFAAEFLGRANILSAIALGITEAPGLVDVSCGGAVIRAFSRGSHHGYNKLLCIRPQHLSLTPRSAYSNRFNATLQSVHWQGDLTHLLCDVAGETVRMVLTHVNPLPRVGDKLALWFEPDDAVLIEV
>TCDB__P74127 FutC aka SLL1878, component of Ferric iron (Fe3+) porter
MTVAQFSPVARLSIEDSVLTVQDLGKSFRGQSTPVLQKINFNLAPGEILGLLGPSGCGKTTLLRIIAGFETPTSGTVHLEGDCVSGENGLTPPEQRQTGMVFQDYALFPHLTITDNIAFGLRHKSQKLNRQQIQGRVAEVLHLVGLTGLEKRYPHELSGGQQQRIALARALAPKPNLILLDEPLSNLDVQVRQRLRHEIRHILKATGTAAIFVTHDQEEAMAISDRIGVMYRGNLEQIGTPEEIYRSPASRFVAEFVTQANFVPAQRQGTLWATEFGQWPLTFQGIQPELPSVGELMLREEEIELSPASDGPVVIRDRQFLGREYRYCLETPAGRQIHARTSLQTVIPVGSRVNLTPTNPCPPLFAQG
>reanno__Phaeo_GFF2754 N-Acetyl-D-glucosamine ABC transport system, ATPase component (Phaeobacter inhibens BS107)
MTALQLTNVCKSFGPVEVLKDINLTVEDGEFVVFVGPSGCGKSTLLRVISGLEDATAGEISIGGQTVTTTPPAKRGIAMVFQSYALYPHLSVRENMALALKQERQPKEEIAARVAEASRMLSLEDYLDRRPSELSGGQRQRVAIGRAVVREPKLFLFDEPLSNLDAALRMNTRLEIARLHRQLSASMIYVTHDQIEAMTLADKIVVLRDGRIEQVGTPMELYNNPANRFVAEFIGAPAMNFVPAQRLGGNPGQFIGIRPEYARISPVGPLAGEVIHVEKLGGDTNILVDMGEDLTFTARLFGQHDTNVGETLQFDFDPANCLSFDEAGQRI