>Dsui_0415 FitnessBrowser__PS:Dsui_0415
MSAPLVSIQDLTVQFNGARRASALNQVSLELGQGEVLGLLGESGSGKSVTLRTLLRLHPERHTRTAGRIRVDGQDVLALRGRELDRYRGGTVSMVFQEPGLAFDPVYTIGQQISEAVRVHEGVDQATAAARALAMLERVQIPQARRRFDAYPHELSGGMRQRAMIALALACKPKLLLADEPTTALDATVQIQILLLLRELQRETGMSVIFVTHDIGAAVEVADRIAVMYAGRIVEQGPVGQLVRQPCHPYTRGLLAATVGHEHRGRPLEAIPGSPPDLAALPPGCSFAPRCSHASERCHRDIPPLEQQGARTLACWHPVRLLGEAA
>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__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__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
>TCDB__Q93IU0 BldKD, putative ABC transporter intracellular ATPase 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))
MTTQTKPEEAPAAAAGDAFLSVRDLKVHFSTEGGVVKAVDGLSFDLERGKTLGIVGESGSGKSVTNLAVLGLHDRRRTAIDGSITLDGQELTDASEKQLEKLRGKKMAMIFQDALTALSPYYTVGRQIAEPFMKHNGASKKDARVRAIDLLQKVGIPHPQKRVDDYPHQFSGGMRQRAMIAMALSCNPDLLIADEPTTALDVTVQAQILDLLKDLQQEFGSAIIMITHDLGVVGNMADDIMVMYAGRAVERGTVREVLKSPQHPYTWGLLSSMPNLTSDVDEPLMPIPGSPPSLMNPPSGCAFHPRCGFTDLVSGERCSGERPTLPHGRAAACHLTGDQRQQVFIEKIQPRLG
>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
>SwissProt__A0A0H2ZGN6 Di/tripeptide transport ATP-binding protein DppD; EC 7.4.2.9 (Pseudomonas aeruginosa (strain UCBPP-PA14))
MSLLDIKNLSVRFGDTTAVPVVDGLDLSVDKGEVLAIVGESGSGKSVTMMALMGLIDAPGWVSADHLRFDGHDMLTLKGRQRRRIVGKDMAMVFQDPMTALNPSYTVGYQIEEVLRLHLGLRGKALRQRALELLERVEIPAAASRLDAYPHQLSGGMSQRVAIAMAIAAEPKLLIADEPTTALDVTIQAQIMELLLNLQRDQDMALILITHDLAVVAETAQRVCVMYAGEAVEIGGVPALFDRPTHPYTEALIKAIPEHCAGEARLATLPGIVPGRYDRPRGCLLSPRCPYAQEHCRQERPALEAHERGAVRCFYPLNLLNEVA
>BRENDA__Q5V9R9 ABC-type oligopeptide transporter (EC 7.4.2.6) (Vibrio fluvialis)
MSLLDVKDLRVEFTTQDGIVTAVNDLNFSLKQGETLGIVGESGSGKSQTVFAIMGLLAKNGKISGSAKFEGKEILNLPEKELNKVRSEQIAMIFQDPMTSLNPYMKVSDQLMEVLMPHKGMGKAEAFEESVRMLEAVKIPEARKRITMYPHEFSGGMRQRVMIAMALLCRPKRLIADEPTTALDVTVQAQIMDLLNELKREFNTAIIMITHDLGVVAGSCDKVLVMYAGRTMEYGSVNEIFYNPSHPYAEGLLKAIPRLDTEGEILPTIPGNPPNLLRLPVGCPYQERCHRVMDRCKREAPILTPFGDGRQRACFSDWETWTK
>ecocyc__YDDP-MONOMER putative D,D-dipeptide ABC transporter ATP-binding subunit DdpD (Escherichia coli K-12 substr. MG1655)
MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIDLLEEMQIPDAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQCENVPALTACGDNNQRCACWYPQQEVISV
>SwissProt__P24136 Oligopeptide transport ATP-binding protein OppD; Stage 0 sporulation protein KD (Bacillus subtilis (strain 168))
MIRVTRLLEVKDLAISFKTYGGEVQAIRGVNFHLDKGETLAIVGESGSGKSVTSQAIMKLIPMPPGYFKRGEILFEGKDLVPLSEKEMQNVRGKEIGMIFQDPMTSLNPTMKVGKQITEVLFKHEKISKEAAKKRAVELLELVGIPMPEKRVNQFPHEFSGGMRQRVVIAMALAANPKLLIADEPTTALDVTIQAQILELMKDLQKKIDTSIIFITHDLGVVANVADRVAVMYAGQIVETGTVDEIFYDPRHPYTWGLLASMPTLESSGEEELTAIPGTPPDLTNPPKGDAFALRSSYAMKIDFEQEPPMFKVSDTHYVKSWLLHPDAPKVEPPEAVKAKMRKLANTFEKPVLVREVE
>TCDB__P26905 DppD aka DCIAD, component of Dipeptide porter. Also transports δ-aminolevulinic acid (ALA) and heme (Bacillus subtilis)
MEKVLSVQNLHVSFTTYGGTVQAVRGVSFDLYKGETFAIVGESGCGKSVTSQSIMGLLPPYSAKVTDGRILFKNKDLCRLSDKEMRGIRGADISMIFQDPMTALNPTLTVGDQLGEALLRHKKMSKKAARKEVLSMLSLVGIPDPGERLKQYPHQFSGGMRQRIVIAMALICEPDILIADEPTTALDVTIQAQILELFKEIQRKTDVSVILITHDLGVVAQVADRVAVMYAGKMAEIGTRKDIFYQPQHPYTKGLLGSVPRLDLNGAELTPIDGTPPDLFSPPPGCPFAARCPNRMVVCDRVYPGQTIRSDSHTVNCWLQDQRAEHAVLSGDAKD
>TCDB__P45095 Dipeptide transport ATP-binding protein DppD, 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)
MALLDVKELSVHFGDKKTPFKAVDRISYQVAQGEVLGIVGESGSGKSVSSLAIMGLIDHPGRVSAESLQFENTDLLTLESKAKRQLIGADVAMIFQDPMTSLNPAYTVGFQIMEALKTHEGGTKKARKDRTLELLKLVGIPDPESRIDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIMELLLELQKKECMSLILITHDLALVAEAAERIIVMYAGQIVEEGTAKDIFREPKHPYTQALLRSLPEFAEGKSRLESLQGVVPGKYDRPTGCLLNPRCPYATEYCRQVEPQLHHIGSRKVKCHTPLNEQGNPVEYQGA
>TCDB__Q9X0F4 TM1064, component of Probable rhamnose oligosaccharide porter. Induced by rhamnose
MSTLLQIKNLRTYFFTDEGVVKAVDGVSFEIEEGRTLGVVGESGCGKSVTARSIIKLLSTAGRIVSGEILYNMDGQMVDLVKFSKEEIRKVRGRHIAMIFQEPMAAFSPVYTIGDQITEGMIYHFGITKQEARERAVELLRRVGIPKPEKMIDSYPFEYSGGMRQRAMIAMALSCNPRLLIADEPTTALDVTIQAQVLDLLKDLQQEYKMAIMMITHNMGVVAEMADHVVVMYLGRVVESAPVEELFYNPKHPYTSLLLRSIPVVGKRVERLEVIEGDVPDPRNMPKGCRFHPRCPYMMKGICDEREPVEVEVGPEHRVSCFLYGGEKDGAS
>TCDB__Q9WXR4 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))
MEKVLEIRDLKVYFDLTEGTVKAVDGVSFDIRRGEILGLVGESGCGKSVTAQSILRILPKSARIVNGEIVFHRNGKTLDLTRLDPEGEEIRDIRGKDISMIFQEPMASFSPVYTVGAQMIEAILLHENVSKEEARKRVVEMLKKVKIPNAEKVVDMYPFELSGGMLQRCMIAMAMSLNPTLLLADEPTTALDVTIQAQILYLMKELQKEYHSSILLITHDMGVVAQMADRVAVMYLGNIVETAEVFELFKNPLHPYTQALLRSIPKIGIRKTRLETIKGMVPDPYNLPTGCRFHNRCEKFMKGLCDVKEPPEVEVKPGHKVKCFLYGGEKE
>TCDB__Q2FZR5 OppD, 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))
MTERILEVNDLHVSFDITAGEVQAVRGVDFYLNKGETLAIVGESGSGKSVTTKAITKLFQGDTGRIKKGEILFLGEDLAKKPENELIKLRGKDISMIFQDPMTSLNPTMQIGKQVMEPLIKHKNYSKAQAKKRALEILNLVGLPNAEKRFKAYPHQFSGGQRQRIVIATALACEPKVLIADEPTTALDVTMQAQILDLMKELQQKIDTAIIFITHDLGVVANIADRVAVMYGGQMVETGDVNEIFYDPKHPYTWGLLSSMPDLSTTNDTPLLAIPGAPPDLLHPPKGDAFARRSQYALDIDFKVEPPWFKVSPTHFVKSWLLDARAPKVELPELVKQRMKPMPNNYEKPLKVERVSFNEK
>TCDB__P42064 AppD, component of 5-6 amino acyl oligopeptide transporter AppA-F (Bacillus subtilis)
MSTLLEVNNLKTYFFRKKEPIPAVDGVDFHISKGETVALVGESGSGKSITSLSIMGLVQSSGGKIMDGSIKLEDKDLTSFTENDYCKIRGNEVSMIFQEPMTSLNPVLTIGEQITEVLIYHKNMKKKEARQRAVELLQMVGFSRAEQIMKEYPHRLSGGMRQRVMIAIALSCNPKLLIADEPTTALDVTIQAQVLELMKDLCQKFNTSILLITHDLGVVSEAADRVIVMYCGQVVENATVDDLFLEPLHPYTEGLLTSIPVIDGEIDKLNAIKGSVPTPDNLPPGCRFAPRCPKAMDKCWTNQPSLLTHKSGRTVRCFLYEEEGAEQS
>BRENDA__A0A150QXP6 5-(carboxyamino)imidazole ribonucleotide mutase (EC 5.4.99.18) (Bacillus anthracis)
MAPSPLLSVQDLRVEFITPTGPVCAVDNVSFDIAPGEVLGLAGESGSGKSTVAMAIMRLLRPPAIITGGRVLFAGQDVLSMTEEQLRAFRWRKMALVFQSAMTALNPVLTIGEQIADPIIAHDGVTQAQAMERAAALLKLVNIDPSRLTSYPHQLSGGMRQRVVIAIAMALKPPFLIMDEPTTALDVVVQREILQQIAELKERLGFSILFITHDLSLIAEFSTRIAILYAGKLAETARAKDLFSDPKHPYTQGLLGSFPSVRGPRRRLQGIPGSPPDMRNPPSGCRFHPRCPQAFATCQNELPVLREIAPEHRGACHLY
>ecocyc__DPPD-MONOMER dipeptide ABC transporter ATP binding subunit DppD (EC 7.4.2.9) (Escherichia coli K-12 substr. MG1655)
MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLADGRQSKCHYPLDDAGRPTL
>TCDB__Q9CIK9 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)
MAEEKVLEVKNLHVNFHTYAGDVKAIRDVSFDLEKGQTLAIVGESGSGKSVTTKTLMGLNAKNAVIPQGELLFKGRNLLDLKEEEWQKIRGNEISMIFQDPMTSLDPTMRIGKQIAEPLLKHNKGMSKADAMKRALELMQQVGIPDAEVHINDYPHQWSGGMRQRAVIAIALAADPEILIADEPTTALDVTIQAQIMHMMAELQERINSSIVFITHDLGVVAGFAHKVAVMYAGEIVEYGTVEEIFYNPQHPYTWGLLDSMPTVDSSVDRLVSIPGTPPDLLNPPKGDAFAARNKFALAIDFEEEPPYFEVSPTHFAKTWLLDPRAPKVTPSDNILARWKRWEELKGDK
>SwissProt__A2RI77 Dipeptide transport ATP-binding protein DppD; EC 7.4.2.9 (Lactococcus lactis subsp. cremoris (strain MG1363))
MAEEKVLEVKNLHVNFHTYAGDVKAIRNVSFDLEKGQTLAIVGESGSGKSVTTKTLMGLNAKNAEIPEGELLFKGRNLLDLKEEEWQKIRGNEISMIFQDPMTSLDPTMRIGKQIAEPLLKHNKGMSKADAMKRALELMQQVGIPDAEVHINDYPHQWSGGMRQRAVIAIALAADPEILIADEPTTALDVTIQAQIMHMMAELQERINSSIVFITHDLGVVAGFAHKVAVMYAGEIVEYGTVEEIFYNPQHPYTWGLLDSMPTVDSSVDRLVSIPGTPPDLLNPPKGDAFAARNKFALAIDFEEEPPYFEVSPTHFAKTWLLDPRAPKVTPSDNILARWKRWEELKGDK
>TCDB__O30541 AccB, component of Agrocinopine (an opine)/Agrocin 84 (an antibiotic) porter (Agrobacterium radiobacter)
MRVALEEPKLSNLLTVRDLIVQVPARDITIINGVSFSLDAGQTLGLVGESGCGKSMTCYAIAKALPRGISQTGGTIELDSGPKADGKPAIAMIYQDPTSSLNPVHSIGYYLESSLYRHQGLEGNDARLEAMRLLERVGIDRAKSRLRSYPHEYSGGMNQRVMIAHALAAKPKLMIADEPTTALDVTTQAQILHLLEELRSETGMALLIVSHDLGVIARLADRAAVMYCGKIVETAPVAELLERAAHPYARALIGCMPTIDADDLEPPVPIPGSVPLLDNLPAGCYYHPRCPRASEQCSVSFPGPVNVGAFHDAACYHPVSP
>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__Q07733 OppD, 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))
MESENILEAKQVSVAFRIAGKFQKAIYDIDLSLRRGEVLAIVGESGSGKSTFATAVMGLHNPNQTQITGSILLDEEEVIGKTGDSMASIRGSKVGMIFQNPLTALNPLMKIGQQIKEMLAVHDVYPENQYESRIFQLLEQVGIPNPKRVVNQFPHQLSGGMRQRVMIAIAIANDPDLIIADEPTTALDVTIQAQILDLILEIQKKKNAGVILITHDLGVVAEVADTVAVMYAGQLVEKASVEELFQNPKHPYTRSLLRSNPSAETVSDDLYVIPGSVPSLSEIEYDKDLFLARVPWMKEEAQKVISEKMTEISSNHFVRGQAWKKFEFPDQKLKGGKK
>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__F0TFT0 Oligopeptide ABC transporter, component of ABC α-galactoside uptake porter (Lactobacillus acidophilus (strain 30SC))
MEKQSDLLLDIQHLHTAYRLQGKFYDAADDINLTLKRDEILAIVGESGCGKSTIAASIIGLYDHKNTKVTGDILYNELNLVGLNESLFNKIRGDKIGMIFQDPLASLNPLMRVGDQVAETLYYHTDMDEKARHARVIELFNQVGMPKPEEMYAMYPHELSGGLRQRVVIAMAIACKPEIIIADEPTTALDVTIQAQILDLLEDIQKQSHSGIILITHDLGVVAETADEVAVMYAGQIVEKSDVKTIFENPLHPYTRSLLNSMPQTDDSDEDLHVIHGTVPSLKNMPRTGDRFAARIPWIPASAHEENPQVHEVVPGHWVRCTCWKTFHFEGEDETQKAASGE
>TCDB__O31309 OppD, 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))
MEKENILEIKNLTIEFRLKHTTIHPVSNVNLSVKRGEIRAIVGESGSGKSVTSMAILKLLPELTTVYKSGEILFENQDLLKLSEKELLKIRGNKISMIFQDPMTSLNPFLRISTQLEETIILHQGLGKKEAKEKAIEMLKTVGVVNAEERIKHFPHQFSGGMRQRVMIAMALSCHPSLLIADEPTTALDVTIQEQILLLIKNLSKKFNTSTIFITHDLAVVAEICDTVSVMYQGKIVEEGTVEEIFNNPKHPYTIGLLKSILTLEHDPNKKLYSTKENPMKITKTSTEEF
>reanno__Smeli_SM_b21644 ABC transporter for D-Raffinose, ATPase component (Sinorhizobium meliloti 1021)
MVTIESIVPAPEERRDRDMKDERPVIDARKVAVSFKVENGTVQAVKDVSFQLYRGETVAIVGESGSGKSVTARTVMGLLSKRATIAPQARIEYDGRDVLKFSKRERRALRGDRISMIFQEPMSSLNPVYTIGSQIIEAIRAHRRVSRRAAAERALELLRHVQIPDPEARLNQYPHQLSGGQRQRVMIAMALANDPDVLIADEPTTALDVTVQAQILNLIRKLQQELGMAVILITHDLTVVRQFSDYVYVMQLGEVKEHNTTEALFADPQHAYTRRLLSSEPSGSANPLPDDAPILLDGRNVRVSFTLKKGGFFRPEFKELVAVDGLSLNLRRHETLGLVGESGSGKTTFGQALIRLLNTDGGEIYFEGEPIHDKDRKGMRPLRSKIQIVFQDPFSSLNPRMSVGQIIEEGLIVNGMGENRKDRLKRVEDALVSAGMPSNILSRFPHEFSGGQRQRIAIARAVALEPEFILLDEPTSALDLSVQAQIIELLRRLQDERGLSYLVISHDLKVVRALCHRVVVMQDGKIVEEGPVSEVLNNPKTAYTERLVKAAFEVAA
>TCDB__Q9F9T4 EppD, component of The Ethylene diamine tetraacetate (EDTA) uptake porter, EppABCD
MRPHMSESVHIAGGTGAPLVSVSGLTVSFDRHREEPIEAVRDVSWSIGSGEVLALVGESGSGKSVSALAVMGLLPRNARVAGSIRWRGEELLGASEKRRRALRGSRIGLVPQDPMTSLNPVYTIGAQIREGIRAHQKLSEREMAERTLELLETMGIPHARERMNSYPHELSGGMRQRVVIAMAMANNPDLIIADEATTALDVTVQAQVLDALKKAQALTGAALLLITHDLGVVAGRADRVAVMQRGEVVEQGTVDEIFYQPASSYTRKLLHSIPRLNHTPDLSAPSDVAPDAEVIHSAFERKVGAEGAPILSMRNVGKHFPVYSRGVIRGRVGVIKAVAGVDLDVEAGTTLGIVGESGSGKTTLIRSLFNLEPITHGTILFDGQDVHRMPPRDRRRMRKCVQMVFQDPYASLDPMMTVRDILMEPAVINRMDRKLAERRVMELLERVHLKPEHAARYPNEFSGGQRQRIAIARALMLYPRLLVLDEPVSSLDVSIQAEVLTLLKELQKDLNLSYLFVSHDLSVVAEIAHSVIVMYRGRIVERGRVDELFRNPKHPYTRALLSAVPIPDPRTERRRERIVFNSDTLASPITPVERTGMWRRLFGGRTQEAS
>TCDB__Q9WXS9 TM0074, component of Probable xylan oligosaccharide porter (Conners et al., 2005). Induced by xylan and xylose. Regulated by xylose-responsive regulator XylR
MEVLRTENLKSYYILDIFGKKRVVKAVDDVNISIMENEIYGIAGESGCGKSTLLRALFAAIEPPQRIVGGKVLYRENGKEVDVYSLSDEERRRLRWSFISYVPQGSMSVLNPVVKIKETFKDFIESHTTGKTKEEAYEMAKEHIKELGLPIEILNAYPHQLSGGMRQRVTIALATVLSPKVIIADEPTTALDVVTQRGVVQLLKEIQSSRQNTIILVTHDMGVHANVTDRIAIMYAGKIIEEGKTEEIFENPMHPYTKYLIYSLPKFGDKGRRESAPGSPPSLADLPPGCSFHPRCPHAFDRCKKEVPPLKEYLPGHRVACWLVEEGKNAAS
>BRENDA__Q73NS7 ABC-type dipeptide transporter (EC 7.4.2.9) (Treponema denticola)
MENKEVVLDVKNLRLYYHTSAGIVKALDDVSFTLHAGETLGLVGESGCGKTTTGMALLKMPSPPGRVEENSQIIINGRDIVPLSDSEIRKNVRWQEISMVFQGAMNSLTPVYTIGKQMLETLREHKEMSDKEAQDLMEEYLGYVGLPPEVLNRYPHELSGGMKQRVVIASGLFLKPKLVILDEPTTALDVIVQAQIINLLKELKKKFKLSFIFITHDLSLEAEISDRICVMYAGKIAELGTNEQIYGKEPLHPYTQKLLQATPLLRKRVSELSYIPGTPPDLISPPKGCRFNPRCHCTMDKCFEVEPPLIEVEPGHQVACWRCVK
>TCDB__Q8ZNJ8 YejF, component of The antimicrobial peptide (protamine, melittin, polymyxin B, human defensin (HBD)-1 and HBD-2 exporter, YejABEF (Eswarappa et al., 2008). Prefers N-formyl methionine peptides, such as Microcin C (of prokaryotic origin) to non formylated peptides (of eukaryotic origin) (Salmonella typhimurium)
MTSPLLAIENLSVGFRQQQHVRPVVNAISLQVNAGETLALVGESGSGKSVTALSILRLLPTPPAVYLSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMSREAARAEMIGCLDRVGIRQASQRLRDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILSLLRELQRELNMGLLFITHNLSIVKKLADSVAVMQHGKCVENQRADTLLSAPTHPYTQKLLNSEPTGDPVPLPAGQAPLLEVDKLRVAFPIRKGILKRVVDHNVVVNNISFTLHPGETLGLVGESGSGKSTTGLALLRLIRSEGRIVFDGQSLDTLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSGAQREQQVKAVMMEVGLDPETRHRYPAEFSGGQRQRIAVARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHRLAYIFISHDLHVVRALCHQVIVLRQGEVVEQGQCERVFTAPQQAYTRQLLALS
>ecocyc__YEJF-MONOMER putative oligopeptide ABC transporter ATP binding subunit YejF (EC 7.4.2.6) (Escherichia coli K-12 substr. MG1655)
MTQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESLLHASDQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLLNSEPSGDPVPLPEPASTLLDVEQLQVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLALS
>ecocyc__SAPD-MONOMER putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) (Escherichia coli K-12 substr. MG1655)
MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYACHFPLNMEKE
>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
>biolip__4fwiB Crystal structure of the nucleotide-binding domain of a dipeptide abc transporter
SIIIRVEDLRAVYLVREGTIKAADGISLDILENSVTAIVGESASGKSTIIEAMTKTLPPNGRILSGRVLYKGKDLLTMREEELRKIRWKEIALVPQAAQQSLNPTMKVIEHFKDTVEAHGVRWSHSELIEKASEKLRMVRLNPEAVLNSYPLQLSGGMKQRVLIALALLLDPVVLILDEPTSALDVLTQAHIIQLLKELKKMLKITLIFVTHDIAVAAELADKVAVIYGGNLVEYNSTFQIFKNPLHPYTRGLINSIMPIPGDPPSLLNPPSGCRFHPRCEYAMEICKKEKPKWIRLDGEAHVACHLYEE
>biolip__7z15I E. Coli c-p lyase bound to a phnk/phnl dual abc dimer and adp + pi
QPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSISARLTPQQGEIHYENRSLYAMSEADRRRLLRTEWGVVHQHPLDGLRRQVSAGGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQRLQIARNLVTHPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIVTHDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYTQLLVSSVLQNENL
>PDB_7z18_I E. Coli c-p lyase bound to a phnk abc dimer and atp
QPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSISARLTPQQGEIHYENRSLYAMSEADRRRLLR
TEWGVVHQHPLDGLRRQVSAGGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQRLQIARNLVT
HPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIVTHDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYT
QLLVSSVLQN
>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__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_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
>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
>biolip__4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps
MIFVNDVYKNFGSLEVLKGVTLKVNKGEVVVIIGPSGSGKSTLLRCINLLEEPTKGEVFIDGVKINNGKVNINKVRQKVGMVFQHFNLFPHLTAIENITLAPVKVKKMNKKEAEELAVDLLAKVGLLDKKDQYPIKLSGGQKQRLAIARALAMQPEVMLFDEPTSALDPEMVKEVLNVMKQLANEGMTMVVVTHEMGFAREVGDRVIFMDDGVIVEEGTPEEIFYRAKNERTREFLSKIL
>SwissProt_P0AAH0 Phosphate import ATP-binding protein PstB; ABC phosphate transporter; Phosphate-transporting ATPase; EC 7.3.2.1 from Escherichia coli (strain K12)
MSMVETAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNIL
TNSQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQ
RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF
TKPAKKQTEDYITGRYG
>biolip__1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp
VIKMVEVKLENLTKRFGNFTAVNKLNLTIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTEGRIYFGDRDVTYLPPKDRNISMVFQHMTVYENIAFPLKKFPKDEIDKRVRWAAELLQIEELLNRYPAQLSGGQRQRVAVARAIVVEPDVLLMDEPLSNLDAKLRVAMRAEIKKLQQKLKVTTIYVTHDQVEAMTMGDRIAVMNRGQLLQIGSPTEVYLRPNSVFVATFIGAPEMNILEVSVGDGYLEGRGFRIELPQMDLLKDYVGKTVLFGIRPEHMTVEGVHMKRTARLIGKVDFVEALGTDTILHVKFGDELVKVKLPGHIPIEPGREVKVIMDLDMIHVFDKDTEKAIV
>biolip__2d62A Crystal structure of multiple sugar binding transport atp- binding protein
MIGMAEVKLINIWKRFGDVTAVKDLSLEIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTRGQIYIEDNLVADPEKGVFVPPKERDVAMVFQSYALYPHMTVYDNIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIIRRPKVFLMDEPLSNLDAKLRVKMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNKGELQQVGTPDEVYYKPVNTFVAGFIGSPPMNFLDATITDDGFLDFGEFKLKLLQDQFEVLEEENMVGKEVIFGIRPEDVHDASFTHIDVPEENTVKATVDIIENLGGEKIVHLRRGNISFTAKFPKESKVREGDEVSVVFDMKKIHIFRKDTEKAIF
>biolip__1f3oA Crystal structure of mj0796 atp-binding cassette
MIKLKNVTKTYKMGEEIIYALKNVNLNIKEGEFVSIMGPSGSGKSTMLNIIGCLDKPTEGEVYIDNIKTNDLDDDELTKIRRDKIGFVFQQFNLIPLLTALENVELPLIFKYRGAMSGEERRKRALECLKMAELEERFANHKPNQLSGGQQQRVAIARALANNPPIILADEPTGALDSKTGEKIMQLLKKLNEEDGKTVVVVTHDINVARFGERIIYLKDGEVEREEKLRGF
>PDB_1l2t_A Dimeric structure of mj0796, a bacterial abc transporter cassette
MIKLKNVTKTYKMGEEIIYALKNVNLNIKEGEFVSIMGPSGSGKSTMLNIIGCLDKPTEGEVYIDNIKTNDLDDDELTKI
RRDKIGFVFQQFNLIPLLTALENVELPLIFKYRGAMSGEERRKRALECLKMAELEERFANHKPNQLSGGQQQRVAIARAL
ANNPPIILADQPTGALDSKTGEKIMQLLKKLNEEDGKTVVVVTHDINVARFGERIIYLKDGEVEREEKLR
>biolip__8hplC Lpqy-sugabc in state 1
AEIVLDRVTKSYPRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQPLSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMNFFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVHFTTEGAGAESAQLAELAADSGAGTNQFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>biolip__1g291 Malk
MAGVRLVDVWKVFGEVTAVREMSLEVKDGEFMILLGPSGCGKTTTLRMIAGLEEPSRGQIYIGDKLVADPEKGIFVPPKDRDIAMVFQSYALYPHMTVYDNIAFPLKLRKVPRQEIDQRVREVAELLGLTELLNRKPRELSGGQRQRVALGRAIVRKPQVFLMDEPLSNLDAKLRVRMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNRGVLQQVGSPDEVYDKPANTFVAGFIGSPPMNFLDAIVTEDGFVDFGEFRLKLLPDQFEVLGELGYVGREVIFGIRPEDLYDAMFAQVRVPGENLVRAVVEIVENLGSERIVRLRVGGVTFVGSFRSESRVREGVEVDVVFDMKKIHIFDKTTGKAIF
>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
>BRENDA__Q8TTZ3 ABC-type molybdate transporter (EC 7.3.2.5) (Methanosarcina acetivorans)
MIEIESLSRKWKNFSLDNLSLKVESGEYFVILGPTGAGKTLFLELIAGFHVPDSGRILLDGKDVTDLSPEKHDIAFVYQNYSLFPHMNVKKNLEFGMRMKKIKDPKRVLDTARDLKIEHLLDRNPLTLSGGEQQRVALARALVTNPKILLLDEPLSALDPRTQENAREMLSVLHKKNKLTVLHITHDQTEARIMADRIAVVMDGKLIQVGKPEEIFEKPVEGRVASFVGFENVLKGRVISAEQGLLRIRVGEVVIDAAGDMEVGDQVYAFLRPENIALSKSSTQSSIRNSLQGRVTEAWVLGALVRVKVDCGVPLNVLITRRSAEEMELSPGVQIYARFKASSVHVLR
>metacyc__G185E-5409-MONOMER ABC-type trehalose transporter ATP-binding protein (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MAEIVLDHVNKSYPDGHTAVRDLNLTIADGEFLILVGPSGCGKTTTLNMIAGLEDISSGELRIAGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKMRKADIAQKVSETAKILDLTNLLDRKPSQLSGGQRQRVAMGRAIVRHPKAFLMDEPLSNLDAKLRVQMRGEIAQLQRRLGTTTVYVTHDQTEAMTLGDRVVVMYGGIAQQIGTPEELYERPANLFVAGFIGSPAMNFFPARLTAIGLTLPFGEVTLAPEVQGVIAAHPKPENVIVGVRPEHIQDAALIDAYQRIRALTFQVKVNLVESLGADKYLYFTTESPAVHSVQLDELAEVEGESALHENQFVARVPAESKVAIGQSVELAFDTARLAVFDADSGANLTIPHRA
>biolip__5x40A Structure of a cbio dimer bound with amppcp
MTPILAAEALTYAFPGGVKALDDLSLAVPKGESLAILGPNGAGKSTLLLHLNGTLRPQSGRVLLGGTATGHSRKDLTGWRRRVGLVLQDADDQLFATTVFEDVSFGPLNLGLSEAEARARVEEALAALSISDLRDRPTHMLSGGQKRRVAIAGAVAMRPEVLLLDQPTAGLDLAGTEQLLTLLRGLRAAGMTLVFSTHDVELAAALADRVALFRTGRVLAEGAAEAVLSDRATLAKVALRPPLVIDLALLARDHGLLAPEAPLPKTRDALAAQMAGWTRR
>ecocyc__MACB ABC-type tripartite efflux pump ATP binding/membrane subunit (Escherichia coli K-12 substr. MG1655)
MTPLLELKDIRRSYPAGDEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKATSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAEQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRTEYYPAQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAIEKVNVTGGTEPVVNTVSGWRQFVSGFNEALTMAWRALAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRSIGTNTIDVYPGKDFGDDDPQYQQALKYDDLIAIQKQPWVASATPAVSQNLRLRYNNVDVAASANGVSGDYFNVYGMTFSEGNTFNQEQLNGRAQVVVLDSNTRRQLFPHKADVVGEVILVGNMPARVIGVAEEKQSMFGSSKVLRVWLPYSTMSGRVMGQSWLNSITVRVKEGFDSAEAEQQLTRLLSLRHGKKDFFTWNMDGVLKTVEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVLQQFLIEAVLVCLVGGALGITLSLLIAFTLQLFLPGWEIGFSPLALLLAFLCSTVTGILFGWLPARNAARLDPVDALARE
>ecocyc__YCFV-MONOMER lipoprotein release complex - ATP binding subunit (Escherichia coli K-12 substr. MG1655)
MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLKAVGLDHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE
>biolip__7w78A Heme exporter hrtba in complex with mg-amppnp
AAPVLSITNASVVYPDGISTVTALDSANVEIFPGELVAIVGESGSGKSTLLSIAGFLQEPTSGTVTLHGAEGLDATSTRREHIGFVFQQPNLLGSLTAREQLLITDHLRGIKPRKDRADELLARVGLKGLGGRRVAQLSGGQRQRVNIARALMGNPQLLLADEPTSALDARLSKEIVELLRDVTKEFALATLMVTHDRSQLAYADRFVEMADGKALQT
>PDB_7w79_A Heme exporter hrtba in complex with mn-amppnp
AAPVLSITNASVVYPDGISTVTALDSANVEIFPGELVAIVGESGSGKSTLLSIAGFLQEPTSGTVTLHGAEGLDATSTRR
EHIGFVFQQPNLLGSLTAREQLLITDHLRGIKPRKDRADELLARVGLKGLGGRRVAQLSGGQRQRVNIARALMGNPQLLL
ADEPTSALDARLSKEIVELLRDVTKEFALATLMVTHDRSQLAYADRFVEMADGKAL
>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
>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