>Ac3H11_694 FitnessBrowser__acidovorax_3H11:Ac3H11_694
MNAVLNTPQPMAPTDTAAPLLEIAHLRKHFGSGPHPVRAVDDVSFTIHRGETLGLVGESGSGKSTIGRLLTRLVDPTSGQMRYHGGAAPQDLAQLSQSQYRPLRSQIQIIFQDPYASLNPRMRIRDVLAEALDTHGLAKGAARLPRIHQLLEQVGLRPEHAERFPHEFSGGQRQRIGIARALAVEPQFIVADEPLSALDVSIQAQVVNLLGELKEQLGLTLLFISHDLDVVEYLCDRVVVLYLGRVMEIAPTEALYAQPQHPYTQALLAAAPIPDPAQRRSIALLQGDLPSPANPPSGCVFRTRCPQAEARCASADMQLREVAPGHLHACWKTAPLSHANP
>TCDB__Q8CJS2 Putative peptide transport system ATP-binding subunit, component of Peptide transporter encoded adjacent to the putative transport system with TC#3.A.1.5.35 (Akanuma et al. 2011). Induced by exogenous S-adenosylmethionine (SAM) at a concentration of 2muM which also enhanced antibiotic production and inhibited morphological development (Park et al. 2005). SAM can be imported into cells. Mutants in the bldK genes confer resistance to the toxic tripeptide, bialaphos (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
MSDNSKTTTAVADDFPQQRDGDTAPLLKVSGLSKHFPIKGGFPIKRTVGHVKAVDGVDFEVFPGESLGLVGESGCGKSTTGRLLTRLYEPTQGSIEYRGKDITRANRRELAPVRSEIQMIFQDPYASLNPRQTVGTIISGPMEINGINPPGGREKRVRELLEIVGLNPEHYNRFPHEFSGGQRQRIGVARAVALQPKLIVADEPVSALDVSIQAQVVNLLQEVQREMGIAFVFIAHDLAIVRHFSQRVAVMYLGKIVEIADRDSLYNRPRHPYTHALLSAVPETDLDAEKRERIRLEGDVPSPISPPSGCRFRTRCWKAQDKCATEEPPLVQLSGNREGHLTACHFPEEGSTEARAEDIVMDPGLKAMEDGADGGATLSKG
>TCDB__P42065 AppF, component of 5-6 amino acyl oligopeptide transporter AppA-F (Bacillus subtilis)
MTAANQETILELRDVKKYFPIRSGLFQRKVGDVKAVDGVSFSLKKGETLGIVGESGCGKSTAGRTMIRLYKPTEGQILFKGQDISNLSEEKLRKSVRKNIQMVFQDPFASLNPRKTLRSIIKEPFNTHNMYTMRERNEKVEELLARVGLHPSFAGRYPHEFSGGQRQRIGIARALTLNPELIIADEPVSALDVSIQAQVINLMEELQEEFNLTYLFISHDLSVVRHISDRVGVMYLGKMMELTGKHELYDNPLHPYTQALLSSVPVTRKRGSVKRERIVLKGELPSPANPPKGCVFHTRCPVAKPICKEQIPEFKEAAPSHFVACHLYS
>SwissProt__P24137 Oligopeptide transport ATP-binding protein OppF; Stage 0 sporulation protein KE (Bacillus subtilis (strain 168))
MTEKLLEIKHLKQHFVTPRGTVKAVDDLSFDIYKGETLGLVGESGCGKSTTGRSIIRLYEATDGEVLFNGENVHGRKSRKKLLEFNRKMQMIFQDPYASLNPRMTVADIIAEGLDIHKLAKTKKERMQRVHELLETVGLNKEHANRYPHEFSGGQRQRIGIARALAVDPEFIIADEPISALDVSIQAQVVNLMKELQKEKGLTYLFIAHDLSMVKYISDRIGVMYFGKLVELAPADELYENPLHPYTKSLLSAIPLPDPDYERNRVRQKYDPSVHQLKDGETMEFREVKPGHFVMCTEAEFKAFS
>TCDB__Q9WXR3 Oligopeptide ABC transporter, ATP-binding protein, component of Probable xylan oligosaccharide porter (Conners et al. 2005). Induced by cylan and xylose. Regulated by xylose-responsive regulator XylR (Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099))
MKLLEVKGLKKYFPLTKGFFKKVVGYVRAVDDVSFDIKQGETLALVGESGCGKTTTAKSILRAIDPTDGDVILHLDGKDVNIAKLSRDELKPYRRYMQMIFQNPYTSLNPRMKVKEIVGEPLLVNGIAKGKELEDRVAELLKAVGLRPEYMIRYPHAFSGGQRQRIVIARAIALRPKLVVCDEPTSALDVSIRAQILNLLMDLQEEFALTYLFITHDLSVVEHISDRVAVMYLGKIVELSSTEEIFENPKHPYTETLLRSVPKPDPDLREELVPIEGEVPNPANPPSGCYFHPRCPYAKSICKEEYPEFRNLGTEDNPHYVACHFAESLKLRGVKITL
>BRENDA__Q5V9R8 ABC-type oligopeptide transporter (EC 7.4.2.6) (Vibrio fluvialis)
MSADKPLLLDVKNLKVHFSIAAKSGWPWTKPSTLKAVDGVNVRLYEGETLGVVGESGCGKSTFARAIIGLVQSTEGEVVWLGQDLTRMQEVKRRNTRKEIQMIFQDPLASLNPRMTVGDIIAEPLQTFYPELSKQEVKDRVKEMMAKVGLLPNVINRYPHEFSGGQCQRIGIARALILKPKMIICDEPVSALDVSIQAQVVNLLKELQKELGLSLVFIAHDLSVVKHISDRVLVMYLGNAVELGEADELFANPLHPYTKALMSAVPIPDPNLERAKVIQMLEGDLPSPINPPSGCVFRTRCPQATAECAKTKPQIEGTDTHSVSCLHVSA
>TCDB__B1W1L8 Putative peptide ABC transporter ATP-binding protein, component of The ABC BldKA-E (SGR_2418-2414) oligopeptide transport system. It controls aerial mycelium formation on glucose media. Probably involved in extracellular peptide signalling (Akanuma et al. 2011).  Probably orthologous to 3.A.1.5.35 (Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350))
MDATPNVSAVETVDVATEAEAVAAIDAPVSQGEPILQVRNLVKHFPLTQGILFKKQIGAVKAVDGISFDLYAGETLGIVGESGCGKSTVAKLLMTLERATAGEVFYKGQDITKLSGRALKAVRRNIQMVFQDPYTSLNPRMTVGDIIGETFEIHPEVAPKGDRRRRVQDLLDVVGLNPEYINRYPHQFSGGQRQRIGIARGLALNPEIIICDEPVSALDVSVQAQVINLMEKLQDEFNLSYVFIAHDLSIVRHISDRVGVMYLGKMAEIGTDTQIYDHPTHPYTQALLSAVPVPDPSAREGRDRIILTGDVPSPANPPSGCRFRTRCWKAEERCATEEPLLAIPERFVAGSTPATHESACHFAEERDVVHAA
>TCDB__P08007 OppF aka STM1742, component of Oligopeptide porter (also takes up amino glycoside antibiotics such as kanamycin, streptomycin and neomycin as well as cell wall-derived peptides such as murein tripeptide). It transports substrate peptides of 2-5 amino acids with highest affinity for tripeptides. Also transports δ-aminolevulinic acid (ALA). [May be regulated by PTS Enzyme INtr-aspartokinase.] ATP-binding to OppDF may result in donation of peptide to OppBC and simultaneous release of OppA (Salmonella typhimurium)
MNAVIEQRKVLLEIADLKVHFDIKEGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGKVAWLGKDLLGMKADEWREVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQDVRDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKKIQLLEGELPSPINPPSGCVFRTRCPIAGPECAQTRPVLEGSFRHAVSCLKVDPL
>TCDB__Q9X0F3 TM1063, component of Probable rhamnose oligosaccharide porter. Induced by rhamnose
MALLEVKNLKKYFPIIKRGFRRKVVGYLKAVDGISFHIEEGETLGLVGESGCGKTTTAKLIMRGIEPTEGEIVLNMDGEKVDITKLSEKELREKGVRRFLQMIFQDPYSSLNPRMTVRDIIAEPLVVNGVIKGKEEIDAIVSDLLRAVGLRPEYMQRYPHAFSGGQRQRIAIARAIALKPKLVLCDEPTSALDVSVQAQIINLLKDLQKEYNLTYLFISHDLGVVEHITNRVAVMYVGRIVELAETEELFSSPKHPYTEALLSAVPKPDPKRKRKKAQLTGEVPDPSNPPSGCYFHPRCPYAKAICKEVYPDLRNVGTDQNPHLVACHFADSLKLEGVGTM
>ecocyc__OPPF-MONOMER murein tripeptide ABC transporter / oligopeptide ABC transporter ATP binding subunit OppF (EC 7.4.2.6) (Escherichia coli K-12 substr. MG1655)
MNAVTEGRKVLLEIADLKVHFEIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGHVAWLGKELLGMKPDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKMSRQEVRERVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTRALMSAVPIPDPDLEKNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLEGSFRHSVSCLKVDPL
>TCDB__Q9X272 TM1750, component of Probable mannose/mannoside porter. Induced by beta-mannan (Conners et al., 2005). Regulated by mannose-responsive regulator manR
MPFDQGGIKMKPLLQTVDLKKYFPQGKRILKAVDGISIEIKEGETLGLVGESGCGKSTLGRTILKLLRPDGGKIFFEGKDITNLNDKEMKPYRKKMQIIFQDPLGSLNPQMTVGRIIEDPLIIHKIGTKKERRKRVEELLDMVGIGREFINSFPHEFSGGQQQRIGIARALALNPKFIVCDEPVSALDVSIQAQIIDLLEEIQQKMGISYLFIAHNLAVVEHISHKVAVMYLGKIVEYGDVDKIFLNPIHPYTRALLKSVPKIPWDGQKQRFYSLKGELPSPIDLPKGCRFQTRCTEKKAICFEKEPELTEVEKNHFVSCHLVRSYRG
>TCDB__P45094 Dipeptide transport ATP-binding protein DppF, component of The glutathione uptake porter, DppBCDF with the glutathione binding protein, DppA (GbpA; HbpA). Takes up reduced (GSH) and oxidized (GSSG) but not bulky glutathione S conjugates or glutathione derivatives with C-terminal modifications (Haemophilus influenzae)
MTNEVKENTPLLNAIGLKKYYPVKKGLFAKPQQVKALDGVSFQLERGKTLAVVGESGCGKSTLGRLLTMIEEPTKGELYYKGHNFLENDSETKALRRKKIQIVFQNPYASLNPRKKIGSILEEPLIINTKLSAKERREKVLSMMEKVGLRAEFYDRYPHMFSGGQRQRIAIARGLMLDPDVVVADEPVSALDVSVRAQVLNLMMDLQDELGLSYVFISHDLSVVEHIADEVMVMYLGRCIEKGTTEQIFSNPQHPYTKALLSATPRLSPNLRRERIKLTGELPSPINPPKGCAFNPRCWKATEKCRENQPHLEQHTDGKLIACFHID
>TCDB__Q2FZR4 OppF, component of The major oligopeptide uptake porter, Opp-3 (of four paralogues, this is the only one that mediates nitrogen nutrition (Staphylococcus aureus (strain NCTC 8325))
MKNDEVLLSIKNLKQYFNAGKKNEVRAIENISFDIYKGETLGLVGESGCGKSTTGKSIIKLNDITSGEILYEGIDIQKIRKRKDLLKFNKKIQMIFQDPYASLNPRLKVMDIVAEGIDIHHLATDKRDRKKRVYDLLETVGLSKEHANRYPHEFSGGQRQRIGIARALAVEPEFIIADEPISALDVSIQAQVVNLLLKLQRERGITFLFIAHDLSMVKYISDRIAVMHFGKIVEIGPAEEIYQNPLHDYTKSLLSAIPQPDPESERSRKRFSYIDDEANNHLRQLHEIRPNHFVFSTEEEAAQLRENKLVTQN
>ecocyc__DPPF-MONOMER dipeptide ABC transporter ATP binding subunit DppF (EC 7.4.2.9) (Escherichia coli K-12 substr. MG1655)
MSTQEATLQQPLLQAIDLKKHYPVKKGMFAPERLVKALDGVSFNLERGKTLAVVGESGCGKSTLGRLLTMIEMPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSKEQRREKALSMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKDQIFNNPRHPYTQALLSATPRLNPDDRRERIKLSGELPSPLNPPPGCAFNARCRRRFGPCTQLQPQLKDYGGQLVACFAVDQDENPQR
>TCDB__W0WLZ8 Dipeptide transport ATP-binding protein DppF, component of Di- and tri-peptide transporter, DppBCDF with periplasmic substrate binding receptors, A1, A3, A5, A7 and A9, each with differing specificities for peptides (Pseudomonas aeruginosa MH38)
METVLTARDLTRHYEVSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSATPAIHPDPTKPKIRIQGELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLLDQRQVACHHAEQFLG
>SwissProt__A0A0H2ZH52 Di/tripeptide transport ATP-binding protein DppF; EC 7.4.2.9 (Pseudomonas aeruginosa (strain UCBPP-PA14))
METVLTARDLTRHYEVSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSATPAIHPDPTKPKIRIQGELPNPLHPPEGCAFHKRCPYATERCRSEVPELRLLDQRQVACHHAEQFLG
>SwissProt__A2RI78 Dipeptide transport ATP-binding protein DppF; EC 7.4.2.9 (Lactococcus lactis subsp. cremoris (strain MG1363))
MTEPKKVVEIKNLDLTFNKGKKGANKAINNVSLDIYEGETFGLVGESGSGKTTIGRAILKLYDNFITGGEILFEGKDVRNLKGSELREYRSEAQMIFQDPQASLNGRMRVKDIVAEGLDANGLVKTKAERDARVLELLRLVGLNDDHLTRYPHEFSGGQRQRIGIARALAVKPKFVVADEPISALDVSIQAQVVNLMRDIQAKENLTYLFIAHDLSMVKYISDRIGVMHWGKILEVGTSEQVYNHPIHPYTKSLLSSIPSPDPISERQRTPIVYDPTAELDGQEREMREITPGHFVFSTEAEAEVYKKNATL
>TCDB__Q9CIK8 Oligopeptide ABC trasporter ATP binding protein, component of The ABC peptide/signalling peptide transporter. OptA binds peptides of 3-6 aas; OptS binds dipeptides. OptB,C,D are most similar to 3.A.1.5.19 (Lactococcus lactis subsp. lactis)
MMTEPKKVIEIKNLDLTFNKGKKGANKAINNVSLDIYEGETFGLVGESGSGKTTIGRAILKLYDNFITGGEILFEGKDVRNLKGSELREYRSEAQMIFQDPQASLNGRMRVKDIVAEGLDANGLVKTKAERDARVLELLRLVGLNDDHLTRYPHEFSGGQRQRIGIARALAVKPKFVVADEPISALDVSIQAQVVNLMRDIQAKENLTYLFIAHDLSMVKYISDRIGVMHWGKILEVGTSDQVYNHPIHPYTKSLLSSIPSPDPISERERTPIVYDPTAELDGQEREMREITPGHFVFSTEAEAEIYKKNATV
>BRENDA__Q73NS6 ABC-type dipeptide transporter (EC 7.4.2.9) (Treponema denticola)
MSDNEKKIDPNDHVLELINIKKYFEPHQGFVQSLSKGTAKKIKAVDDVTLRLRRGEIFGLIGESGSGKTTIGKIAMKLHTPTEGTILYNGEDVTNSDKEKTAFYRRRVQMIFQDPYASMNPRFKIRDVMEEPLLIHKIKGTRAENDEKIIKAISEVKLNPPEEFMTRYPHMLSGGQRQRIATARTLILNPEVIVADEPVSMIDLSTRAEILHMMREVQRKLGLTYLYITHDLSTARYFTDRIAVMYLGRIVEMGDADDVIDNPMHPYTQALIEAVPEPKPGMLEVIKKLPISGEIPSPANVPSGCRFHTRCPYADESCSSMEEPSLMDIGKGHFHACRKAEEIKKG
>BRENDA__Q8ZQM4 ABC-type glutathione transporter (EC 7.4.2.10) (Salmonella enterica subsp. enterica serovar Typhimurium)
MPHSDELDSRDVLSVSGLNIAFHHEGQQVDAVRNVSLRLKRGETLAIVGESGSGKSVTALALMRLIEQSGANVRCGEMLLRRRNRQVIELSEQSDAQMRRVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEALAEAKRMLDQVRIPESQAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQEMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPTHPYTQTLLAAVPQLGAMRGHSLPRRFPLISADEPALYESQIEQDTVVEGEPILQVRGLVTRFPLRSGLFNRVTREVHAVENISFDLWPGETLSLVGESGSGKSTTGRALLRLVESRQGEIIFNGQRIDTLSAGKLQPLRRDIQCIFQDPYASLDPRQTVGYSIMEPLRIHGLGQGDAAAKRVAWLLERVGLRPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSVRGQIINLLLDLQREMGIAYLFISHDMAVVERISHRVAVMYLGQIVEMGPRRAVFENPQHPYTRKLMAAVPVADPSRHRPRRVLLSDDIPSNIHKRGEETPAVSLQLVGPGHYVARPLQDNALSRL
>ecocyc__YLIA-MONOMER glutathione ABC transporter ATP binding subunit GsiA (EC 7.4.2.10) (Escherichia coli K-12 substr. MG1655)
MPHSDELDAGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLQRRSREVIELSEQNAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQAPPIEQKTVVDGEPVLRVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKDAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPVAEPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFMRR
>TCDB__O31310 OppF, component of The oligopeptide transporter OppA1-5, B1, C1, DF (functions with five binding proteins of differing induction properties and peptide specificities; OppA1-3 are chromosomally encoded; OppA4 and 5 are plasmid encoded.) (Borrelia burgdorferi (Lyme disease spirochete))
MSSKKEIILKVENLMQTFTTGEDFLFWKNKQKVNAVNNVSFEVEKNKTLGLVGESGCGKSTTLRSIMQLYTPTSGNIYFNGKNITKLSKKELLKTKKDMQMVFQDPHTSLDPRMTIKEIIAEPLEIYNENKILPKTKQEIEQRVNELTDIVGLHKSMLTRYPHEFSGGQRQRIGIARALALNPKLLLLDEAVSALDVSIRAQILNLLKALQKEFNLSYLFISHDLAVVKYMSDKIAVMYLGVILELAPRETLFSNPIHPYTKMLIASIPEINPEKRKNKNIKLDEQTLANIRKIHLSTQVHPKLEEVEKDHFVSKYLFDEMNR
>BRENDA__A0A150QXP6 5-(carboxyamino)imidazole ribonucleotide mutase (EC 5.4.99.18) (Bacillus anthracis)
MAPSPLLSVQDLRVEFITPTGPVCAVDNVSFDIAPGEVLGLAGESGSGKSTVAMAIMRLLRPPAIITGGRVLFAGQDVLSMTEEQLRAFRWRKMALVFQSAMTALNPVLTIGEQIADPIIAHDGVTQAQAMERAAALLKLVNIDPSRLTSYPHQLSGGMRQRVVIAIAMALKPPFLIMDEPTTALDVVVQREILQQIAELKERLGFSILFITHDLSLIAEFSTRIAILYAGKLAETARAKDLFSDPKHPYTQGLLGSFPSVRGPRRRLQGIPGSPPDMRNPPSGCRFHPRCPQAFATCQNELPVLREIAPEHRGACHLY
>TCDB__P63395 Uncharacterized ABC transporter ATP-binding protein Rv1281c/MT1318, component of The glutathione transporter, OppA (Dasgupta et al., 2010). OppA binds glutathione and the nanopeptide, bradykinin. Also regulates cytokine release, apoptosis and the innate immune response of macrophages infected with M. tuberculosis (Mycobacterium tuberculosis)
MSPLLEVTDLAVTFRTDGDPVTAVRGISYRVEPGEVVAMVGESGSGKSAAAMAVVGLLPEYAQVRGSVRLQGTELLGLADNAMSRFRGKAIGTVFQDPMSALTPVYTVGDQIAEAIEVHQPRVGKKAARRRAVELLDLVGISQPQRRSRAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLKAARDVTGAGVLIITHDLGVVAEFADRALVMYAGRVVESAGVNDLYRDRRMPYTVGLLGSVPRLDAAQGTRLVPIPGAPPSLAGLAPGCPFAPRCPLVIDECLTAEPELLDVATDHRAACIRTELVTGRSAADIYRVKTEARPAALGDASVVVRVRHLVKTYRLAKGVVLRRAIGEVRAVDGISLELRQGRTLGIVGESGSGKSTTLHEILELAAPQSGSIEVLGTDVATLGTAERRSLRRDIQVVFQDPVASLDPRLPVFDLIAEPLQANGFGKNETHARVAELLDIVGLRHGDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIINLLLDLQEQFGLSYLFVSHDLSVVKHLAHQVAVMLAGTVVEQGDSEEVFGNPKHEYTRRLLGAVPQPDPARRG
>TCDB__Q9X0F4 TM1064, component of Probable rhamnose oligosaccharide porter. Induced by rhamnose
MSTLLQIKNLRTYFFTDEGVVKAVDGVSFEIEEGRTLGVVGESGCGKSVTARSIIKLLSTAGRIVSGEILYNMDGQMVDLVKFSKEEIRKVRGRHIAMIFQEPMAAFSPVYTIGDQITEGMIYHFGITKQEARERAVELLRRVGIPKPEKMIDSYPFEYSGGMRQRAMIAMALSCNPRLLIADEPTTALDVTIQAQVLDLLKDLQQEYKMAIMMITHNMGVVAEMADHVVVMYLGRVVESAPVEELFYNPKHPYTSLLLRSIPVVGKRVERLEVIEGDVPDPRNMPKGCRFHPRCPYMMKGICDEREPVEVEVGPEHRVSCFLYGGEKDGAS
>TCDB__Q9X271 TM1749, component of Probable mannose/mannoside porter. Induced by beta-mannan (Conners et al., 2005). Regulated by mannose-responsive regulator manR
MMELLNVNNLKVEFHRVEGIVKAVDGISYKLNKGESLGIVGESGSGKSVSVLSLLRLINRNGRIVDGEAIFLGKDLLKLNKEELRNIRGKDISIIFQNPMTSLNPIIRVGIQVMEPIIWHRLMKNEEARERAIELLERVGIPESPKRFLNYPFQFSGGMRQRVMIAMALACHPKLLIADEPTTALDVTIQAQIMELLQELKEEYGMSVIFITHDLSVATNFCDRIITMYAGKIVEEAPVEEILKTPLHPYTKGLLNSTLEIGSRGKKLVPIPGNPPNPTKHPSGCKFHPRCSFAMEICQREEPPLVNISENHRVACHLIKGESK
>TCDB__P0A2V4 OppF, component of Oligopeptide porter (transports peptides of 4-35) amino acyl residues; di- and tripeptides are not transported; hydrophobic basic peptides are preferred). OppA determines the specificity of the system (Doeven et al., 2004). A large cavity in OppA binds proline-rich peptides preferentially (Berntsson et al., 2009). Two crystal structures of OppA with different nonapeptides show binding in different registers (Lactococcus lactis subsp. lactis (Streptococcus lactis))
MSEILNLKDLKVYYPIRSGFFNRVTDNVLAVDGVDLTIHEGETVGLVGESGSGKSTIGKTIVGLEQMTSGQLIYKGQDVSKKKIRNQLKYNKDVQMIFQDAFSSLNPRKTIYDIIAEPIRNFEKIDANTENKRIHELLDIVGLPKQALEQYPFQFSGGQQQRIGIARAVATNPKLIVADEPVSALDLSVQAQVLNFMKLIQKDLGIAFLFISHDLGVVRHMTDNIAVMHNGRIVEKGTRRDIFDEPQHIYTKRLLSAIPSIDVTRRAENRKNRLKVEQDFEDKKANFYDKDGHALPLKKLSESHWAALPKGGENVESNY
>ecocyc__YDDO-MONOMER putative D,D-dipeptide ABC transporter ATP-binding subunit DdpF (Escherichia coli K-12 substr. MG1655)
MSDTLLTLRDVHINFPARKNWLGKTTEHVHAINGIDLQIRRGETLGIVGESGCGKSTLAQLLMGMLQPSHGQYIRSGSQRIMQMVFQDPLSSLNPRLPVWRIITEPLWIAKRSSEQQRRALAEELAVQVGIRPEYLDRLPHAFSGGQRQRIAIARALSSQPDVIVLDEPTSALDISVQAQILNLLVTLQENHGLTYVLISHNVSVIRHMSDRVAVMYLGQIVELGDAQQVLTAPAHPYTRLLLDSLPAIDKPLEEEWALRKTDLPGNRTLPQGCFFYERCPLATHGCEVRQSLAIREDGRELRCWRAL
>TCDB__P04285 OppD aka STM1743, component of Oligopeptide porter (also takes up amino glycoside antibiotics such as kanamycin, streptomycin and neomycin as well as cell wall-derived peptides such as murein tripeptide). It transports substrate peptides of 2-5 amino acids with highest affinity for tripeptides. Also transports δ-aminolevulinic acid (ALA). [May be regulated by PTS Enzyme INtr-aspartokinase.] ATP-binding to OppDF may result in donation of peptide to OppBC and simultaneous release of OppA (Salmonella typhimurium)
MSLSETATQAPQPANVLLEVNDLRVTFATPDGDVTAVNDLNFTLRAGETLGIVGESGSGKSQTAFALMGLLATNGRIGGSATFNGREILNLPERELNTLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGKARDVFYQPVHPYSIGLLNAVPRLDSEGAEMLTIPGNPPNLLRLPKGCPFQPRCPHAMEICNNAPPLEAFSPGRLRACFKPVEELL
>ecocyc__OPPD-MONOMER murein tripeptide ABC transporter / oligopeptide ABC transporter ATP binding subunit OppD (EC 7.4.2.6) (Escherichia coli K-12 substr. MG1655)
MSVIETATVPLAQQQADALLNVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPEHELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKNMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLVVVAGICDKVLVMYAGRTMEYGNARDVFYQPVHPYSIGLLNAVPRLDAEGETMLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAPPLEEFTPGRLRACFKPVEELL
>TCDB__Q9F9T4 EppD, component of The Ethylene diamine tetraacetate (EDTA) uptake porter, EppABCD
MRPHMSESVHIAGGTGAPLVSVSGLTVSFDRHREEPIEAVRDVSWSIGSGEVLALVGESGSGKSVSALAVMGLLPRNARVAGSIRWRGEELLGASEKRRRALRGSRIGLVPQDPMTSLNPVYTIGAQIREGIRAHQKLSEREMAERTLELLETMGIPHARERMNSYPHELSGGMRQRVVIAMAMANNPDLIIADEATTALDVTVQAQVLDALKKAQALTGAALLLITHDLGVVAGRADRVAVMQRGEVVEQGTVDEIFYQPASSYTRKLLHSIPRLNHTPDLSAPSDVAPDAEVIHSAFERKVGAEGAPILSMRNVGKHFPVYSRGVIRGRVGVIKAVAGVDLDVEAGTTLGIVGESGSGKTTLIRSLFNLEPITHGTILFDGQDVHRMPPRDRRRMRKCVQMVFQDPYASLDPMMTVRDILMEPAVINRMDRKLAERRVMELLERVHLKPEHAARYPNEFSGGQRQRIAIARALMLYPRLLVLDEPVSSLDVSIQAEVLTLLKELQKDLNLSYLFVSHDLSVVAEIAHSVIVMYRGRIVERGRVDELFRNPKHPYTRALLSAVPIPDPRTERRRERIVFNSDTLASPITPVERTGMWRRLFGGRTQEAS
>TCDB__P42064 AppD, component of 5-6 amino acyl oligopeptide transporter AppA-F (Bacillus subtilis)
MSTLLEVNNLKTYFFRKKEPIPAVDGVDFHISKGETVALVGESGSGKSITSLSIMGLVQSSGGKIMDGSIKLEDKDLTSFTENDYCKIRGNEVSMIFQEPMTSLNPVLTIGEQITEVLIYHKNMKKKEARQRAVELLQMVGFSRAEQIMKEYPHRLSGGMRQRVMIAIALSCNPKLLIADEPTTALDVTIQAQVLELMKDLCQKFNTSILLITHDLGVVSEAADRVIVMYCGQVVENATVDDLFLEPLHPYTEGLLTSIPVIDGEIDKLNAIKGSVPTPDNLPPGCRFAPRCPKAMDKCWTNQPSLLTHKSGRTVRCFLYEEEGAEQS
>TCDB__Q9WXT0 TM0075, component of Probable xylan oligosaccharide porter (Conners et al., 2005). Induced by xylan and xylose. Regulated by xylose-responsive regulator XylR
MPLLEIKNLTKIFTIGSIFSRTRIVAVDNVNFDINEAEIFTLAGESGCGKTTTAKIILGFEEPTSGEIIYKGRKIDRVHQNEKERRELLKEIQAVFQNPFSTFNPLRKVDRYFYETLFNLGIADTKKKAEEIIKEKLSAVGISFEEFSEKYPSEFSGGQLQRISIARALLTNPSLLVADEPVSMVDASLRMSIVNLFKDLKEQYGVSVLYITHDLTTAYYVSDRIAVMFRGNIVELGPAEKVLMEPKHPYTQLLRESVPEPDPKKKWDIRIKLSETEQAEYLRQGCKFAGRCPKAMDICRKEPPPYFEVDGVQVKCWLYR
>TCDB__O30542 AccC, component of Agrocinopine (an opine)/Agrocin 84 (an antibiotic) porter (Agrobacterium radiobacter)
MSAPLLQARGVTKVFRLKSGLFVKPSVHVAVNSIDLELAPRERVGVVGESGSGKSTLGRLLLGLTSTTEGEVLFEGLAHTDRSARDWSTFRKETSLVQQNPLSALNPQMTIGEQIAEAVWVHRVANAGARDRAATMLDRVGLSSAMMNRYPHQMSGGQRQRVVIARALILDPKLVVFDEAVSALDVSVQAQVVALLRQLWQELDLAYVFITHDLRIVRHLVDRIVVMYLGRVVETGDIKSVYAWPRHPYTRALLASVPTMDPTVRNIEPPIKGELDAGKVMTGCAFRSRCPFAIERCAKETPLLRPAGGQLAACHRAEEFPRSIVAQTDPAQMMEVAR
>TCDB__B1W1L9 Putative peptide ABC transporter ATP-binding protein, component of The ABC BldKA-E (SGR_2418-2414) oligopeptide transport system. It controls aerial mycelium formation on glucose media. Probably involved in extracellular peptide signalling (Akanuma et al. 2011).  Probably orthologous to 3.A.1.5.35 (Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350))
MSGDGPLLDVRDLHVEFHTRDGVAKAVNGVNYTVSAGETLAVLGESGSGKSVTAQTIMGILDMPPGKITQGEILFRGQDMLKMSNEERRKIRGRKIAMIFQDALSSLNPVLSVGYQLGEMFRVHQGLSKKEAKAKSIELMDQVKIPAAAARISDFPHQFSGGMRQRIMIAMALALEPDLIIADEPTTALDVTVQAQVMDLLAELQREYNMGLILITHDLGVVADVADKIAVMYAGRIVETAPVDELYSRPAHPYTKGLLESIPRLDQKGQELYAIKGLPPNLTRIPAGCAFSPRCPKAQDICRTDVPPLVPVTEQDGLELVGRGSACHFWKETIHG
>TCDB__F0TFS9 Oligopeptide ABC transporter ATP-binding protein, component of ABC α-galactoside uptake porter (Lactobacillus acidophilus (strain 30SC))
MGKEIIQIKDLKVYYPIRSGFWNRITDYVRAVDGVNFSIGEGETYGLIGESGSGKSTTGKVIVGVEKATSGQIMYKGLDVTKASNRRKLDYNKDVQMIFQDSMSSLNPRKRIEDIIAEPIRNFENLTTDQERDRVQELLDIVGMPSDAIYKYPHEFSGGQRQRIGVARAVATNPKLIVADEPTSALDLSVQAQVLNFMKHIQQQYNIAYLFISHDLGVVKHMSENLAIMHRGRLVELGSRDEIYKHPIHIYTKRLLSAIPRVDVEHREEHKKHREQVEREFKENQSKWYDENGRVYPLQKVAPNHWVALPKDMAQEAKIEEREEKESD
>reanno__Smeli_SM_b21644 ABC transporter for D-Raffinose, ATPase component (Sinorhizobium meliloti 1021)
MVTIESIVPAPEERRDRDMKDERPVIDARKVAVSFKVENGTVQAVKDVSFQLYRGETVAIVGESGSGKSVTARTVMGLLSKRATIAPQARIEYDGRDVLKFSKRERRALRGDRISMIFQEPMSSLNPVYTIGSQIIEAIRAHRRVSRRAAAERALELLRHVQIPDPEARLNQYPHQLSGGQRQRVMIAMALANDPDVLIADEPTTALDVTVQAQILNLIRKLQQELGMAVILITHDLTVVRQFSDYVYVMQLGEVKEHNTTEALFADPQHAYTRRLLSSEPSGSANPLPDDAPILLDGRNVRVSFTLKKGGFFRPEFKELVAVDGLSLNLRRHETLGLVGESGSGKTTFGQALIRLLNTDGGEIYFEGEPIHDKDRKGMRPLRSKIQIVFQDPFSSLNPRMSVGQIIEEGLIVNGMGENRKDRLKRVEDALVSAGMPSNILSRFPHEFSGGQRQRIAIARAVALEPEFILLDEPTSALDLSVQAQIIELLRRLQDERGLSYLVISHDLKVVRALCHRVVVMQDGKIVEEGPVSEVLNNPKTAYTERLVKAAFEVAA
>ecocyc__SAPD-MONOMER putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) (Escherichia coli K-12 substr. MG1655)
MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYACHFPLNMEKE
>biolip__4fwiB Crystal structure of the nucleotide-binding domain of a dipeptide abc transporter
SIIIRVEDLRAVYLVREGTIKAADGISLDILENSVTAIVGESASGKSTIIEAMTKTLPPNGRILSGRVLYKGKDLLTMREEELRKIRWKEIALVPQAAQQSLNPTMKVIEHFKDTVEAHGVRWSHSELIEKASEKLRMVRLNPEAVLNSYPLQLSGGMKQRVLIALALLLDPVVLILDEPTSALDVLTQAHIIQLLKELKKMLKITLIFVTHDIAVAAELADKVAVIYGGNLVEYNSTFQIFKNPLHPYTRGLINSIMPIPGDPPSLLNPPSGCRFHPRCEYAMEICKKEKPKWIRLDGEAHVACHLYEE
>SwissProt__Q8RDH4 Dipeptide transport ATP-binding protein DppD; EC 7.4.2.9 (Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis))
MSIIIRVEDLRAVYLVREGTIKAADGISLDILENSVTAIVGESASGKSTIIEAMTKTLPPNGRILSGRVLYKGKDLLTMREEELRKIRWKEIALVPQAAQQSLNPTMKVIEHFKDTVEAHGVRWSHSELIEKASEKLRMVRLNPEAVLNSYPLQLSGGMKQRVLIALALLLDPVVLILDEPTSALDVLTQAHIIQLLKELKKMLKITLIFVTHDIAVAAELADKVAVIYGGNLVEYNSTFQIFKNPLHPYTRGLINSIMAVNADMSKVKPIPGDPPSLLNPPSGCRFHPRCEYAMEICKKEKPKWIRLDGEAHVACHLYEEGRPLK
>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
>PDB_7z18_I E. Coli c-p lyase bound to a phnk abc dimer and atp
QPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSISARLTPQQGEIHYENRSLYAMSEADRRRLLR
TEWGVVHQHPLDGLRRQVSAGGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQRLQIARNLVT
HPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIVTHDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYT
QLLVSSVLQN
>biolip__7z15I E. Coli c-p lyase bound to a phnk/phnl dual abc dimer and adp + pi
QPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSISARLTPQQGEIHYENRSLYAMSEADRRRLLRTEWGVVHQHPLDGLRRQVSAGGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQRLQIARNLVTHPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIVTHDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYTQLLVSSVLQNENL
>PDB_7z16_I E. Coli c-p lyase bound to phnk/phnl dual abc dimer with amppnp and phnk e171q mutation
QPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSISARLTPQQGEIHYENRSLYAMSEADRRRLLR
TEWGVVHQHPLDGLRRQVSAGGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQRLQIARNLVT
HPKLVFMDQPTGGLDVSVQARLLDLLRGLVVELNLAVVIVTHDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYT
QLLVSSVLQN
>PDB_7ahh_C Opua inhibited inward-facing, sbd docked
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTS
GKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYP
KQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGK
IMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAA
RKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>biolip__7aheC Opua inhibited inward facing
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTSGKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYPKQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGKIMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAARKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>biolip__4u00A Crystal structure of ttha1159 in complex with adp
PIIRIRNLHKWFGPLHVLKGIHLEVAPGEKLVIIGPSGSGKSTLIRTINRLEDFQEGEVVVDGLSVKDDRALREIRREVGMVFQQFNLFPHMTVLENVTLAPMRVRRWPREKAEKKALELLERVGILDQARKYPAQLSGGQQQRVAIARALAMEPKIMLFDEPTSALDPEMVGEVLDVMRDLAQGGMTMVVVTHEMGFAREVADRVVFMDGGQIVEEGRPEEIFTRPKEERTRSFLQRVLH
>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
>PDB_3c4j_A Abc protein artp in complex with atp-gamma-s
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREE
VGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIM
LFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSK
VF
>biolip__3c41J Abc protein artp in complex with amp-pnp/mg2+
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREEVGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIMLFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSKVF
>PDB_2olk_A Abc protein artp in complex with adp-beta-s
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREE
VGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIM
LFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSK
VF
>PDB_2olj_A Abc protein artp in complex with adp/mg2+
LQMIDVHQLKKSFGSLEVLKGINVHIREGEVVVVIGPSGSGKSTFLRCLNLLEDFDEGEIIIDGINLKAKDTNLNKVREE
VGMVFQRFNLFPHMTVLNNITLAPMKVRKWPREKAEAKAMELLDKVGLKDKAHAYPDSLSGGQAQRVAIARALAMEPKIM
LFDEPTSALDPEMVGEVLSVMKQLANEGMTMVVVTHEMGFAREVGDRVLFMDGGYIIEEGKPEDLFDRPQHERTKAFLSK
VF
>metacyc__G185E-5409-MONOMER ABC-type trehalose transporter ATP-binding protein (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MAEIVLDHVNKSYPDGHTAVRDLNLTIADGEFLILVGPSGCGKTTTLNMIAGLEDISSGELRIAGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKMRKADIAQKVSETAKILDLTNLLDRKPSQLSGGQRQRVAMGRAIVRHPKAFLMDEPLSNLDAKLRVQMRGEIAQLQRRLGTTTVYVTHDQTEAMTLGDRVVVMYGGIAQQIGTPEELYERPANLFVAGFIGSPAMNFFPARLTAIGLTLPFGEVTLAPEVQGVIAAHPKPENVIVGVRPEHIQDAALIDAYQRIRALTFQVKVNLVESLGADKYLYFTTESPAVHSVQLDELAEVEGESALHENQFVARVPAESKVAIGQSVELAFDTARLAVFDADSGANLTIPHRA
>biolip__2d62A Crystal structure of multiple sugar binding transport atp- binding protein
MIGMAEVKLINIWKRFGDVTAVKDLSLEIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTRGQIYIEDNLVADPEKGVFVPPKERDVAMVFQSYALYPHMTVYDNIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIIRRPKVFLMDEPLSNLDAKLRVKMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNKGELQQVGTPDEVYYKPVNTFVAGFIGSPPMNFLDATITDDGFLDFGEFKLKLLQDQFEVLEEENMVGKEVIFGIRPEDVHDASFTHIDVPEENTVKATVDIIENLGGEKIVHLRRGNISFTAKFPKESKVREGDEVSVVFDMKKIHIFRKDTEKAIF
>SwissProt__Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA1; ECF transporter A component EcfA1; EC 7.-.-.- (Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311))
MIEIKNLKFKYNQDQTSYTLNDVSFHVKHGEWLSIVGHNGSGKSTTARLIGGLLVADSGQIIVDGQELTEETVWDIRDKIGMVFQNPDNQFVGATVEDDVAFGLENKGLPYKEMVSRVQEALSFVGMMDFKDREPARLSGGQKQRVAIAGIIAMRPSILILDEATSMLDPEGRQELIQYIEDIRQQYGMTVLSITHDLDEVAMSNRVLVLKQGKVESISSPRELFSRGSELVDLGLDIPFSALLTQKLKNQGLIDCEGYLTEKELVEQLWEYLSKM