ID LMRA_LACLM Reviewed; 590 AA. AC P97046; A2RMA0; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2003, sequence version 3. DT 04-NOV-2026, entry version 153. DE RecName: Full=Multidrug resistance ABC transporter ATP-binding and permease protein; DE EC=7.6.2.2; GN Name=lmrA; OrderedLocusNames=llmg_1856; OS Lactococcus lactis subsp. cremoris (strain MG1363). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus; Lactococcus cremoris subsp. cremoris. OX NCBI_TaxID=416870; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8855237; DOI=10.1073/pnas.93.20.10668; RA van Veen H.W., Venema K., Bolhuis H., Oussenko I., Kok J., Poolman B., RA Driessen A.J., Konings W.N.; RT "Multidrug resistance mediated by a bacterial homolog of the human RT multidrug transporter MDR1."; RL Proc. Natl. Acad. Sci. U.S.A. 93:10668-10672(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MG1363; RX PubMed=17307855; DOI=10.1128/jb.01768-06; RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., RA van Sinderen D., Kok J.; RT "The complete genome sequence of the lactic acid bacterial paradigm RT Lactococcus lactis subsp. cremoris MG1363."; RL J. Bacteriol. 189:3256-3270(2007). CC -!- FUNCTION: Efflux transporter for a variety of amphiphilic cationic CC compounds, including antibiotics. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + CC xenobioticSide 2.; EC=7.6.2.2; CC -!- SUBUNIT: Homodimer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Multidrug CC exporter LmrA (TC 3.A.1.117.1) family. {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; U63741; AAB49750.1; -; Genomic_DNA. DR EMBL; AM406671; CAL98427.1; -; Genomic_DNA. DR AlphaFoldDB; P97046; -. DR BMRB; P97046; -. DR SMR; P97046; -. DR STRING; 416870.llmg_1856; -. DR TCDB; 3.A.1.117.1; the atp-binding cassette (abc) superfamily. DR PaxDb; 416870-llmg_1856; -. DR KEGG; llm:llmg_1856; -. DR eggNOG; COG1132; Bacteria. DR HOGENOM; CLU_000604_84_3_9; -. DR OMA; AAAVIWY; -. DR PhylomeDB; P97046; -. DR BRENDA; 7.6.2.2; 2903. DR Proteomes; UP000000364; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; IEA:TreeGrafter. DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR CDD; cd18551; ABC_6TM_LmrA_like; 1. DR FunFam; 3.40.50.300:FF:000218; 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 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 Antibiotic resistance; ATP-binding; Cell membrane; Membrane; KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..590 FT /note="Multidrug resistance ABC transporter ATP-binding and FT permease protein" FT /id="PRO_0000092414" FT TRANSMEM 35..55 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 150..170 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 176..196 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 261..281 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 292..312 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 38..317 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 349..584 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 382..389 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" SQ SEQUENCE 590 AA; 64617 MW; CCE4E7D4EF912B8D CRC64; MERGPQMANR IEGKAVDKTS IKHFVKLIRA AKPRYLFFVI GIVAGIIGTL IQLQVPKMVQ PLINSFGHGV NGGKVALVIA LYIGSAAVSA IAAIVLGIFG ESVVKNLRTR VWDKMIHLPV KYFDEVKTGE MSSRLANDTT QVKNLIANSI PQAFTSILLL VGSIIFMLQM QWRLTLAMII AVPIVMLIMF PIMTFGQKIG WTRQDSLANF QGIASESLSE IRLVKSSNAE KQASKKAEND VNALYKIGVK EAVFDGLMSP VMMLSMMLMI FGLLAYGIYL ISTGVMSLGT LLGMMMYLMN LIGVVPTVAT FFTELAKASG STGRLTELLD EEQEVLHQGD SLDLEGKTLS AHHVDFAYDD SEQILHDISF EAQPNSIIAF AGPSGGGKST IFSLLERFYQ PTAGEITIGG QPIDSVSLEN WRSQIGFVSQ DSAIMAGTIR ENLTYGLEGN FTDEDLWQVL DLAFARSFVE NMPDQLNTEV GERGVKISGG QRQRLAIARA FLRNPKILML DEATASLDSE SESMVQRALD SLMKGRTTLV IAHRLSTIVD ADKIYFIEKG EITGSGKHNE LVATHPLYAK YVSEQLTVGQ //