>GFF3629 FitnessBrowser__Phaeo:GFF3629 MTMKETQPVLEVRNLCTTFKRGGVLLPAVRDVSFDVRQGEVLGLVGESGSGKSVTLRSILGLTRRHGEVTGEVRWQGRDISRLSDRQLRQVRGGEVAMIFQEPMTSLNPLLTVGLQLTETLKAHTDLSRAARRNRAIEMLDHVGIPAAASRLQDYPHQFSGGMRQRVMIAIALAAEPKLLLADEPTTALDVTIQAQILDLILRLSQEMNMGVILVTHDLGVVAQTCENVAVMYAGRIVEQGAVRQVLRAPRHPYTAGLMRSVPQDIAPRTPLYSVPGTPPSLEMLPRGCAYAPRCEVRTEACLSKRPALETISAGRRAACFNPVPSIQGEVA >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__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 >BRENDA__Q5V9R9 ABC-type oligopeptide transporter (EC 7.4.2.6) (Vibrio fluvialis) MSLLDVKDLRVEFTTQDGIVTAVNDLNFSLKQGETLGIVGESGSGKSQTVFAIMGLLAKNGKISGSAKFEGKEILNLPEKELNKVRSEQIAMIFQDPMTSLNPYMKVSDQLMEVLMPHKGMGKAEAFEESVRMLEAVKIPEARKRITMYPHEFSGGMRQRVMIAMALLCRPKRLIADEPTTALDVTVQAQIMDLLNELKREFNTAIIMITHDLGVVAGSCDKVLVMYAGRTMEYGSVNEIFYNPSHPYAEGLLKAIPRLDTEGEILPTIPGNPPNLLRLPVGCPYQERCHRVMDRCKREAPILTPFGDGRQRACFSDWETWTK >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__P42064 AppD, component of 5-6 amino acyl oligopeptide transporter AppA-F (Bacillus subtilis) MSTLLEVNNLKTYFFRKKEPIPAVDGVDFHISKGETVALVGESGSGKSITSLSIMGLVQSSGGKIMDGSIKLEDKDLTSFTENDYCKIRGNEVSMIFQEPMTSLNPVLTIGEQITEVLIYHKNMKKKEARQRAVELLQMVGFSRAEQIMKEYPHRLSGGMRQRVMIAIALSCNPKLLIADEPTTALDVTIQAQVLELMKDLCQKFNTSILLITHDLGVVSEAADRVIVMYCGQVVENATVDDLFLEPLHPYTEGLLTSIPVIDGEIDKLNAIKGSVPTPDNLPPGCRFAPRCPKAMDKCWTNQPSLLTHKSGRTVRCFLYEEEGAEQS >TCDB__Q9X271 TM1749, component of Probable mannose/mannoside porter. Induced by beta-mannan (Conners et al., 2005). Regulated by mannose-responsive regulator manR MMELLNVNNLKVEFHRVEGIVKAVDGISYKLNKGESLGIVGESGSGKSVSVLSLLRLINRNGRIVDGEAIFLGKDLLKLNKEELRNIRGKDISIIFQNPMTSLNPIIRVGIQVMEPIIWHRLMKNEEARERAIELLERVGIPESPKRFLNYPFQFSGGMRQRVMIAMALACHPKLLIADEPTTALDVTIQAQIMELLQELKEEYGMSVIFITHDLSVATNFCDRIITMYAGKIVEEAPVEEILKTPLHPYTKGLLNSTLEIGSRGKKLVPIPGNPPNPTKHPSGCKFHPRCSFAMEICQREEPPLVNISENHRVACHLIKGESK >SwissProt__P24136 Oligopeptide transport ATP-binding protein OppD; Stage 0 sporulation protein KD (Bacillus subtilis (strain 168)) MIRVTRLLEVKDLAISFKTYGGEVQAIRGVNFHLDKGETLAIVGESGSGKSVTSQAIMKLIPMPPGYFKRGEILFEGKDLVPLSEKEMQNVRGKEIGMIFQDPMTSLNPTMKVGKQITEVLFKHEKISKEAAKKRAVELLELVGIPMPEKRVNQFPHEFSGGMRQRVVIAMALAANPKLLIADEPTTALDVTIQAQILELMKDLQKKIDTSIIFITHDLGVVANVADRVAVMYAGQIVETGTVDEIFYDPRHPYTWGLLASMPTLESSGEEELTAIPGTPPDLTNPPKGDAFALRSSYAMKIDFEQEPPMFKVSDTHYVKSWLLHPDAPKVEPPEAVKAKMRKLANTFEKPVLVREVE >SwissProt__A2RI77 Dipeptide transport ATP-binding protein DppD; EC 7.4.2.9 (Lactococcus lactis subsp. cremoris (strain MG1363)) MAEEKVLEVKNLHVNFHTYAGDVKAIRNVSFDLEKGQTLAIVGESGSGKSVTTKTLMGLNAKNAEIPEGELLFKGRNLLDLKEEEWQKIRGNEISMIFQDPMTSLDPTMRIGKQIAEPLLKHNKGMSKADAMKRALELMQQVGIPDAEVHINDYPHQWSGGMRQRAVIAIALAADPEILIADEPTTALDVTIQAQIMHMMAELQERINSSIVFITHDLGVVAGFAHKVAVMYAGEIVEYGTVEEIFYNPQHPYTWGLLDSMPTVDSSVDRLVSIPGTPPDLLNPPKGDAFAARNKFALAIDFEEEPPYFEVSPTHFAKTWLLDPRAPKVTPSDNILARWKRWEELKGDK >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__P26905 DppD aka DCIAD, component of Dipeptide porter. Also transports δ-aminolevulinic acid (ALA) and heme (Bacillus subtilis) MEKVLSVQNLHVSFTTYGGTVQAVRGVSFDLYKGETFAIVGESGCGKSVTSQSIMGLLPPYSAKVTDGRILFKNKDLCRLSDKEMRGIRGADISMIFQDPMTALNPTLTVGDQLGEALLRHKKMSKKAARKEVLSMLSLVGIPDPGERLKQYPHQFSGGMRQRIVIAMALICEPDILIADEPTTALDVTIQAQILELFKEIQRKTDVSVILITHDLGVVAQVADRVAVMYAGKMAEIGTRKDIFYQPQHPYTKGLLGSVPRLDLNGAELTPIDGTPPDLFSPPPGCPFAARCPNRMVVCDRVYPGQTIRSDSHTVNCWLQDQRAEHAVLSGDAKD >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__A0A0H2ZGN6 Di/tripeptide transport ATP-binding protein DppD; EC 7.4.2.9 (Pseudomonas aeruginosa (strain UCBPP-PA14)) MSLLDIKNLSVRFGDTTAVPVVDGLDLSVDKGEVLAIVGESGSGKSVTMMALMGLIDAPGWVSADHLRFDGHDMLTLKGRQRRRIVGKDMAMVFQDPMTALNPSYTVGYQIEEVLRLHLGLRGKALRQRALELLERVEIPAAASRLDAYPHQLSGGMSQRVAIAMAIAAEPKLLIADEPTTALDVTIQAQIMELLLNLQRDQDMALILITHDLAVVAETAQRVCVMYAGEAVEIGGVPALFDRPTHPYTEALIKAIPEHCAGEARLATLPGIVPGRYDRPRGCLLSPRCPYAQEHCRQERPALEAHERGAVRCFYPLNLLNEVA >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__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 >biolip__8j5qD Cryo-em structure of mycobacterium tuberculosis oppabcd in the pre- translocation state SPLLEVTDLAVTFRTDGDPVTAVRGISYRVEPGEVVAMVGESGSGKSAAAMAVVGLLPEYAQVRGSVRLQGTELLGLADNAMSRFRGKAIGTVFQDPMSALTPVYTVGDQIAEAIEVHQPRVGKKAARRRAVELLDLVGISQPQRRSRAFPHELSGGERQRVVIAIAIANDPDLLICDEPTTALDVTVQAQILDVLKAARDVTGAGVLIITHDLGVVAEFADRALVMYAGRVVESAGVNDLYRDRRMPYTVGLLGSVPRLDAAQGTRLVPIPGAPPSLAGLAPGCPFAPRCPLVIDECLTAEPELLDVATDHRAACIRTELVTGRSAADIYRVKTEARPAALGDASVVVRVRHLVKTYRLAKGVVLRRAIGEVRAVDGISLELRQGRTLGIVGESGSGKSTTLHEILELAAPQSGSIEVLGTDVATLGTAERRSLRRDIQVVFQDPVASLDPRLPVFDLIAEPLQANGFGKNETHARVAELLDIVGLRHGDASRYPAEFSGGQKQRIGIARALALQPKILALDEPVSALDVSIQAGIINLLLDLQEQFGLSYLFVSHDLSVVKHLAHQVAVMLAGTVVEQGDSEEVFGNPKHEYTRRLLGAVPQPDPARRG >PDB_8j5t_D Cryo-em structure of mycobacterium tuberculosis oppabcd in the catalytic intermediate state SPLLEVTDLAVTFRTDGDPVTAVRGISYRVEPGEVVAMVGESGSGKSAAAMAVVGLLPEYAQVRGSVRLQGTELLGLADN AMSRFRGKAIGTVFQDPMSALTPVYTVGDQIAEAIEVHQPRVGKKAARRRAVELLDLVGISQPQRRSRAFPHELSGGERQ RVVIAIAIANDPDLLICDDPTTALDVTVQAQILDVLKAARDVTGAGVLIITHDLGVVAEFADRALVMYAGRVVESAGVND LYRDRRMPYTVGLLGSVPRLDAAQGTRLVPIPGAPPSLAGLAPGCPFAPRCPLVIDECLTAEPELLDVATDHRAACIRTE LVTGRSAADIYRVKTEARPAALGDASVVVRVRHLVKTYRLAKGVVLRRAIGEVRAVDGISLELRQGRTLGIVGESGSGKS TTLHEILELAAPQSGSIEVLGTDVATLGTAERRSLRRDIQVVFQDPVASLDPRLPVFDLIAEPLQANGFGKNETHARVAE LLDIVGLRHGDASRYPAEFSGGQKQRIGIARALALQPKILALDDPVSALDVSIQAGIINLLLDLQEQFGLSYLFVSHDLS VVKHLAHQVAVMLAGTVVEQGDSEEVFGNPKHEYTRRLLGAVPQPDPA >PDB_8j5s_D Cryo-em structure of mycobacterium tuberculosis oppabcd in the pre- catalytic intermediate state SPLLEVTDLAVTFRTDGDPVTAVRGISYRVEPGEVVAMVGESGSGKSAAAMAVVGLLPEYAQVRGSVRLQGTELLGLADN AMSRFRGKAIGTVFQDPMSALTPVYTVGDQIAEAIEVHQPRVGKKAARRRAVELLDLVGISQPQRRSRAFPHELSGGERQ RVVIAIAIANDPDLLICDDPTTALDVTVQAQILDVLKAARDVTGAGVLIITHDLGVVAEFADRALVMYAGRVVESAGVND LYRDRRMPYTVGLLGSVPRLDAAQGTRLVPIPGAPPSLAGLAPGCPFAPRCPLVIDECLTAEPELLDVATDHRAACIRTE LVTGRSAADIYRVKTEARPAALGDASVVVRVRHLVKTYRLAKGVVLRRAIGEVRAVDGISLELRQGRTLGIVGESGSGKS TTLHEILELAAPQSGSIEVLGTDVATLGTAERRSLRRDIQVVFQDPVASLDPRLPVFDLIAEPLQANGFGKNETHARVAE LLDIVGLRHGDASRYPAEFSGGQKQRIGIARALALQPKILALDDPVSALDVSIQAGIINLLLDLQEQFGLSYLFVSHDLS VVKHLAHQVAVMLAGTVVEQGDSEEVFGNPKHEYTRRLLGAVPQPDPA >ecocyc__YDDP-MONOMER putative D,D-dipeptide ABC transporter ATP-binding subunit DdpD (Escherichia coli K-12 substr. MG1655) MTQPVLDIQQLHLSFPGFNGDVHALNNVSLQINRGEIVGLVGESGSGKSVTAMLIMRLLPTGSYCVHRGQISLLGEDVLNAREKQLRQWRGARVAMIFQEPMTALNPTRRIGLQMMDVIRHHQPISRREARAKAIDLLEEMQIPDAVEVMSRYPFELSGGMRQRVMIALAFSCEPQLIIADEPTTALDVTVQLQVLRLLKHKARASGTAVLFISHDMAVVSQLCDSVYVMYAGSVIESGVTADVIHHPRHPYTIGLLQCAPEHGVPRQLLPAIPGTVPNLTHLPDGCAFRDRCYAAGAQCENVPALTACGDNNQRCACWYPQQEVISV >TCDB__Q9X0F4 TM1064, component of Probable rhamnose oligosaccharide porter. Induced by rhamnose MSTLLQIKNLRTYFFTDEGVVKAVDGVSFEIEEGRTLGVVGESGCGKSVTARSIIKLLSTAGRIVSGEILYNMDGQMVDLVKFSKEEIRKVRGRHIAMIFQEPMAAFSPVYTIGDQITEGMIYHFGITKQEARERAVELLRRVGIPKPEKMIDSYPFEYSGGMRQRAMIAMALSCNPRLLIADEPTTALDVTIQAQVLDLLKDLQQEYKMAIMMITHNMGVVAEMADHVVVMYLGRVVESAPVEELFYNPKHPYTSLLLRSIPVVGKRVERLEVIEGDVPDPRNMPKGCRFHPRCPYMMKGICDEREPVEVEVGPEHRVSCFLYGGEKDGAS >TCDB__F0TFT0 Oligopeptide ABC transporter, component of ABC α-galactoside uptake porter (Lactobacillus acidophilus (strain 30SC)) MEKQSDLLLDIQHLHTAYRLQGKFYDAADDINLTLKRDEILAIVGESGCGKSTIAASIIGLYDHKNTKVTGDILYNELNLVGLNESLFNKIRGDKIGMIFQDPLASLNPLMRVGDQVAETLYYHTDMDEKARHARVIELFNQVGMPKPEEMYAMYPHELSGGLRQRVVIAMAIACKPEIIIADEPTTALDVTIQAQILDLLEDIQKQSHSGIILITHDLGVVAETADEVAVMYAGQIVEKSDVKTIFENPLHPYTRSLLNSMPQTDDSDEDLHVIHGTVPSLKNMPRTGDRFAARIPWIPASAHEENPQVHEVVPGHWVRCTCWKTFHFEGEDETQKAASGE >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__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__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 >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 >BRENDA__A0A150QXP6 5-(carboxyamino)imidazole ribonucleotide mutase (EC 5.4.99.18) (Bacillus anthracis) MAPSPLLSVQDLRVEFITPTGPVCAVDNVSFDIAPGEVLGLAGESGSGKSTVAMAIMRLLRPPAIITGGRVLFAGQDVLSMTEEQLRAFRWRKMALVFQSAMTALNPVLTIGEQIADPIIAHDGVTQAQAMERAAALLKLVNIDPSRLTSYPHQLSGGMRQRVVIAIAMALKPPFLIMDEPTTALDVVVQREILQQIAELKERLGFSILFITHDLSLIAEFSTRIAILYAGKLAETARAKDLFSDPKHPYTQGLLGSFPSVRGPRRRLQGIPGSPPDMRNPPSGCRFHPRCPQAFATCQNELPVLREIAPEHRGACHLY >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__Q9X272 TM1750, component of Probable mannose/mannoside porter. Induced by beta-mannan (Conners et al., 2005). Regulated by mannose-responsive regulator manR MPFDQGGIKMKPLLQTVDLKKYFPQGKRILKAVDGISIEIKEGETLGLVGESGCGKSTLGRTILKLLRPDGGKIFFEGKDITNLNDKEMKPYRKKMQIIFQDPLGSLNPQMTVGRIIEDPLIIHKIGTKKERRKRVEELLDMVGIGREFINSFPHEFSGGQQQRIGIARALALNPKFIVCDEPVSALDVSIQAQIIDLLEEIQQKMGISYLFIAHNLAVVEHISHKVAVMYLGKIVEYGDVDKIFLNPIHPYTRALLKSVPKIPWDGQKQRFYSLKGELPSPIDLPKGCRFQTRCTEKKAICFEKEPELTEVEKNHFVSCHLVRSYRG >ecocyc__YEJF-MONOMER putative oligopeptide ABC transporter ATP binding subunit YejF (EC 7.4.2.6) (Escherichia coli K-12 substr. MG1655) MTQTLLAIENLSVGFRHQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVEYLSGDIRFHGESLLHASDQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQGELNMGMLFITHNLSIVRKLAHRVAVMQNGRCVEQNYAATLFASPTHPYTQKLLNSEPSGDPVPLPEPASTLLDVEQLQVAFPIRKGILKRIVDHNVVVKNISFTLRAGETLGLVGESGSGKSTTGLALLRLINSQGSIIFDGQPLQNLNRRQLLPIRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMHEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILTLLKSLQQKHQLAYLFISHDLHVVRALCHQVIILRQGEVVEQGPCARVFATPQQEYTRQLLALS >BRENDA__Q73NS7 ABC-type dipeptide transporter (EC 7.4.2.9) (Treponema denticola) MENKEVVLDVKNLRLYYHTSAGIVKALDDVSFTLHAGETLGLVGESGCGKTTTGMALLKMPSPPGRVEENSQIIINGRDIVPLSDSEIRKNVRWQEISMVFQGAMNSLTPVYTIGKQMLETLREHKEMSDKEAQDLMEEYLGYVGLPPEVLNRYPHELSGGMKQRVVIASGLFLKPKLVILDEPTTALDVIVQAQIINLLKELKKKFKLSFIFITHDLSLEAEISDRICVMYAGKIAELGTNEQIYGKEPLHPYTQKLLQATPLLRKRVSELSYIPGTPPDLISPPKGCRFNPRCHCTMDKCFEVEPPLIEVEPGHQVACWRCVK >TCDB__Q9F9T4 EppD, component of The Ethylene diamine tetraacetate (EDTA) uptake porter, EppABCD MRPHMSESVHIAGGTGAPLVSVSGLTVSFDRHREEPIEAVRDVSWSIGSGEVLALVGESGSGKSVSALAVMGLLPRNARVAGSIRWRGEELLGASEKRRRALRGSRIGLVPQDPMTSLNPVYTIGAQIREGIRAHQKLSEREMAERTLELLETMGIPHARERMNSYPHELSGGMRQRVVIAMAMANNPDLIIADEATTALDVTVQAQVLDALKKAQALTGAALLLITHDLGVVAGRADRVAVMQRGEVVEQGTVDEIFYQPASSYTRKLLHSIPRLNHTPDLSAPSDVAPDAEVIHSAFERKVGAEGAPILSMRNVGKHFPVYSRGVIRGRVGVIKAVAGVDLDVEAGTTLGIVGESGSGKTTLIRSLFNLEPITHGTILFDGQDVHRMPPRDRRRMRKCVQMVFQDPYASLDPMMTVRDILMEPAVINRMDRKLAERRVMELLERVHLKPEHAARYPNEFSGGQRQRIAIARALMLYPRLLVLDEPVSSLDVSIQAEVLTLLKELQKDLNLSYLFVSHDLSVVAEIAHSVIVMYRGRIVERGRVDELFRNPKHPYTRALLSAVPIPDPRTERRRERIVFNSDTLASPITPVERTGMWRRLFGGRTQEAS >ecocyc__SAPD-MONOMER putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) (Escherichia coli K-12 substr. MG1655) MPLLDIRNLTIEFKTGDEWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVNKDNWRVTADRMRFDDIDLLRLSARERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIVTPRLTGAKNHLYACHFPLNMEKE >TCDB__O30541 AccB, component of Agrocinopine (an opine)/Agrocin 84 (an antibiotic) porter (Agrobacterium radiobacter) MRVALEEPKLSNLLTVRDLIVQVPARDITIINGVSFSLDAGQTLGLVGESGCGKSMTCYAIAKALPRGISQTGGTIELDSGPKADGKPAIAMIYQDPTSSLNPVHSIGYYLESSLYRHQGLEGNDARLEAMRLLERVGIDRAKSRLRSYPHEYSGGMNQRVMIAHALAAKPKLMIADEPTTALDVTTQAQILHLLEELRSETGMALLIVSHDLGVIARLADRAAVMYCGKIVETAPVAELLERAAHPYARALIGCMPTIDADDLEPPVPIPGSVPLLDNLPAGCYYHPRCPRASEQCSVSFPGPVNVGAFHDAACYHPVSP >SwissProt__P36636 Peptide transport system ATP-binding protein SapD (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) MPLLDIRNLTIEFKTSEGWVKAVDRVSMTLSEGEIRGLVGESGSGKSLIAKAICGVAKDNWRVTADRMRFDDIDLLRLSSRERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPAWTYKGRWWQRLGWRKRRAIELLHRVGIKDHKDAMRSFPYELTDGECQKVMIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLTRLNQNSNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKDLVTMPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEQLPIGCRLGPRCPYAQRECIITPRLTGAKNHLYACHFPLNMERE >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_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 >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__4u00A Crystal structure of ttha1159 in complex with adp PIIRIRNLHKWFGPLHVLKGIHLEVAPGEKLVIIGPSGSGKSTLIRTINRLEDFQEGEVVVDGLSVKDDRALREIRREVGMVFQQFNLFPHMTVLENVTLAPMRVRRWPREKAEKKALELLERVGILDQARKYPAQLSGGQQQRVAIARALAMEPKIMLFDEPTSALDPEMVGEVLDVMRDLAQGGMTMVVVTHEMGFAREVADRVVFMDGGQIVEEGRPEEIFTRPKEERTRSFLQRVLH >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__6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein HMIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDQATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNAIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV >PDB_7ahh_C Opua inhibited inward-facing, sbd docked VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTS GKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYP KQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGK IMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAA RKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD >biolip__7aheC Opua inhibited inward facing VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTSGKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYPKQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGKIMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAARKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD >biolip__1f3oA Crystal structure of mj0796 atp-binding cassette MIKLKNVTKTYKMGEEIIYALKNVNLNIKEGEFVSIMGPSGSGKSTMLNIIGCLDKPTEGEVYIDNIKTNDLDDDELTKIRRDKIGFVFQQFNLIPLLTALENVELPLIFKYRGAMSGEERRKRALECLKMAELEERFANHKPNQLSGGQQQRVAIARALANNPPIILADEPTGALDSKTGEKIMQLLKKLNEEDGKTVVVVTHDINVARFGERIIYLKDGEVEREEKLRGF >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 >PDB_1l2t_A Dimeric structure of mj0796, a bacterial abc transporter cassette MIKLKNVTKTYKMGEEIIYALKNVNLNIKEGEFVSIMGPSGSGKSTMLNIIGCLDKPTEGEVYIDNIKTNDLDDDELTKI RRDKIGFVFQQFNLIPLLTALENVELPLIFKYRGAMSGEERRKRALECLKMAELEERFANHKPNQLSGGQQQRVAIARAL ANNPPIILADQPTGALDSKTGEKIMQLLKKLNEEDGKTVVVVTHDINVARFGERIIYLKDGEVEREEKLR >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__5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) MNIIEIKQLNRYFGEGENRVHVLKDISLSIERGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSSKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQSQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADQPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKRQVKSAVKNPSVFSKDQLMEAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFQNLKISDANTLSKQSYIQSVTPNTSSSGILVVGNKSFTSANLYGIGEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFANENPLGKTVIFNKRPFRVIGVVSDQSLNLYSPYSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKSLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALA >biolip__8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii TFVEIDHVDRIFDLPNGGRYIALKNIELKIKQGEFVSLIGHSGCGKSTLLNIIAGLDRASIGGVTLEGREIREPSPDRMVVFQNYSLLPWLTVRENVALAVDEVYQGKSKGERRAIIEEHIDMVGLRLAANKRPSELSGGMKQRVAIARALATRPKLLLLDEPFGALDALTRGSLQEQLMKICNEHQITCVMVTHDVDEALLLSDRVVMLTNGPEAHIGQILEVPISRPRQRLEVVKHPSYYNLRNEIIYFLNQQKLAKKRQTQQASAPLGTAKAVIEIGFMPLTDSAPLIVAKEKGFFAKYGLDNVILNRANNWQAIATGVVTGKLDAAQMVAGMPIALTLGAGSQTPTPVINALNLSRNANAITFSKRLYNQGVRSLADLKAVIDSSPDQILTLGVVHSASMQNLILRYWLAAGGIDPDRDVSLTVIPPTQMVSQLKAGNIDGYCAGEPWNYQAVHDDLGFVAATALEIWSGQPKKVLGVREDWAQKYPETYLNLVKALIEACKYCDDLRNREEILEILCRPEYLDVNPAYVRSGFIDPYDRGDGTPPQQLTAYNQFYLNKTNYPNRTEILWMITQMARWGLTPFPKNWVEITERVCRTDIFGAAARDLGLLDIGEDDPIHLFDGKLFNPSEPIEYLKSLEIRRQIRIEEVFISSG >ecocyc__FHUC-MONOMER iron(III) hydroxamate ABC transporter ATP binding subunit (EC 7.2.2.16) (Escherichia coli K-12 substr. MG1655) MQEYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLSLVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGILPHPAGAAPVSFVY >biolip__5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) MNIIEIKQLNRYFGEGENRVHVLKDISLSIERGDFVAIMGQSGSGKSTLMNIIGCLDTATGGSSKIDGKETIELTNDQLSDLRSQKFGFIFQRYNLLSSLTAAENVALPAIYAGMPQSQRLERAKQLLEKLGLGDKWQNKPNQLSGGQQQRVSIARALMNGGEIILADQPTGALDSHSGENVMEILRQLHEEGHTIIMVTHDKHIAASANRIIEIKDGEIISDTQKRQVKSAVKNPSVFSKDQLMEAFRMSVSAIVAHKMRSLLTMLGIIIGITSVVSVVALGNGSQQKILENIRGIGTNTMTIFQNLKISDANTLSKQSYIQSVTPNTANLYGIGEQYFDVEGLKLKQGRLLTEDDVDQSNQVVVLDESAKKAIFVIFNKRPFRVIGVVSDQSLNLYSPYSTVLNKITGGSRIGSITVKISDDVNSTVAEKSLTELLKSLHGKKDFFIMNSDTIKQTIENTTGTMKLLISSIAFISLIVGGIGVMNIMLVSVTERTKEIGVRMAIGARQINILQQFLIEAVLICLIGGVAGILLSVLIGVLFNSFITDFSMDFSTASIVTAVLFSTLIGVLFGYMPAKKAAELNPITALAQ >PDB_8w9m_C Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp TFVEIDHVDRIFDLPNGGRYIALKNIELKIKQGEFVSLIGHSGCGKSTLLNIIAGLDRASIGGVTLEGREIREPSPDRMV VFQNYSLLPWLTVRENVALAVDEVYQGKSKGERRAIIEEHIDMVGLRLAANKRPSELSGGMKQRVAIARALATRPKLLLL DQPFGALDALTRGSLQEQLMKICNEHQITCVMVTHDVDEALLLSDRVVMLTNGPEAHIGQILEVPISRPRQRLEVVKHPS YYNLRNEIIYFLNQQK >biolip__5ws4A Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii KQALLEVSNLVREFPAGESTIQILKGIDLTIYEGELVAIVGQSGSGKSTLMNILGCLDRPTSGSYKVNGQETGKLEPDQLAQLRREYFGFIFQRYHLLGDLSAEGNVEVPAVYAGVTPADRKQRATALLTELGLGTKTQNRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDSHSGVEVMRILRELNAAGHTIILVTHDMQVAKNATRIIEISDGEIISDRPNVPDQSLEEVKSDPDAAPAAWRSTLDRLSEAFQMALLSMNAHRMRTFLTMLGIIIGIASVVTVVALGNGSQQQILSNISSLGTNTITVFQGRGFGDNSKTANFKTLVPADADALMTQPYVSAVSPMVSTSKTMRYQQNEANATINGVSNDYFDVKGLVFKDGQTFDQRSVRDRSQDVVIDTNTQKQFFSDGTNPIGQVVLLGSVPARIIGIVEPQTSGMGSDDTLNVYMPYTTVMSRMLGQAHVRNIVVRINDKYSTSAAENAIVNLLTQRHGAQDIFTMNSDSIRQTIEKTTSTMTLLVSAIAVISLVVGGIGVMNIMLVSVTERTQEIGVRMAVGARQSDILQQFLIEAILVCLIGGVLGVLLSLGLGQLINKFAGGNFAVAYSTTSIVAAFVCSTLIGVVFGFLPAKNAAKLDPVAALSRE >PDB_8hpr_C Lpqy-sugabc in state 4 AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH FTTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD >biolip__8hplC Lpqy-sugabc in state 1 AEIVLDRVTKSYPRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQPLSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMNFFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVHFTTEGAGAESAQLAELAADSGAGTNQFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD >PDB_8hpr_D Lpqy-sugabc in state 4 AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH FTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD >PDB_7d0a_B Acinetobacter mlafedb complex in adp-vanadate trapped vclose conformation TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAAR ARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPD LIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFL TGSAEGPVEYQFSHQAYLDNEVR >biolip__7d08B Acinetobacter mlafedb complex in atp-bound vtrans1 conformation TQSLIEVKNLSFNRGERVIYDNISLNIRRGQITAIMGPSGTGKTTLLRLIGGQLVPDQGEVLLDGKDIAQMSRQELFAARARMGMLFQSGALFTDMSVYENVAFPIRAHTKLSENLIAELVALKLESVGLRGTEQLMPTELSGGMNRRVALARAIALDPDLIMYDEPFAGQDPIVKGVLTRLIRSLREALDLTTIIVSHDVPETLSIADYIYVVAEGKIQGEGTPEELQAYASPFVKQFLTGSAEGPVEYQFSHQAYLDNEVR