>PfGW456L13_5057 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_5057
MSLLEIKNLNVRFGDKNATPVVDGLDLQVDKGEVLAIVGESGSGKSVTMMALMGLIEHPGIVTADALNFDGKNMLKLNNRQRRQIVGKDLSMVFQDPMTALNPSYTVGFQIEEVLRLHLKMSGKAARKRAIELLEKVEIPGAASRMDAYPHQLSGGMSQRVAIAMAIAGEPKLLIADEPTTALDVTIQAQIMDLLLALQKEQNMGLVLITHDLAVVAETAQRVCVMYAGQAVEVGQVPQLFDIPAHPYSEALLKAIPEHSLGASRLSTLPGIVPGRYDRPQGCLLSPRCPYVKDNCRQQRPALDQKSNSLARCFYPLNQEVA
>SwissProt__A0A0H2ZGN6 Di/tripeptide transport ATP-binding protein DppD; EC 7.4.2.9 (Pseudomonas aeruginosa (strain UCBPP-PA14))
MSLLDIKNLSVRFGDTTAVPVVDGLDLSVDKGEVLAIVGESGSGKSVTMMALMGLIDAPGWVSADHLRFDGHDMLTLKGRQRRRIVGKDMAMVFQDPMTALNPSYTVGYQIEEVLRLHLGLRGKALRQRALELLERVEIPAAASRLDAYPHQLSGGMSQRVAIAMAIAAEPKLLIADEPTTALDVTIQAQIMELLLNLQRDQDMALILITHDLAVVAETAQRVCVMYAGEAVEIGGVPALFDRPTHPYTEALIKAIPEHCAGEARLATLPGIVPGRYDRPRGCLLSPRCPYAQEHCRQERPALEAHERGAVRCFYPLNLLNEVA
>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
>ecocyc__DPPD-MONOMER dipeptide ABC transporter ATP binding subunit DppD (EC 7.4.2.9) (Escherichia coli K-12 substr. MG1655)
MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLADGRQSKCHYPLDDAGRPTL
>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__P42064 AppD, component of 5-6 amino acyl oligopeptide transporter AppA-F (Bacillus subtilis)
MSTLLEVNNLKTYFFRKKEPIPAVDGVDFHISKGETVALVGESGSGKSITSLSIMGLVQSSGGKIMDGSIKLEDKDLTSFTENDYCKIRGNEVSMIFQEPMTSLNPVLTIGEQITEVLIYHKNMKKKEARQRAVELLQMVGFSRAEQIMKEYPHRLSGGMRQRVMIAIALSCNPKLLIADEPTTALDVTIQAQVLELMKDLCQKFNTSILLITHDLGVVSEAADRVIVMYCGQVVENATVDDLFLEPLHPYTEGLLTSIPVIDGEIDKLNAIKGSVPTPDNLPPGCRFAPRCPKAMDKCWTNQPSLLTHKSGRTVRCFLYEEEGAEQS
>SwissProt__P24136 Oligopeptide transport ATP-binding protein OppD; Stage 0 sporulation protein KD (Bacillus subtilis (strain 168))
MIRVTRLLEVKDLAISFKTYGGEVQAIRGVNFHLDKGETLAIVGESGSGKSVTSQAIMKLIPMPPGYFKRGEILFEGKDLVPLSEKEMQNVRGKEIGMIFQDPMTSLNPTMKVGKQITEVLFKHEKISKEAAKKRAVELLELVGIPMPEKRVNQFPHEFSGGMRQRVVIAMALAANPKLLIADEPTTALDVTIQAQILELMKDLQKKIDTSIIFITHDLGVVANVADRVAVMYAGQIVETGTVDEIFYDPRHPYTWGLLASMPTLESSGEEELTAIPGTPPDLTNPPKGDAFALRSSYAMKIDFEQEPPMFKVSDTHYVKSWLLHPDAPKVEPPEAVKAKMRKLANTFEKPVLVREVE
>TCDB__Q9X271 TM1749, component of Probable mannose/mannoside porter. Induced by beta-mannan (Conners et al., 2005). Regulated by mannose-responsive regulator manR
MMELLNVNNLKVEFHRVEGIVKAVDGISYKLNKGESLGIVGESGSGKSVSVLSLLRLINRNGRIVDGEAIFLGKDLLKLNKEELRNIRGKDISIIFQNPMTSLNPIIRVGIQVMEPIIWHRLMKNEEARERAIELLERVGIPESPKRFLNYPFQFSGGMRQRVMIAMALACHPKLLIADEPTTALDVTIQAQIMELLQELKEEYGMSVIFITHDLSVATNFCDRIITMYAGKIVEEAPVEEILKTPLHPYTKGLLNSTLEIGSRGKKLVPIPGNPPNPTKHPSGCKFHPRCSFAMEICQREEPPLVNISENHRVACHLIKGESK
>BRENDA__Q5V9R9 ABC-type oligopeptide transporter (EC 7.4.2.6) (Vibrio fluvialis)
MSLLDVKDLRVEFTTQDGIVTAVNDLNFSLKQGETLGIVGESGSGKSQTVFAIMGLLAKNGKISGSAKFEGKEILNLPEKELNKVRSEQIAMIFQDPMTSLNPYMKVSDQLMEVLMPHKGMGKAEAFEESVRMLEAVKIPEARKRITMYPHEFSGGMRQRVMIAMALLCRPKRLIADEPTTALDVTVQAQIMDLLNELKREFNTAIIMITHDLGVVAGSCDKVLVMYAGRTMEYGSVNEIFYNPSHPYAEGLLKAIPRLDTEGEILPTIPGNPPNLLRLPVGCPYQERCHRVMDRCKREAPILTPFGDGRQRACFSDWETWTK
>TCDB__P26905 DppD aka DCIAD, component of Dipeptide porter. Also transports δ-aminolevulinic acid (ALA) and heme (Bacillus subtilis)
MEKVLSVQNLHVSFTTYGGTVQAVRGVSFDLYKGETFAIVGESGCGKSVTSQSIMGLLPPYSAKVTDGRILFKNKDLCRLSDKEMRGIRGADISMIFQDPMTALNPTLTVGDQLGEALLRHKKMSKKAARKEVLSMLSLVGIPDPGERLKQYPHQFSGGMRQRIVIAMALICEPDILIADEPTTALDVTIQAQILELFKEIQRKTDVSVILITHDLGVVAQVADRVAVMYAGKMAEIGTRKDIFYQPQHPYTKGLLGSVPRLDLNGAELTPIDGTPPDLFSPPPGCPFAARCPNRMVVCDRVYPGQTIRSDSHTVNCWLQDQRAEHAVLSGDAKD
>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__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__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
>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
>ecocyc__YLIA-MONOMER glutathione ABC transporter ATP binding subunit GsiA (EC 7.4.2.10) (Escherichia coli K-12 substr. MG1655)
MPHSDELDAGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLQRRSREVIELSEQNAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQAPPIEQKTVVDGEPVLRVRNLVTRFPLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTIGDSIIEPLRVHGLLPGKDAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLLAAVPVAEPSRQRPQRVLLSDDLPSNIHLRGEEVAAVSLQCVGPGHYVAQPQSEYAFMRR
>BRENDA__Q8ZQM4 ABC-type glutathione transporter (EC 7.4.2.10) (Salmonella enterica subsp. enterica serovar Typhimurium)
MPHSDELDSRDVLSVSGLNIAFHHEGQQVDAVRNVSLRLKRGETLAIVGESGSGKSVTALALMRLIEQSGANVRCGEMLLRRRNRQVIELSEQSDAQMRRVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEALAEAKRMLDQVRIPESQAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQEMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPTHPYTQTLLAAVPQLGAMRGHSLPRRFPLISADEPALYESQIEQDTVVEGEPILQVRGLVTRFPLRSGLFNRVTREVHAVENISFDLWPGETLSLVGESGSGKSTTGRALLRLVESRQGEIIFNGQRIDTLSAGKLQPLRRDIQCIFQDPYASLDPRQTVGYSIMEPLRIHGLGQGDAAAKRVAWLLERVGLRPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSVRGQIINLLLDLQREMGIAYLFISHDMAVVERISHRVAVMYLGQIVEMGPRRAVFENPQHPYTRKLMAAVPVADPSRHRPRRVLLSDDIPSNIHKRGEETPAVSLQLVGPGHYVARPLQDNALSRL
>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
>SwissProt__P36636 Peptide transport system ATP-binding protein SapD (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MPLLDIRNLTIEFKTSEGWVKAVDRVSMTLSEGEIRGLVGESGSGKSLIAKAICGVAKDNWRVTADRMRFDDIDLLRLSSRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRLGWRKRRAIELLHRVGIKDHKDAMRSFPYELTDGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKDLVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIITPRLTGAKNHLYACHFPLNMERE
>ecocyc__SAPD-MONOMER putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) (Escherichia coli K-12 substr. MG1655)
MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYACHFPLNMEKE
>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__O86190 SapD protein, component of Peptide transporter, SapABCDF. Mutants are more sensitive than the wild type to wheat alpha-thionin and to snakin-1, which is the most abundant antimicrobial peptide from potato tubers. They were also less virulent than was the wild-type strain in potato tubers: lesion areas were 37% that of the control, and the growth rate was two orders of magnitude lower. Thus, the interaction of antimicrobial peptides from the host with the sapA-F operon from the pathogen plays a similar role in animal and in plant bacterial pathogenesis (Dickeya chrysanthemi)
MALLEIRNVTIEFLTPDGPVKAVDRVSINLNEGEIRGLVGESGSGKSLIAKAICGINKENWRITADRFRFDDVDMLQLTPPQRRKLVRHNMSMIFQEPQSCLDPSARVGRQLIQSIPGWTYKGRWWQRFNWRKRRAIELLHRVGIKDHKDVMRSFPYELTEGECQKVMIAIALANQPRLLIADEPNNAMEATTQAQIFRLLSRLNQNNNTTILLISHDLQTMSKWADRINVLYCGQTVESAVSDELISAPHHPYTQALIRAMPDFGCSLPHKSRLNTLPGAIPSLAHLPVGCRLGPRCPYSQKQCMTAPPLIPVRNHWYACHFPLNMEES
>TCDB__F0TFT0 Oligopeptide ABC transporter, component of ABC α-galactoside uptake porter (Lactobacillus acidophilus (strain 30SC))
MEKQSDLLLDIQHLHTAYRLQGKFYDAADDINLTLKRDEILAIVGESGCGKSTIAASIIGLYDHKNTKVTGDILYNELNLVGLNESLFNKIRGDKIGMIFQDPLASLNPLMRVGDQVAETLYYHTDMDEKARHARVIELFNQVGMPKPEEMYAMYPHELSGGLRQRVVIAMAIACKPEIIIADEPTTALDVTIQAQILDLLEDIQKQSHSGIILITHDLGVVAETADEVAVMYAGQIVEKSDVKTIFENPLHPYTRSLLNSMPQTDDSDEDLHVIHGTVPSLKNMPRTGDRFAARIPWIPASAHEENPQVHEVVPGHWVRCTCWKTFHFEGEDETQKAASGE
>ecocyc__YDDP-MONOMER putative D,D-dipeptide ABC transporter ATP-binding subunit DdpD (Escherichia coli K-12 substr. MG1655)
MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIDLLEEMQIPDAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQCENVPALTACGDNNQRCACWYPQQEVISV
>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
>reanno__Smeli_SM_b21644 ABC transporter for D-Raffinose, ATPase component (Sinorhizobium meliloti 1021)
MVTIESIVPAPEERRDRDMKDERPVIDARKVAVSFKVENGTVQAVKDVSFQLYRGETVAIVGESGSGKSVTARTVMGLLSKRATIAPQARIEYDGRDVLKFSKRERRALRGDRISMIFQEPMSSLNPVYTIGSQIIEAIRAHRRVSRRAAAERALELLRHVQIPDPEARLNQYPHQLSGGQRQRVMIAMALANDPDVLIADEPTTALDVTVQAQILNLIRKLQQELGMAVILITHDLTVVRQFSDYVYVMQLGEVKEHNTTEALFADPQHAYTRRLLSSEPSGSANPLPDDAPILLDGRNVRVSFTLKKGGFFRPEFKELVAVDGLSLNLRRHETLGLVGESGSGKTTFGQALIRLLNTDGGEIYFEGEPIHDKDRKGMRPLRSKIQIVFQDPFSSLNPRMSVGQIIEEGLIVNGMGENRKDRLKRVEDALVSAGMPSNILSRFPHEFSGGQRQRIAIARAVALEPEFILLDEPTSALDLSVQAQIIELLRRLQDERGLSYLVISHDLKVVRALCHRVVVMQDGKIVEEGPVSEVLNNPKTAYTERLVKAAFEVAA
>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
>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
>TCDB__Q9F9T4 EppD, component of The Ethylene diamine tetraacetate (EDTA) uptake porter, EppABCD
MRPHMSESVHIAGGTGAPLVSVSGLTVSFDRHREEPIEAVRDVSWSIGSGEVLALVGESGSGKSVSALAVMGLLPRNARVAGSIRWRGEELLGASEKRRRALRGSRIGLVPQDPMTSLNPVYTIGAQIREGIRAHQKLSEREMAERTLELLETMGIPHARERMNSYPHELSGGMRQRVVIAMAMANNPDLIIADEATTALDVTVQAQVLDALKKAQALTGAALLLITHDLGVVAGRADRVAVMQRGEVVEQGTVDEIFYQPASSYTRKLLHSIPRLNHTPDLSAPSDVAPDAEVIHSAFERKVGAEGAPILSMRNVGKHFPVYSRGVIRGRVGVIKAVAGVDLDVEAGTTLGIVGESGSGKTTLIRSLFNLEPITHGTILFDGQDVHRMPPRDRRRMRKCVQMVFQDPYASLDPMMTVRDILMEPAVINRMDRKLAERRVMELLERVHLKPEHAARYPNEFSGGQRQRIAIARALMLYPRLLVLDEPVSSLDVSIQAEVLTLLKELQKDLNLSYLFVSHDLSVVAEIAHSVIVMYRGRIVERGRVDELFRNPKHPYTRALLSAVPIPDPRTERRRERIVFNSDTLASPITPVERTGMWRRLFGGRTQEAS
>BRENDA__A0A150QXP6 5-(carboxyamino)imidazole ribonucleotide mutase (EC 5.4.99.18) (Bacillus anthracis)
MAPSPLLSVQDLRVEFITPTGPVCAVDNVSFDIAPGEVLGLAGESGSGKSTVAMAIMRLLRPPAIITGGRVLFAGQDVLSMTEEQLRAFRWRKMALVFQSAMTALNPVLTIGEQIADPIIAHDGVTQAQAMERAAALLKLVNIDPSRLTSYPHQLSGGMRQRVVIAIAMALKPPFLIMDEPTTALDVVVQREILQQIAELKERLGFSILFITHDLSLIAEFSTRIAILYAGKLAETARAKDLFSDPKHPYTQGLLGSFPSVRGPRRRLQGIPGSPPDMRNPPSGCRFHPRCPQAFATCQNELPVLREIAPEHRGACHLY
>ecocyc__YEJF-MONOMER putative oligopeptide ABC transporter ATP binding subunit YejF (EC 7.4.2.6) (Escherichia coli K-12 substr. MG1655)
MTQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESLLHASDQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLLNSEPSGDPVPLPEPASTLLDVEQLQVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLALS
>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__O30541 AccB, component of Agrocinopine (an opine)/Agrocin 84 (an antibiotic) porter (Agrobacterium radiobacter)
MRVALEEPKLSNLLTVRDLIVQVPARDITIINGVSFSLDAGQTLGLVGESGCGKSMTCYAIAKALPRGISQTGGTIELDSGPKADGKPAIAMIYQDPTSSLNPVHSIGYYLESSLYRHQGLEGNDARLEAMRLLERVGIDRAKSRLRSYPHEYSGGMNQRVMIAHALAAKPKLMIADEPTTALDVTTQAQILHLLEELRSETGMALLIVSHDLGVIARLADRAAVMYCGKIVETAPVAELLERAAHPYARALIGCMPTIDADDLEPPVPIPGSVPLLDNLPAGCYYHPRCPRASEQCSVSFPGPVNVGAFHDAACYHPVSP
>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
>BRENDA__Q5V9R8 ABC-type oligopeptide transporter (EC 7.4.2.6) (Vibrio fluvialis)
MSADKPLLLDVKNLKVHFSIAAKSGWPWTKPSTLKAVDGVNVRLYEGETLGVVGESGCGKSTFARAIIGLVQSTEGEVVWLGQDLTRMQEVKRRNTRKEIQMIFQDPLASLNPRMTVGDIIAEPLQTFYPELSKQEVKDRVKEMMAKVGLLPNVINRYPHEFSGGQCQRIGIARALILKPKMIICDEPVSALDVSIQAQVVNLLKELQKELGLSLVFIAHDLSVVKHISDRVLVMYLGNAVELGEADELFANPLHPYTKALMSAVPIPDPNLERAKVIQMLEGDLPSPINPPSGCVFRTRCPQATAECAKTKPQIEGTDTHSVSCLHVSA
>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
>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
>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
>biolip__4u00A Crystal structure of ttha1159 in complex with adp
PIIRIRNLHKWFGPLHVLKGIHLEVAPGEKLVIIGPSGSGKSTLIRTINRLEDFQEGEVVVDGLSVKDDRALREIRREVGMVFQQFNLFPHMTVLENVTLAPMRVRRWPREKAEKKALELLERVGILDQARKYPAQLSGGQQQRVAIARALAMEPKIMLFDEPTSALDPEMVGEVLDVMRDLAQGGMTMVVVTHEMGFAREVADRVVFMDGGQIVEEGRPEEIFTRPKEERTRSFLQRVLH
>PDB_7ahh_C Opua inhibited inward-facing, sbd docked
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTS
GKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYP
KQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGK
IMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAA
RKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>biolip__7aheC Opua inhibited inward facing
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTSGKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYPKQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGKIMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAARKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>biolip__4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps
MIFVNDVYKNFGSLEVLKGVTLKVNKGEVVVIIGPSGSGKSTLLRCINLLEEPTKGEVFIDGVKINNGKVNINKVRQKVGMVFQHFNLFPHLTAIENITLAPVKVKKMNKKEAEELAVDLLAKVGLLDKKDQYPIKLSGGQKQRLAIARALAMQPEVMLFDEPTSALDPEMVKEVLNVMKQLANEGMTMVVVTHEMGFAREVGDRVIFMDDGVIVEEGTPEEIFYRAKNERTREFLSKIL
>PDB_7ahd_C Opua (e190q) occluded
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTS
GKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYP
KQLSGGMQQRVGLARALANDPEILLMDQAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGK
IMQIGTGEEILTNPANDYVK
>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__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__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
>biolip__5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21)
MNIIEIKQLNRYFGEGENRVHVLKDISLSIERGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSSKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQSQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADQPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKRQVKSAVKNPSVFSKDQLMEAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFQNLKISDANTLSKQSYIQSVTPNTSSSGILVVGNKSFTSANLYGIGEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFANENPLGKTVIFNKRPFRVIGVVSDQSLNLYSPYSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKSLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALA
>biolip__5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21)
MNIIEIKQLNRYFGEGENRVHVLKDISLSIERGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSSKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQSQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADQPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKRQVKSAVKNPSVFSKDQLMEAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFQNLKISDANTLSKQSYIQSVTPNTANLYGIGEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFVIFNKRPFRVIGVVSDQSLNLYSPYSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKSLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALAQ
>biolip__2d62A Crystal structure of multiple sugar binding transport atp- binding protein
MIGMAEVKLINIWKRFGDVTAVKDLSLEIKDGEFLVLLGPSGCGKTTTLRMIAGLEEPTRGQIYIEDNLVADPEKGVFVPPKERDVAMVFQSYALYPHMTVYDNIAFPLKLRKVPKQEIDKRVREVAEMLGLTELLNRKPRELSGGQRQRVALGRAIIRRPKVFLMDEPLSNLDAKLRVKMRAELKKLQRQLGVTTIYVTHDQVEAMTMGDRIAVMNKGELQQVGTPDEVYYKPVNTFVAGFIGSPPMNFLDATITDDGFLDFGEFKLKLLQDQFEVLEEENMVGKEVIFGIRPEDVHDASFTHIDVPEENTVKATVDIIENLGGEKIVHLRRGNISFTAKFPKESKVREGDEVSVVFDMKKIHIFRKDTEKAIF
>biolip__8g4cB Bceabs atpgs high res tm
HVILEANKIRKSYGNKLNKQEVLKGIDIHIEKGEFVSIMGASGSGKTTLLNVLSSIDQVSHGTIHINGNDMTAMKEKQLAEFRKQHLGFIFQDYNLLDTLTVKENILLPLSITKLSKKEANRKFEEVAKELGIYELRDKYPNEISGGQKQRTSAGRAFIHDPSIIFADEPTGALDSKSASDLLNKLSQLNQKRNATIIMVTHDPVAASYCGRVIFIKDGQMYTQLNKGGQDRQTFFQDIMKTQGVLGG
>PDB_7tch_B Bceab e169q variant atp-bound conformation
VILEANKIRKSYGNKLNKQEVLKGIDIHIEKGEFVSIMGASGSGKTTLLNVLSSIDQVSHGTIHINGNDMTAMKEKQLAE
FRKQHLGFIFQDYNLLDTLTVKENILLPLSITKLSKKEANRKFEEVAKELGIYELRDKYPNEISGGQKQRTSAGRAFIHD
PSIIFADQPTGALDSKSASDLLNKLSQLNQKRNATIIMVTHDPVAASYCGRVIFIKDGQMYTQLNKGGQDRQTFFQDIMK
TQGVL
>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__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__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