ID MDLA_ECOLI Reviewed; 590 AA. AC P77265; P30751; Q2MBX8; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 190. DE RecName: Full=Multidrug resistance-like ATP-binding protein MdlA; DE EC=7.6.2.2; GN Name=mdlA; Synonyms=mdl; OrderedLocusNames=b0448, JW0438; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=TAP90 / ATCC 47037; RX PubMed=7904973; DOI=10.1016/0378-1119(93)90470-n; RA Allikmets R., Gerrard B.C., Court D., Dean M.C.; RT "Cloning and organization of the abc and mdl genes of Escherichia coli: RT relationship to eukaryotic multidrug resistance."; RL Gene 136:231-236(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + CC xenobioticSide 2.; EC=7.6.2.2; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15919996}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Drug exporter-2 CC (TC 3.A.1.117) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC36870.1; Type=Frameshift; Note=Fuses together mdlA and mdlB.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L08627; AAC36870.1; ALT_FRAME; Unassigned_DNA. DR EMBL; U82664; AAB40204.1; -; Genomic_DNA. DR EMBL; U00096; AAC73551.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76228.1; -; Genomic_DNA. DR PIR; H64774; H64774. DR RefSeq; NP_414982.1; NC_000913.3. DR RefSeq; WP_001235649.1; NZ_CP009789.1. DR AlphaFoldDB; P77265; -. DR SMR; P77265; -. DR BioGRID; 4261677; 158. DR DIP; DIP-10173N; -. DR FunCoup; P77265; 298. DR IntAct; P77265; 1. DR STRING; 511145.b0448; -. DR TCDB; 3.A.1.106.13; the atp-binding cassette (abc) superfamily. DR PaxDb; 511145-b0448; -. DR EnsemblBacteria; AAC73551; AAC73551; b0448. DR GeneID; 945092; -. DR KEGG; ecj:JW0438; -. DR KEGG; eco:b0448; -. DR KEGG; ecoc:C3026_02195; -. DR PATRIC; fig|1411691.4.peg.1828; -. DR EchoBASE; EB1579; -. DR eggNOG; COG1132; Bacteria. DR HOGENOM; CLU_000604_84_6_6; -. DR InParanoid; P77265; -. DR OMA; CRLYEPQ; -. DR OrthoDB; 9806127at2; -. DR PhylomeDB; P77265; -. DR BioCyc; EcoCyc:MDLA-MONOMER; -. DR PRO; PR:P77265; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016020; C:membrane; ISM:EcoCyc. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0046618; P:xenobiotic export from cell; IC:EcoCyc. DR CDD; cd18541; ABC_6TM_TmrB_like; 1. DR FunFam; 1.20.1560.10:FF:000011; Multidrug ABC transporter ATP-binding protein; 1. DR FunFam; 3.40.50.300:FF:000221; Multidrug ABC transporter ATP-binding protein; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039421; Type_1_exporter. DR NCBIfam; NF008055; PRK10789.1; 1. DR PANTHER; PTHR43394:SF1; ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10, MITOCHONDRIAL; 1. DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Membrane; KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..590 FT /note="Multidrug resistance-like ATP-binding protein MdlA" FT /id="PRO_0000092492" FT TRANSMEM 23..43 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 53..73 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 134..154 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 155..175 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 280..300 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 18..303 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 337..570 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 369..376 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT CONFLICT 145 FT /note="G -> A (in Ref. 1; AAC36870)" FT /evidence="ECO:0000305" FT CONFLICT 234..235 FT /note="NM -> KL (in Ref. 1; AAC36870)" FT /evidence="ECO:0000305" FT CONFLICT 318 FT /note="A -> R (in Ref. 1; AAC36870)" FT /evidence="ECO:0000305" FT CONFLICT 371 FT /note="T -> N (in Ref. 1; AAC36870)" FT /evidence="ECO:0000305" FT CONFLICT 390 FT /note="E -> P (in Ref. 1; AAC36870)" FT /evidence="ECO:0000305" FT CONFLICT 410..411 FT /note="SR -> TG (in Ref. 1; AAC36870)" FT /evidence="ECO:0000305" SQ SEQUENCE 590 AA; 66017 MW; AD1CEBE41030200D CRC64; MRLFAQLSWY FRREWRRYLG AVALLVIIAM LQLVPPKVVG IVVDGVTEQH FTTGQILMWI ATMVLIAVVV YLLRYVWRVL LFGASYQLAV ELREDYYRQL SRQHPEFYLR HRTGDLMARA TNDVDRVVFA AGEGVLTLVD SLVMGCAVLI MMSTQISWQL TLFSLLPMPV MAIMIKRNGD ALHERFKLAQ AAFSSLNDRT QESLTSIRMI KAFGLEDRQS ALFAADAEDT GKKNMRVARI DARFDPTIYI AIGMANLLAI GGGSWMVVQG SLTLGQLTSF MMYLGLMIWP MLALAWMFNI VERGSAAYSR IRAMLAEAPV VNDGSEPVPE GRGELDVNIH QFTYPQTDHP ALENVNFALK PGQMLGICGP TGSGKSTLLS LIQRHFDVSE GDIRFHDIPL TKLQLDSWRS RLAVVSQTPF LFSDTVANNI ALGCPNATQQ EIEHVARLAS VHDDILRLPQ GYDTEVGERG VMLSGGQKQR ISIARALLVN AEILILDDAL SAVDGRTEHQ ILHNLRQWGQ GRTVIISAHR LSALTEASEI IVMQHGHIAQ RGNHDVLAQQ SGWYRDMYRY QQLEAALDDA PENREEAVDA //