LMRA_LACLM
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 03-AUG-2022, entry version 142.
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; Firmicutes; 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}.
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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 EnsemblBacteria; CAL98427; CAL98427; llmg_1856.
DR KEGG; llm:llmg_1856; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_9; -.
DR OMA; ERQRMTI; -.
DR PhylomeDB; P97046; -.
DR BRENDA; 7.6.2.2; 2903.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 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; Translocase; Transmembrane; Transmembrane helix;
KW 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
